Accepted name: purine-nucleoside phosphorylase
Reaction: (1) purine ribonucleoside + phosphate = purine + α-D-ribose 1-phosphate
(2) purine 2'-deoxyribonucleoside + phosphate = purine + 2-deoxy-α-D-ribose 1-phosphate
Other name(s): inosine phosphorylase; PNPase (ambiguous); PUNPI; PUNPII; inosine-guanosine phosphorylase; purine deoxynucleoside phosphorylase; purine deoxyribonucleoside phosphorylase; purine nucleoside phosphorylase; purine ribonucleoside phosphorylase
Systematic name: purine-nucleoside:phosphate ribosyltransferase
Comments: Specificity not completely determined. Can also catalyse ribosyltransferase reactions of the type catalysed by EC 2.4.2.5, nucleoside ribosyltransferase.
Links to other databases: BRENDA, EXPASY, GTD, KEGG, Metacyc, PDB, CAS registry number: 9030-21-1
References:
1. Agarwal, R.P. and Parks, R.E. Purine nucleoside phosphorylase from human erythrocytes. IV. Crystallization and some properties. J. Biol. Chem. 244 (1969) 644-647. [PMID: 69183117]
2. Friedkin, M. and Kalckar, H. Nucleoside phosphorylases. In: Boyer, P.D., Lardy, H. and Myrbäck, K. (Eds.), The Enzymes, 2nd edn., vol. 5, Academic Press, New York, 1961, p. 237-255.
3. Heppel, L.A. and Hilmoe, R.J. Phosphorolysis and hydrolysis of purine ribosides from yeast. J. Biol. Chem. 198 (1952) 683-694.
4. Kalckar, H.M. The enzymatic synthesis of purine ribosides. J. Biol. Chem. 167 (1947) 477-486.
5. Saunders, P.P., Wilson, B.A. and Saunders, G.F. Purification and comparative properties of a pyrimidine nucleoside phosphorylase from Bacillus stearothermophilus. J. Biol. Chem. 244 (1969) 3691-3697. [PMID: 4978445].
6. Tsuboi, K.K. and Hudson, P.B. Enzymes of the human erythrocyte. I. Purine nucleoside phosphorylase; isolation procedure. J. Biol. Chem. 224 (1957) 879-887.
Accepted name: pyrimidine-nucleoside phosphorylase
Reaction: (1) uridine + phosphate = uracil + α-D-ribose 1-phosphate
(2) cytidine + phosphate = cytosine + α-D-ribose 1-phosphate
(3) 2'-deoxyuridine + phosphate = uracil + 2-deoxy-α-D-ribose 1-phosphate
(4) thymidine + phosphate = thymine + 2-deoxy-α-D-ribose 1-phosphate
Other name(s): Py-NPase; pdp (gene name)
Systematic name: pyrimidine-nucleoside:phosphate (2'-deoxy)-α-D-ribosyltransferase
Comments: Unlike EC 2.4.2.3, uridine phosphorylase, and EC 2.4.2.4, thymidine phosphorylase, this enzyme can accept both the ribonucleosides uridine and cytidine and the 2'-deoxyribonucleosides 2'-deoxyuridine and thymidine [3,6]. The reaction is reversible, and the enzyme does not distinguish between α-D-ribose 1-phosphate and 2-deoxy-α-D-ribose 1-phosphate in the synthetic direction.
Links to other databases: BRENDA, EXPASY, GTD, KEGG, MetaCyc, PDB, CAS registry number: 9055-35-0
References:
1. Friedkin, M. and Kalckar, H. Nucleoside phosphorylases. In: Boyer, P.D., Lardy, H. and Myrbäck, K. (Ed.), The Enzymes, 2nd edn, vol. 5, Academic Press, New York, 1961, pp. 237-255.
2. Saunders, P.P., Wilson, B.A. and Saunders, G.F. Purification and comparative properties of a pyrimidine nucleoside phosphorylase from Bacillus stearothermophilus. J. Biol. Chem. 244 (1969) 3691-3697. [PMID: 4978445]
3. Hamamoto, T., Noguchi, T. and Midorikawa, Y. Purification and characterization of purine nucleoside phosphorylase and pyrimidine nucleoside phosphorylase from Bacillus stearothermophilus TH 6-2. Biosci. Biotechnol. Biochem. 60 (1996) 1179-1180. [PMID: 8782414]
4. Okuyama, K., Hamamoto, T., Noguchi, T. and Midorikawa, Y. Molecular cloning and expression of the pyrimidine nucleoside phosphorylase gene from Bacillus stearothermophilus TH 6-2. Biosci. Biotechnol. Biochem. 60 (1996) 1655-1659. [PMID: 8987664]
5. Pugmire, M.J. and Ealick, S.E. The crystal structure of pyrimidine nucleoside phosphorylase in a closed conformation. Structure 6 (1998) 1467-1479. [PMID: 9817849]
6. Wei, X.K., Ding, Q.B., Zhang, L., Guo, Y.L., Ou, L. and Wang, C.L. Induction of nucleoside phosphorylase in Enterobacter aerogenes and enzymatic synthesis of adenine arabinoside. J Zhejiang Univ Sci B 9 (2008) 520-526. [PMID: 18600781]
EC 2.4.2.3
Accepted name: uridine phosphorylase
Reaction: uridine + phosphate = uracil + α-D-ribose 1-phosphate
Other name(s): pyrimidine phosphorylase; UrdPase; UPH; UPase
Systematic name: uridine:phosphate α-D-ribosyltransferase
Comments: The enzyme participates the the pathways of pyrimidine ribonucleosides degradation and salvage. The mammalian enzyme also accepts 2'-deoxyuridine.
Links to other databases:
BRENDA,
EXPASY,
GTD,
KEGG,
Metacyc,
PDB,
CAS registry number: 9030-22-2
References:
1. Canellakis, E.S. Pyrimidine metabolism. II. Enzymatic pathways of uracil anabolism. J. Biol. Chem. 227 (1957) 329-338.
2. Paege, L.M. and Schlenk, F. Bacterial uracil riboside phosphorylase. Arch. Biochem. Biophys. 40 (1952) 42-49.
3. Pontis, H., Degerstedt, G. and Reichard, P. Uridine and deoxyuridine phosphorylases from Ehrlich ascites tumor. Biochim. Biophys. Acta 51 (1961) 138-147.
4. Pontis, H., Degerstedt, G. and Reichard, P. Uridine and deoxyuridine phosphorylases from Ehrlich ascites tumor. Biochim. Biophys. Acta 51 (1961) 138-147. [PMID: 13737038]
5. Watanabe, S. and Uchida, T. Cloning and expression of human uridine phosphorylase. Biochem. Biophys. Res. Commun. 216 (1995) 265-272. [PMID: 7488099]
6. Liu, M., Cao, D., Russell, R., Handschumacher, R.E. and Pizzorno, G. Expression, characterization, and detection of human uridine phosphorylase and identification of variant uridine phosphorolytic activity in selected human tumors. Cancer Res. 58 (1998) 5418-5424. [PMID: 9850074]
Accepted name: thymidine phosphorylase
Reaction: thymidine + phosphate = thymine + 2-deoxy-α-D-ribose 1-phosphate
Other name(s): pyrimidine phosphorylase; thymidine-orthophosphate deoxyribosyltransferase; animal growth regulators, blood platelet-derived endothelial cell growth factors; blood platelet-derived endothelial cell growth factor; deoxythymidine phosphorylase; gliostatins; pyrimidine deoxynucleoside phosphorylase; thymidine:phosphate deoxy-D-ribosyltransferase
Systematic name: thymidine:phosphate deoxy-α-D-ribosyltransferase
Comments: The enzyme in some tissues also catalyses deoxyribosyltransferase reactions of the type catalysed by EC 2.4.2.6, nucleoside deoxyribosyltransferase.
Links to other databases:
BRENDA,
EXPASY,
KEGG,
Metacyc,
PDB,
CAS registry number: 9030-23-3
References:
1. Friedkin, M. and Roberts, D. The enzymatic synthesis of nucleosides. I. Thymidine phosphorylase in mammalian tissue. J. Biol. Chem. 207 (1954) 245-256.
2. Zimmerman, M. and Seidenberg, J. Deoxyribosyl transfer. I. Thymidine phosphorylase and nucleoside deoxyribosyltransferase in normal and malignant tissues. J. Biol. Chem. 239 (1964) 2618-2621.
3. Zimmerman, M. Deoxyribosyl transfer. II. Nucleoside:pyrimidine deoxyribosyltransferase activity of three partially purified thymidine phosphorylases. J. Biol. Chem. 239 (1964) 2622-2627.
Accepted name: nucleoside ribosyltransferase
Reaction: D-ribosyl-base1 + base2 = D-ribosyl-base2 + base1
Other name(s): nucleoside N-ribosyltransferase
Systematic name: nucleoside:purine(pyrimidine) D-ribosyltransferase
Comments: Base1 and base2 represent various purines and pyrimidines.
Links to other databases:
BRENDA,
EXPASY,
KEGG,
Metacyc,
CAS registry number: 9030-31-3
References:
1. Koch, A.L. Some enzymes of nucleoside metabolism of Escherichia coli. J. Biol. Chem. 223 (1956) 535-549.
Accepted name: nucleoside deoxyribosyltransferase
Reaction: 2-deoxy-D-ribosyl-base1 + base2 = 2-deoxy-D-ribosyl-base2 + base1
Other name(s): purine(pyrimidine) nucleoside:purine(pyrimidine) deoxyribosyl transferase; deoxyribose transferase; nucleoside trans-N-deoxyribosylase; trans-deoxyribosylase; trans-N-deoxyribosylase; trans-N-glycosidase; nucleoside deoxyribosyltransferase I (purine nucleoside:purine deoxyribosyltransferase: strictly specific for transfer between purine bases); nucleoside deoxyribosyltransferase II [purine(pyrimidine) nucleoside:purine(pyrimidine) deoxyribosyltransferase]
Systematic name: nucleoside:purine(pyrimidine) deoxy-D-ribosyltransferase
Comments: Base1 and base2 represent various purines and pyrimidines.
Links to other databases:
BRENDA,
EXPASY,
GTD,
KEGG,
Metacyc,
PDB,
CAS registry number: 9026-86-2
References:
1. Kalckar, H.M., MacNutt, W.S. and Hoff-Jørgensen, E. Trans-N-glycosidase studied with radioactive adenine. Biochem. J. 50 (1952) 397-400.
2. MacNutt, W.S. The enzymically catalysed transfer of the deoxyribosyl group from one purine or pyrimidine to another. Biochem. J. 50 (1952) 384-397.
3. Roush, A.H. and Betz, R.F. Purification and properties of trans-N-deoxyribosylase. J. Biol. Chem. 233 (1958) 261-266.
Accepted name: adenine phosphoribosyltransferase
Reaction: AMP + diphosphate = adenine + 5-phospho-α-D-ribose 1-diphosphate
For diagram of reaction click here.
Other name(s): AMP pyrophosphorylase; transphosphoribosidase; APRT; AMP-pyrophosphate phosphoribosyltransferase; adenine phosphoribosylpyrophosphate transferase; adenosine phosphoribosyltransferase; adenylate pyrophosphorylase; adenylic pyrophosphorylase
Systematic name: AMP:diphosphate phospho-D-ribosyltransferase
Comments: 5-Amino-4-imidazolecarboxamide can replace adenine.
Links to other databases:
BRENDA,
EXPASY,
GTD,
KEGG,
Metacyc,
PDB,
CAS registry number: 9027-80-9
References:
1. Flaks, J.G., Erwin, M.J. and Buchanan, J.M. Biosynthesis of the purines. XVI. The synthesis of adenosine 5'-phosphate and 5-amino-4-imidazolecarboxamide ribotide by a nucleotide pyrophosphorylase. J. Biol. Chem. 228 (1957) 201-213.
2. Kornberg, A., Lieberman, I. and Simms, E.S. Enzymatic synthesis of purine nucleotides. J. Biol. Chem. 215 (1955) 417-427.
3. Lukens, L.N. and Herrington, K.A. Enzymic formation of 6-mercaptopurine ribotide. Biochim. Biophys. Acta 24 (1957) 432-433.
Accepted name: hypoxanthine phosphoribosyltransferase
Reaction: IMP + diphosphate = hypoxanthine + 5-phospho-α-D-ribose 1-diphosphate
Other name(s): IMP pyrophosphorylase; transphosphoribosidase; hypoxanthine—guanine phosphoribosyltransferase; guanine phosphoribosyltransferase; GPRT; HPRT; guanosine 5'-phosphate pyrophosphorylase; IMP-GMP pyrophosphorylase; HGPRTase; 6-hydroxypurine phosphoribosyltransferase; 6-mercaptopurine phosphoribosyltransferase; GMP pyrophosphorylase; guanine-hypoxanthine phosphoribosyltransferase; guanosine phosphoribosyltransferase; guanylate pyrophosphorylase; guanylic pyrophosphorylase; inosinate pyrophosphorylase; inosine 5'-phosphate pyrophosphorylase; inosinic acid pyrophosphorylase; inosinic pyrophosphorylase; 6-mercaptopurine phosphoribosyltransferase; purine-6-thiol phosphoribosyltransferase
Systematic name: IMP:diphosphate phospho-D-ribosyltransferase
Comments: Guanine and purine-6-thiol can replace hypoxanthine.
Links to other databases:
BRENDA,
EXPASY,
GTD,
KEGG,
Metacyc,
PDB,
CAS registry number: 9016-12-0
References:
1. Flaks, J.G. Nucleotide synthesis from 5-phosphoribosylpyrophosphate. Methods Enzymol. 6 (1963) 136-158.
2. Kornberg, A., Lieberman, I. and Simms, E.S. Enzymatic synthesis of purine nucleotides. J. Biol. Chem. 215 (1955) 417-427.
3. Lukens, L.N. and Herrington, K.A. Enzymic formation of 6-mercaptopurine ribotide. Biochim. Biophys. Acta 24 (1957) 432-433.
4. Remy, C.N., Remy, W.T. and Buchanan, J.M. Biosynthesis of the purines. VIII. Enzymatic synthesis and utilization of α-5-phosphoribosylpyrophosphate. J. Biol. Chem. 217 (1955) 885-895.
Accepted name: uracil phosphoribosyltransferase
Reaction: UMP + diphosphate = uracil + 5-phospho-α-D-ribose 1-diphosphate
Other name(s): UMP pyrophosphorylase; UPRTase; UMP:pyrophosphate phosphoribosyltransferase; uridine 5'-phosphate pyrophosphorylase; uridine monophosphate pyrophosphorylase; uridylate pyrophosphorylase; uridylic pyrophosphorylase
Systematic name: UMP:diphosphate phospho-α-D-ribosyltransferase
Links to other databases:
BRENDA,
EXPASY,
KEGG,
Metacyc,
PDB,
CAS registry number: 9030-24-4
References:
1. Crawford, I., Kornberg, A. and Simms, E.S. Conversion of uracil and orotate to uridine 5'-phosphate by enzymes in lactobacilli. J. Biol. Chem. 226 (1967) 1093-1101.
2. Flaks, J.G. Nucleotide synthesis from 5-phosphoribosylpyrophosphate. Methods Enzymol. 6 (1963) 136-158.
Accepted name: orotate phosphoribosyltransferase
Reaction: orotidine 5'-phosphate + diphosphate = orotate + 5-phospho-α-D-ribose 1-diphosphate
For diagram click here.
Other name(s): orotidylic acid phosphorylase; orotidine-5'-phosphate pyrophosphorylase; OPRTase; orotate phosphoribosyl pyrophosphate transferase; orotic acid phosphoribosyltransferase; orotidine 5'-monophosphate pyrophosphorylase; orotidine monophosphate pyrophosphorylase; orotidine phosphoribosyltransferase; orotidylate phosphoribosyltransferase; orotidylate pyrophosphorylase; orotidylic acid pyrophosphorylase; orotidylic phosphorylase; orotidylic pyrophosphorylase
Systematic name: orotidine-5'-phosphate:diphosphate phospho-α-D-ribosyl-transferase
Comments: The enzyme from higher eukaryotes also catalyses the reaction listed as EC 4.1.1.23, orotidine-5'-phosphate decarboxylase.
Links to other databases:
BRENDA,
EXPASY,
GTD,
KEGG,
Metacyc,
PDB,
CAS registry number: 9030-25-5
References:
1. Jones, M.E., Kavipurapu, P.R. and Traut, T.W. Orotate phosphoribosyltransferase: orotidylate decarboxylase (Ehrlich ascites cell). Methods Enzymol. 51 (1978) 155-167. [PMID: 692383]
2. Lieberman, I., Kornberg, A. and Simms, E.S. Enzymatic synthesis of pyrimidine nucleotides. Orotidine-5'-phosphate and uridine-5'-phosphate. J. Biol. Chem. 215 (1955) 403-415.
3. McClard, R.W., Black, M.J., Livingstone, L.R. and Jones, M.E. Isolation and initial characterization of the single polypeptide that synthesizes uridine 5'-monophosphate from orotate in Ehrlich ascites carcinoma. Purification by tandem affinity chromatography of uridine-5'-monophosphate synthase. Biochemistry 19 (1980) 4699-4706. [PMID: 6893554]
[EC 2.4.2.11 Transferred entry: EC 2.4.2.11, nicotinate phosphoribosyltransferase. Now EC 6.3.4.21 nicotinate phosphoribosyltransferase. (EC 2.4.2.11 created 1961, deleted 2013)]
Accepted name: nicotinamide phosphoribosyltransferase
Reaction: nicotinamide D-ribonucleotide + diphosphate = nicotinamide + 5-phospho-α-D-ribose 1-diphosphate
For diagram of reaction click here.
Other name(s): NMN pyrophosphorylase; nicotinamide mononucleotide pyrophosphorylase; nicotinamide mononucleotide synthetase; NMN synthetase; nicotinamide-nucleotide:diphosphate phospho-α-D-ribosyltransferase
Systematic name: nicotinamide-D-ribonucleotide:diphosphate phospho-α-D-ribosyltransferase
Links to other databases:
BRENDA,
EXPASY,
KEGG,
Metacyc,
PDB,
CAS registry number: 9030-27-7
References:
1. Preiss, J. and Handler, P. Enzymatic synthesis of nicotinamide mononucleotide. J. Biol. Chem. 225 (1957) 759-770.
[EC 2.4.2.13 Transferred entry: now EC 2.5.1.6 methionine adenosyltransferase (EC 2.4.2.13 created 1961, deleted 1965)]
Accepted name: amidophosphoribosyltransferase
Reaction: 5-phospho-β-D-ribosylamine + diphosphate + L-glutamate = L-glutamine + 5-phospho-α-D-ribose 1-diphosphate + H2O
For diagram click here.
Other name(s): phosphoribosyldiphosphate 5-amidotransferase; glutamine phosphoribosyldiphosphate amidotransferase; α-5-phosphoribosyl-1-pyrophosphate amidotransferase; 5′-phosphoribosylpyrophosphate amidotransferase; 5-phosphoribosyl-1-pyrophosphate amidotransferase; 5-phosphororibosyl-1-pyrophosphate amidotransferase; glutamine 5-phosphoribosylpyrophosphate amidotransferase; glutamine ribosylpyrophosphate 5-phosphate amidotransferase; phosphoribose pyrophosphate amidotransferase; phosphoribosyl pyrophosphate amidotransferase; phosphoribosylpyrophosphate glutamyl amidotransferase; 5-phosphoribosylamine:diphosphate phospho-α-D-ribosyltransferase (glutamate-amidating)
Systematic name: 5-phospho-β-D-ribosylamine:diphosphate phospho-α-D-ribosyltransferase (glutamate-amidating)
Links to other databases:
BRENDA,
EXPASY,
KEGG,
Metacyc,
PDB,
CAS registry number: 9031-82-7
References:
1. Caskey, C.T., Ashton, D.M. and Wyngaarden, J.B. The enzymology of feedback inhibition of glutamine phosphoribosylpyrophosphate amidotransferase by purine ribonucleotides. J. Biol. Chem. 239 (1964) 2570-2579.
2. Hartman, S.C. and Buchanan, J.M. Biosynthesis of the purines. XXI. 5-Phosphoribosylpyrophosphate amidotransferase. J. Biol. Chem. 233 (1958) 451-455.
Accepted name: guanosine phosphorylase
Reaction: guanosine + phosphate = guanine + α-D-ribose 1-phosphate
Other Name(s): guanosine:phosphate D-ribosyltransferase
Systematic name: guanosine:phosphate α-D-ribosyltransferase
Comments: Also acts on deoxyguanosine.
Links to other databases:
BRENDA,
EXPASY,
GTD,
KEGG,
Metacyc,
CAS registry number: 9030-28-8
References:
1. Yamada, E.W. The phosphorolysis of nucleosides by rabbit bone marrow. J. Biol. Chem. 236 (1961) 3043-3046.
Accepted name: urate-ribonucleoside phosphorylase
Reaction: urate D-ribonucleoside + phosphate = urate + α-D-ribose 1-phosphate
Other name(s): UAR phosphorylase; urate-ribonucleotide:phosphate D-ribosyltransferase (incorrect); urate-ribonucleotide:phosphate α-D-ribosyltransferase (incorrect); urate-ribonucleotide phosphorylase (incorrect)
Systematic name: urate-D-ribonucleoside:phosphate α-D-ribosyltransferase
Links to other databases:
BRENDA,
EXPASY,
KEGG,
Metacyc,
CAS registry number: 9030-29-9
References:
1. Laster, L. and Blair, A. An intestinal phosphorylase for uric acid ribonucleoside. J. Biol. Chem. 238 (1963) 3348-3357.
Accepted name: ATP phosphoribosyltransferase
Reaction: 1-(5-phospho-D-ribosyl)-ATP + diphosphate = ATP + 5-phospho-α-D-ribose 1-diphosphate
For diagram click here.
Other name(s): phosphoribosyl-ATP pyrophosphorylase; adenosine triphosphate phosphoribosyltransferase; phosphoribosyladenosine triphosphate:pyrophosphate phosphoribosyltransferase; phosphoribosyl ATP synthetase; phosphoribosyl ATP:pyrophosphate phosphoribosyltransferase; phosphoribosyl-ATP:pyrophosphate-phosphoribosyl phosphotransferase; phosphoribosyladenosine triphosphate pyrophosphorylase; phosphoribosyladenosine triphosphate synthetase; 1-(5-phospho-D-ribosyl)-ATP:diphosphate phospho-α-D-ribosyl-transferase
Systematic name: 1-(5-phospho-β-D-ribosyl)-ATP:diphosphate phospho-α-D-ribosyl-transferase
Comments: Involved in histidine biosynthesis.
Links to other databases:
BRENDA,
EXPASY,
KEGG,
Metacyc,
PDB,
CAS registry number: 9031-46-3
References:
1. Ames, B.N., Martin, R.G. and Garry, B.J. The first step of histidine biosynthesis. J. Biol. Chem. 236 (1961) 2019-2026.
2. Martin, R.G. The phosphorolysis of nucleosides by rabbit bone marrow: The nature of feedback inhibition by histidine. J. Biol. Chem. 238 (1963) 257-268.
3. Voll, M.J., Appella, E. and Martin, R.G. Purification and composition studies of phosphoribosyladenosine triphosphate:pyrophosphate phosphoribosyltransferase, the first enzyme of histidine biosynthesis. J. Biol. Chem. 242 (1967) 1760-1767. [PMID: 5337591]
Accepted name: anthranilate phosphoribosyltransferase
Reaction: N-(5-phospho-D-ribosyl)-anthranilate + diphosphate = anthranilate + 5-phospho-α-D-ribose 1-diphosphate
For diagram click here.
Other name(s): phosphoribosyl-anthranilate pyrophosphorylase; PRT; anthranilate 5-phosphoribosylpyrophosphate phosphoribosyltransferase; anthranilate phosphoribosylpyrophosphate phosphoribosyltransferase; phosphoribosylanthranilate pyrophosphorylase; phosphoribosylanthranilate transferase; anthranilate-PP-ribose-P phosphoribosyltransferase
Systematic name: N-(5-phospho-D-ribosyl)-anthranilate:diphosphate phospho-α-D-ribosyltransferase
Comments: In some organisms, this enzyme is part of a multifunctional protein together with one or more other components of the system for biosynthesis of tryptophan [EC 4.1.1.48 (indole-3-glycerol-phosphate synthase), EC 4.1.3.27 (anthranilate synthase), EC 4.2.1.20 (tryptophan synthase) and EC 5.3.1.24 (phosphoribosylanthranilate isomerase)].
Links to other databases:
BRENDA,
EXPASY,
KEGG,
Metacyc,
PDB,
CAS registry number: 9059-35-2
References:
1. Creighton, T.E. and Yanofsky, C. Chorismate to tryptophan (Escherichia coli) - Anthranilate synthetase, PR transferase, PRA isomerase, InGP synthetase, tryptophan synthetase. Methods Enzymol. 17A (1970) 365-380.
2. Hütter, R., Niederberger, P. and DeMoss, J.A. Tryptophan synthetic genes in eukaryotic microorganisms. Annu. Rev. Microbiol. 40 (1986) 55-77.
3. Ito, J. and Yanofsky, C. Anthranilate synthetase, an enzyme specified by the tryptophan operon of Escherichia coli: Comparative studies on the complex and the subunits. J. Bacteriol. 97 (1969) 734-742.
4. Wegman, J. and DeMoss, J.A. The enzymatic conversion of anthranilate to indolylglycerol phosphate in Neurospora crassa. J. Biol. Chem. 240 (1965) 3781-3788. [PMID: 5842052]
Accepted name: nicotinate-nucleotide diphosphorylase (carboxylating)
Reaction: nicotinate β-D-ribonucleotide + diphosphate + CO2 = pyridine-2,3-dicarboxylate + 5-phospho-α-D-ribose 1-diphosphate
For diagram of reaction click here.
Other name(s): quinolinate phosphoribosyltransferase (decarboxylating); quinolinic acid phosphoribosyltransferase; QAPRTase; NAD+ pyrophosphorylase; nicotinate mononucleotide pyrophosphorylase (carboxylating); quinolinic phosphoribosyltransferase; nicotinate-D-ribonucleotide:diphosphate phospho-α-D-ribosyltransferase (carboxylating)
Systematic name: nicotinate-β-D-ribonucleotide:diphosphate phospho-α-D-ribosyltransferase (carboxylating)
Comments: This is the first enzyme that prokaryotes and eukaryotes have in common in the production of NAD+ as some prokaryotes use an L-aspartate pathway to produce quinolinate whereas all eukaryotes use tryptophan as the starting material [3].
Links to other databases:
BRENDA,
EXPASY,
KEGG,
Metacyc,
PDB,
CAS registry number: 37277-74-0
References:
1. Gholson, R.K., Ueda, I., Ogasawara, N. and Henderson, L.M. The enzymatic conversion of quinolinate to nicotinic acid mononucleotide in mammalian liver. J. Biol. Chem. 239 (1964) 1208-1214.
2. Packman, P.M. and Jakoby, W.B. Crystalline quinolinate phosphoribosyltransferase. J. Biol. Chem. 240 (1965) 4107-4108. [PMID: 5320648]
3. Katoh, A., Uenohara, K., Akita, M. and Hashimoto, T. Early steps in the biosynthesis of NAD in Arabidopsis start with aspartate and occur in the plastid. Plant Physiol. 141 (2006) 851–857. [PMID: 16698895]
Accepted name: dioxotetrahydropyrimidine phosphoribosyltransferase
Reaction: A 2,4-dioxotetrahydropyrimidine D-ribonucleotide + diphosphate = a 2,4-dioxotetrahydropyrimidine + 5-phospho-α-D-ribose 1-diphosphate
Other name(s): dioxotetrahydropyrimidine-ribonucleotide pyrophosphorylase; dioxotetrahydropyrimidine phosphoribosyl transferase; dioxotetrahydropyrimidine ribonucleotide pyrophosphorylase; 2,4-dioxotetrahydropyrimidine-nucleotide:diphosphate phospho-α-D-ribosyltransferase
Systematic name: 2,4-dioxotetrahydropyrimidine-D-ribonucleotide:diphosphate phospho-α-D-ribosyltransferase
Comments: Acts (in the reverse direction) on uracil and other pyrimidines and pteridines containing a 2,4-diketo structure.
Links to other databases:
BRENDA,
EXPASY,
KEGG,
Metacyc,
CAS registry number: 37277-75-1
References:
1. Hatfield, D. and Wyngaarden, J.B. 3-Ribosylpurines. I. Synthesis of (3-ribosyluric acid) 5'-phosphate and (3-ribosylxanthine) 5'-phosphate by a pyrimidine ribonucleotide pyrophosphorylase of beef erythrocytes. J. Biol. Chem. 239 (1964) 2580-2586.
Accepted name: nicotinate-nucleotide—dimethylbenzimidazole phosphoribosyltransferase
Reaction: β-nicotinate D-ribonucleotide + dimethylbenzimidazole = nicotinate + N1-(5-phospho-α-D-ribosyl)-5,6-dimethylbenzimidazole
For diagram click here.
Glossary: α-ribazole 5′-phosphate = N1-(5-phospho-α-D-ribosyl)-5,6-dimethylbenzimidazole
Other name(s): nicotinate mononucleotide-dimethylbenzimidazole phosphoribosyltransferase; nicotinate ribonucleotide:benzimidazole (adenine) phosphoribosyltransferase; nicotinate-nucleotide:dimethylbenzimidazole phospho-D-ribosyltransferase; CobT; nicotinate mononucleotide (NaMN):5,6-dimethylbenzimidazole phosphoribosyltransferase
Systematic name: nicotinate-nucleotide:5,6-dimethylbenzimidazole phospho-D-ribosyltransferase
Comments: Also acts on benzimidazole, and the clostridial enzyme acts on adenine to form 7-α-D-ribosyladenine 5'-phosphate. The product of the reaction, α-ribazole 5′-phosphate, forms part of the corrin-biosynthesis pathway and is a substrate for EC 2.7.8.26, adenosylcobinamide-GDP ribazoletransferase [4]. It can also be dephosphorylated to form α-ribazole by the action of EC 3.1.3.73, α-ribazole phosphatase.
Links to other databases:
BRENDA,
EXPASY,
KEGG,
Metacyc,
PDB,
CAS registry number: 37277-76-2
References:
1. Friedmann, H.C. Partial purification and properties of a single displacement trans-N-glycosidase. J. Biol. Chem. 240 (1965) 413-418. [PMID: 14253445]
2. Friedmann, H.C. and Fyfe, J.A. Pseudovitamin B12 biosynthesis. Enzymatic formation of a new adenylic acid, 7-α-D-ribofuranosyladenine 5'-phosphate. J. Biol. Chem. 244 (1969) 1667-1671. [PMID: 5780835]
3. Fyfe, J.A. and Friedmann, H.C. Vitamin B12 biosynthesis. Enzyme studies on the formation of the α-glycosidic nucleotide precursor. J. Biol. Chem. 244 (1969) 1659-1666. [PMID: 4238408]
4. Cameron, B., Blanche, F., Rouyez, M.C., Bisch, D., Famechon, A., Couder, M., Cauchois, L., Thibaut, D., Debussche, L. and Crouzet, J. Genetic analysis, nucleotide sequence, and products of two Pseudomonas denitrificans cob genes encoding nicotinate-nucleotide: dimethylbenzimidazole phosphoribosyltransferase and cobalamin (5′-phosphate) synthase. J. Bacteriol. 173 (1991) 6066-;6073. [PMID: 1917841]
5. Cheong, C.G., Escalante-Semerena, J.C. and Rayment, I. Structural investigation of the biosynthesis of alternative lower ligands for cobamides by nicotinate mononucleotide: 5,6-dimethylbenzimidazole phosphoribosyltransferase from Salmonella enterica. J. Biol. Chem. 276 (2001) 37612-37620. [PMID: 11441022]
6. Cheong, C.G., Escalante-Semerena, J.C. and Rayment, I. Capture of a labile substrate by expulsion of water molecules from the active site of nicotinate mononucleotide:5,6-dimethylbenzimidazole phosphoribosyltransferase (CobT) from Salmonella enterica. J. Biol. Chem. 277 (2002) 41120-41127. [PMID: 12101181]
Accepted name: xanthine phosphoribosyltransferase
Reaction: XMP + diphosphate = 5-phospho-α-D-ribose 1-diphosphate + xanthine
Glossary: XMP = 9-(5-phospho-β-D-ribosyl)xanthine = xanthosine 5'-monophosphate
Other name(s): Xan phosphoribosyltransferase; xanthosine 5'-phosphate pyrophosphorylase; xanthylate pyrophosphorylase; xanthylic pyrophosphorylase; XMP pyrophosphorylase; 5-phospho-α-D-ribose-1-diphosphate:xanthine phospho-D-ribosyltransferase; 9-(5-phospho-β-D-ribosyl)xanthine:diphosphate 5-phospho-α-D-ribosyltransferase
Systematic name: XMP:diphosphate 5-phospho-α-D-ribosyltransferase
Links to other databases:
BRENDA,
EXPASY,
KEGG,
Metacyc,
PDB,
CAS registry number: 9023-10-3
References:
1. Krenitsky, T.A., Neil, S.M. and Miller, R.L. Guanine and xanthine phosphoribosyltransfer activities of Lactobacillus casei and Escherichia coli. Their relationship to hypoxanthine and adenine phosphoribosyltransfer activities. J. Biol. Chem. 245 (1970) 2605-2611. [PMID: 4910918]
[EC 2.4.2.23 Transferred entry: deoxyuridine phosphorylase. This activity has been shown to be catalysed by EC 2.4.2.2, pyrimidine-nucleoside phosphorylase, EC 2.4.2.3, uridine phosphorylase, and EC 2.4.2.4, thymidine phosphorylase. (EC 2.4.2.23 created 1972, deleted 2013)]
Accepted name: 1,4-β-D-xylan synthase
Reaction: UDP-D-xylose + [(1→4)-β-D-xylan]n = UDP + [(1→4)-β-D-xylan]n+1
Other name(s): uridine diphosphoxylose-1,4-β-xylan xylosyltransferase; 1,4-β-xylan synthase; xylan synthase; xylan synthetase
Systematic name: UDP-D-xylose:1,4-β-D-xylan 4-β-D-xylosyltransferase
Comments: Formerly EC 2.4.1.72.
Links to other databases:
BRENDA,
EXPASY,
KEGG,
Metacyc,
CAS registry number: 37277-73-9
References:
1. Bailey, R.W. and Hassid, W.Z. Xylan synthesis from uridine-diphosphate-D-xylose by particulate preparations from immature corncobs. Proc. Natl. Acad. Sci. USA 56 (1966) 1586-1593.
Accepted name: flavone apiosyltransferase
Reaction: UDP-α-D-apiose + apigenin 7-O-β-D-glucoside = UDP + apigenin 7-O-[β-D-apiosyl-(1→2)-β-D-glucoside]
For diagram click here.
Glossary: apigenin = 5,4',7-trihydroxyflavone
Other name(s): uridine diphosphoapiose-flavone apiosyltransferase; UDP-apiose:7-O-(β-D-glucosyl)-flavone apiosyltransferase; UDP-apiose:5,4'-dihydroxyflavone 7-O-β-D-glucoside 2"-O-β-D-apiofuranosyltransferase
Systematic name: UDP-apiose:4',5-dihydroxyflavone 7-O-β-D-glucoside 2"-O-β-D-apiofuranosyltransferase
Comments: 7-O-β-D-Glucosides of a number of flavonoids and of 4-substituted phenols can act as acceptors.
Links to other databases:
BRENDA,
EXPASY,
KEGG,
Metacyc,
CAS registry number: 37332-49-3
References:
1. Ortmann, R., Sutter, A. and Grisebach, H. Purification and properties of UDPapiose: 7-O-(β-D-glucosyl)-flavone apiosyltransferase from cell suspension cultures of parsley. Biochim. Biophys. Acta 289 (1972) 293-302. [PMID: 4650134]
Accepted name: protein xylosyltransferase
Reaction: UDP-α-D-xylose + [protein]-L-serine = UDP + [protein]-3-O-(β-D-xylosyl)-L-serine
For diagram of reaction click here
Other name(s): UDP-D-xylose:core protein β-D-xylosyltransferase; UDP-D-xylose:core protein xylosyltransferase; UDP-D-xylose:proteoglycan core protein β-D-xylosyltransferase; UDP-xylose-core protein β-D-xylosyltransferase; uridine diphosphoxylose-core protein β-xylosyltransferase; uridine diphosphoxylose-protein xylosyltransferase; UDP-D-xylose:protein β-D-xylosyltransferase
Systematic name: UDP-α-D-xylose:protein β-D-xylosyltransferase (configuration-inverting)
Comments: Involved in the biosynthesis of the linkage region of glycosaminoglycan chains as part of proteoglycan biosynthesis (chondroitin, dermatan and heparan sulfates).
Links to other databases:
BRENDA,
EXPASY,
KEGG,
MetaCyc,
PDB,
CAS registry number: 55576-38-0
References:
1. Stoolmiller, A.C., Horwitz, A.L. and Dorfman, A. Biosynthesis of the chondroitin sulfate proteoglycan. Purification and properties of xylosyltransferase. J. Biol. Chem. 247 (1972) 3525-3532. [PMID: 5030630]
2. Götting, C., Kuhn, J., Zahn, R., Brinkmann, T. and Kleesiek, K. Molecular cloning and expression of human UDP-D-xylose:proteoglycan core protein β-D-xylosyltransferase and its first isoform XT-II. J. Mol. Biol. 304 (2000) 517-528. [PMID: 11099377]
Accepted name: dTDP-dihydrostreptose—streptidine-6-phosphate dihydrostreptosyltransferase
Reaction: dTDP-L-dihydrostreptose + streptidine 6-phosphate = dTDP + O-(1→4)-α-L-dihydrostreptosyl-streptidine 6-phosphate
Other name(s): thymidine diphosphodihydrostreptose-streptidine 6-phosphate dihydrostreptosyltransferase
Systematic name: dTDP-L-dihydrostreptose:streptidine-6-phosphate dihydrostreptosyltransferase
Links to other databases:
BRENDA,
EXPASY,
KEGG,
Metacyc,
CAS registry number: 73699-20-4
References:
1. Kniep, B. and Grisebach, H. Biosynthesis of streptomycin. Purification and properties of a dTDP-L-dihydrostreptose: streptidine-6-phosphate dihydrostreptosyltransferase from Streptomyces griseus.Eur. J. Biochem. 105 (1980) 139-144. [PMID: 6768553]
Accepted name: S-methyl-5'-thioadenosine phosphorylase
Reaction: S-methyl-5'-thioadenosine + phosphate = adenine + S-methyl-5-thio-α-D-ribose 1-phosphate
For diagram click here
Other name(s): 5′-deoxy-5′-methylthioadenosine phosphorylase; MTA phosphorylase; MeSAdo phosphorylase; MeSAdo/Ado phosphorylase; methylthioadenosine phosphorylase; methylthioadenosine nucleoside phosphorylase; 5′-methylthioadenosine:phosphate methylthio-D-ribosyl-transferase; S-methyl-5-thioadenosine phosphorylase; S-methyl-5-thioadenosine:phosphate S-methyl-5-thio-α-D-ribosyl-transferase
Systematic name: S-methyl-5'-thioadenosine:phosphate S-methyl-5-thio-α-D-ribosyl-transferase
Comments: Also acts on 5'-deoxyadenosine and other analogues having 5'-deoxy groups.
Links to other databases:
BRENDA,
EXPASY,
KEGG,
Metacyc,
PDB,
CAS registry number: 61970-06-7
References:
1. Carteni-Farina, M., Oliva, A., Romeo, G., Napolitano, G., De Rosa, M., Gambacorta, A. and Zappia, V. 5'-Methylthioadenosine phosphorylase from Caldariella acidophila. Purification and properties. Eur. J. Biochem. 101 (1979) 317-324. [PMID: 118001]
2. Garbers, D.L. Demonstration of 5'-methylthioadenosine phosphorylase activity in various rat tissues. Some properties of the enzyme from rat lung. Biochim. Biophys. Acta 523 (1978) 82-93. [MPID: 415762]
3. Pegg, A.E. and Williams-Ashman, H.G. Phosphate-stimulated breakdown of 5'-methylthioadenosine by rat ventral prostate. Biochem. J. 115 (1969) 241-247. [PMID: 5378381]
Accepted name: tRNA-guanosine34 preQ1 transglycosylase
Reaction: guanine34 in tRNA + 7-aminomethyl-7-carbaguanine = 7-aminomethyl-7-carbaguanine34 in tRNA + guanine
For diagram of reaction click here
Glossary: 7-aminomethyl-7-carbaguanine = preQ1 = 7-aminomethyl-7-deazaguanine
Other name(s): guanine insertion enzyme (ambiguous); tRNA transglycosylase (ambiguous); Q-insertase (ambiguous); transfer ribonucleate glycosyltransferase (ambiguous); tRNA guanine34 transglycosidase (ambiguous); TGT (ambiguous); transfer ribonucleic acid guanine34 transglycosylase (ambiguous)
Systematic name: tRNA-guanosine34:7-aminomethyl-7-deazaguanine tRNA-D-ribosyltransferase
Comments: Certain prokaryotic and eukaryotic tRNAs contain the modified base queuine at position 34. In eubacteria, which produce queuine de novo, the enzyme catalyses the exchange of guanine with the queuine precursor preQ1, which is ultimately modified to queuosine [5]. The enzyme can also use an earlier intermediate, preQ0, to replace guanine in unmodified tRNATyr and tRNAAsn [1]. This enzyme acts after EC 1.7.1.13, preQ1 synthase, in the queuine-biosynthesis pathway. cf. EC 2.4.2.64, tRNA-guanosine34 queuine transglycosylase.
Links to other databases:
BRENDA,
EXPASY,
KEGG,
MetaCyc,
PDB,
CAS registry number: 72162-89-1
References:
1. Okada, N., Noguchi, S., Kasai, H., Shindo-Okada, N., Ohgi, T., Goto, T. and Nishimura, S. Novel mechanism of post-transcriptional modification of tRNA. Insertion of bases of Q precursors into tRNA by a specific tRNA transglycosylase reaction. J. Biol. Chem. 254 (1979) 3067-3073. [PMID: 372186]
2. Noguchi, S., Nishimura, Y., Hirota, Y. and Nishimura, S. Isolation and characterization of an Escherichia coli mutant lacking tRNA-guanine transglycosylase. Function and biosynthesis of queuosine in tRNA. J. Biol. Chem. 257 (1982) 6544-6550. [PMID: 6804468]
3. Chong, S., Curnow, A.W., Huston, T.J. and Garcia, G.A. tRNA-guanine transglycosylase from Escherichia coli is a zinc metalloprotein. Site-directed mutagenesis studies to identify the zinc ligands. Biochemistry 34 (1995) 3694-3701. [PMID: 7893665]
4. Goodenough-Lashua, D.M. and Garcia, G.A. tRNA-guanine transglycosylase from E. coli: a ping-pong kinetic mechanism is consistent with nucleophilic catalysis. Bioorg. Chem. 31 (2003) 331-344. [PMID: 12877882]
5. Todorov, K.A. and Garcia, G.A. Role of aspartate 143 in Escherichia coli tRNA-guanine transglycosylase: alteration of heterocyclic substrate specificity. Biochemistry 45 (2006) 617-625. [PMID: 16401090]
Accepted name: NAD+ ADP-ribosyltransferase
Reaction: NAD+ + (ADP-D-ribosyl)n-acceptor = nicotinamide + (ADP-D-ribosyl)n+1-acceptor + H+
For diagram click here.
Other name(s): poly(ADP-ribose) synthase; ADP-ribosyltransferase (polymerizing); NAD ADP-ribosyltransferase; PARP; PARP-1; NAD+:poly(adenine-diphosphate-D-ribosyl)-acceptor ADP-D-ribosyl-transferase (incorrect); NAD+:poly(adenosine-diphosphate-D-ribosyl)-acceptor ADP-D-ribosyl-transferase
Systematic name: NAD+:poly(ADP-D-ribosyl)-acceptor ADP-D-ribosyl-transferase
Comments: The ADP-D-ribosyl group of NAD+ is transferred to an acceptor carboxy group on a histone or the enzyme itself, and further ADP-ribosyl groups are transferred to the 2'-position of the terminal adenosine moiety, building up a polymer with an average chain length of 20-30 units.
Links to other databases:
BRENDA,
EXPASY,
KEGG,
Metacyc,
PDB,
CAS registry number: 58319-92-9
References:
1. Ueda, K. and Hayaishi, O. ADP-ribosylation. Annu. Rev. Biochem. 54 (1985) 73-100. [PMID: 3927821]
2. Ueda, K., Kawaichi, M. and Hayaishi, O. Poly(ADP-ribose) synthetase. In: Hayaishi, O. and Ueda, K. (Eds.), ADP-Ribosylation Reactions: Biology and Medicine, Academic Press, London, 1982, p. 117-155.
3. Ushiro, H., Yokoyama, Y. and Shizuta, Y. Purification and characterization of poly (ADP-ribose) synthetase from human placenta. J. Biol. Chem. 262 (1987) 2352-2357. [PMID: 2434482]
Accepted name: NAD+—protein-arginine ADP-ribosyltransferase
Reaction: NAD+ + protein L-arginine = nicotinamide + Nω-(ADP-D-ribosyl)-protein-L-arginine
Other name(s): ADP-ribosyltransferase; mono(ADP-ribosyl)transferase; NAD+:L-arginine ADP-D-ribosyltransferase; NAD(P)+-arginine ADP-ribosyltransferase; NAD(P)+:L-arginine ADP-D-ribosyltransferase; mono-ADP-ribosyltransferase; ART; ART1; ART2; ART3; ART4; ART5; ART6; ART7; NAD(P)+—protein-arginine ADP-ribosyltransferase
Systematic name: NAD+:protein-L-arginine ADP-D-ribosyltransferase
Comments: Protein mono-ADP-ribosylation is a reversible post-translational modification that plays a role in the regulation of cellular activities [4]. Arginine residues in proteins act as acceptors. Free arginine, agmatine [(4-aminobutyl)guanidine], arginine methyl ester and guanidine can also do so. The enzyme from some, but not all, species can also use NADP+ as acceptor (giving rise to Nω-[(2'-phospho-ADP)-D-ribosyl]-protein-L-arginine as the product), but more slowly [1,5]. The enzyme catalyses the NAD+-dependent activation of EC 4.6.1.1, adenylate cyclase. Some bacterial enterotoxins possess similar enzymatic activities. (cf. EC 2.4.2.36 NAD+—diphthamide ADP-ribosyltransferase).
Links to other databases: BRENDA, EXPASY,
KEGG,
Metacyc,
PDB,
CAS registry number: 81457-93-4
References:
1. Moss, J., Stanley, S.J. and Oppenheimer, N.J. Substrate specificity and partial purification of a stereospecific NAD- and guanidine-dependent ADP-ribosyltransferase from avian erythrocytes. J. Biol. Chem. 254 (1979) 8891-8894. [PMID: 225315]
2. Moss, J., Stanley, S.J. and Watkins, P.A. Isolation and properties of an NAD- and guanidine-dependent ADP-ribosyltransferase from turkey erythrocytes. J. Biol. Chem. 255 (1980) 5838-5840. [PMID: 6247348]
3. Ueda, K. and Hayaishi, O. ADP-ribosylation. Annu. Rev. Biochem. 54 (1985) 73-100. [PMID: 3927821]
4. Corda, D. and Di Girolamo, M. Functional aspects of protein mono-ADP-ribosylation. EMBO J. 22 (2003) 1953-1958. [PMID: 12727863]
5. Paone, G., Stevens, L.A., Levine, R.L., Bourgeois, C., Steagall, W.K., Gochuico, B.R. and Moss, J. ADP-ribosyltransferase-specific modification of human neutrophil peptide-1. J. Biol. Chem. 281 (2006) 17054–17060. [PMID: 16627471]
Accepted name: dolichyl-phosphate D-xylosyltransferase
Reaction: UDP-D-xylose + dolichyl phosphate = UDP + dolichyl D-xylosyl phosphate
Glossary: dolichol
Systematic name: UDP-D-xylose:dolichyl-phosphate D-xylosyltransferase
Links to other databases:
BRENDA,
EXPASY,
KEGG,
Metacyc,
CAS registry number:
References:
1. Waechter, C.J., Lucas, J.J. and Lennarz, W.J. Evidence for xylosyl lipids as intermediates in xylosyl transfers in hen oviduct membranes. Biochem. Biophys. Res. Commun. 56 (1974) 343-350. [PMID: 4823870]
Accepted name: dolichyl-xylosyl-phosphate—protein xylosyltransferase
Reaction: dolichyl D-xylosyl phosphate + protein = dolichyl phosphate + D-xylosylprotein
Systematic name: dolichyl-D-xylosyl-phosphate:protein D-xylosyltransferase
Links to other databases:
BRENDA,
EXPASY,
KEGG,
Metacyc,
CAS registry number:
References:
1. Waechter, C.J., Lucas, J.J. and Lennarz, W.J. Evidence for xylosyl lipids as intermediates in xylosyl transfers in hen oviduct membranes. Biochem. Biophys. Res. Commun. 56 (1974) 343-350. [PMID: 4823870]
Accepted name: indolylacetylinositol arabinosyltransferase
Reaction: UDP-L-arabinose + (indol-3-yl)acetyl-1D-myo-inositol = UDP + (indol-3-yl)acetyl-myo-inositol 3-L-arabinoside
Other name(s): arabinosylindolylacetylinositol synthase; UDP-L-arabinose:indol-3-ylacetyl-myo-inositol L-arabinosyltransferase; UDP-L-arabinose:(indol-3-yl)acetyl-myo-inositol L-arabinosyltransferase
Systematic name: UDP-L-arabinose:(indol-3-yl)acetyl-1D-myo-inositol L-arabinosyltransferase
Comments: The position of acylation is indeterminate because of the ease of acyl transfer between hydroxy groups. For a diagram showing the biosynthesis of UDP-L-arabinose, click here.
Links to other databases:
BRENDA,
EXPASY,
KEGG,
Metacyc,
PDB,
CAS registry number: 84720-96-7
References:
1. Corcuera, L.J. and Bandurski, R.S. Biosynthesis of indol-3-yl-acetyl-myo-inositol arabinoside in kernels of Zea mays L. Plant Physiol. 70 (1982) 1664-1666.
Accepted name: flavonol-3-O-glycoside xylosyltransferase
Reaction: UDP-α-D-xylose + a flavonol 3-O-glycoside = UDP + a flavonol 3-[β-D-xylosyl-(1→2)-β-D-glycoside]
For diagram of reaction click here.
Other name(s): UDP-D-xylose:flavonol-3-O-glycoside 2''-O-β-D-xylosyltransferase
Systematic name: UDP-α-D-xylose:flavonol-3-O-glycoside 2''-O-β-D-xylosyltransferase
Comments: Flavonol 3-O-glucoside, flavonol 3-O-galactoside and, more slowly, rutin, can act as acceptors.
Links to other databases:
BRENDA,
EXPASY,
KEGG,
MetaCyc,
CAS registry number: 83380-90-9
References:
1. Kleinehollenhorst, G., Behrens, H., Pegels, G., Srunk, N. and Wiermann, R. Formation of flavonol 3-O-diglycosides and flavonol 3-O-triglycosides by enzyme extracts from anthers of Tulipa cv apeldoorn - characterization and activity of 3 different O-glycosyltransferases during anther development. Z. Natursforsch. C: Biosci. 37 (1982) 587-599.
Accepted name: NAD+—diphthamide ADP-ribosyltransferase
Reaction: NAD+ + diphthamide-[translation elongation factor 2] = nicotinamide + N-(ADP-D-ribosyl)diphthamide-[translation elongation factor 2]
For diagram of reaction click here.
Glossary: diphthamide = 2-[4-amino-4-oxo-3-(trimethylammonio)butyl]-L-histidine
Other name(s): ADP-ribosyltransferase; mono(ADPribosyl)transferase; NAD—diphthamide ADP-ribosyltransferase; NAD+:peptide-diphthamide N-(ADP-D-ribosyl)transferase
Systematic name: NAD+:diphthamide-[translation elongation factor 2] N-(ADP-D-ribosyl)transferase
Comments: Diphtheria toxin and some other bacterial toxins catalyse this reaction, which inactivates translation elongation factor 2 (EF2). The acceptor is diphthamide, a unique modification of a histidine residue in the elongation factor found in archaebacteria and all eukaryotes, but not in eubacteria. cf. EC 2.4.2.31 NAD(P)+—protein-arginine ADP-ribosyltransferase. The relevant histidine of EF2 is His715 in mammals, His699 in yeast and His600 in Pyrococcus horikoshii.
Links to other databases:
BRENDA,
EXPASY,
KEGG,
Metacyc,
PDB,
CAS registry number: 52933-21-8
References:
1. Lee, H. and Iglewski, W.J. Cellular ADP-ribosyltransferase with the same mechanism of action as diphtheria toxin and Pseudomonas toxin A. Proc. Natl. Acad. Sci. USA 81 (1984) 2703-2707. [PMID: 6326138]
2. Ueda, K. and Hayaishi, O. ADP-ribosylation. Annu. Rev. Biochem. 54 (1985) 73-100. [PMID: 3927821]
Accepted name: NAD+—dinitrogen-reductase ADP-D-ribosyltransferase
Reaction: NAD+ + [dinitrogen reductase]-L-arginine = nicotinamide + [dinitrogen reductase]-Nω-α-(ADP-D-ribosyl)-L-arginine
Other name(s): NAD-azoferredoxin (ADPribose)transferase; NAD-dinitrogen-reductase ADP-D-ribosyltransferase; draT (gene name)
Systematic name: NAD+:[dinitrogen reductase] (ADP-D-ribosyl)transferase
Comments: The combined action of this enzyme and EC 3.2.2.24, ADP-ribosyl-[dinitrogen reductase] hydrolase, controls the activity level of nitrogenase (EC 1.18.6.1). In the presence of ammonium, the product of nitrogenase, this enzyme covalently links an ADP-ribose moiety to a specific arginine residue of the dinitrogenase reductase component of nitrogenase, blocking its activity.
Links to other databases:
BRENDA,
EXPASY,
KEGG,
MetaCyc,
CAS registry number: 117590-45-1
References:
1. Lowery, R.G. and Ludden, P.W. Purification and properties of dinitrogenase reductase ADP-ribosyltransferase from the photosynthetic bacterium Rhodospirillum rubrum. J. Biol. Chem. 263 (1988) 16714-16719. [PMID: 3141411]
2. Fitzmaurice, W.P., Saari, L.L., Lowery, R.G., Ludden, P.W. and Roberts, G.P. Genes coding for the reversible ADP-ribosylation system of dinitrogenase reductase from Rhodospirillum rubrum. Mol. Gen. Genet. 218 (1989) 340-347. [PMID: 2506427]
3. Moure, V.R., Costa, F.F., Cruz, L.M., Pedrosa, F.O., Souza, E.M., Li, X.D., Winkler, F. and Huergo, L.F. Regulation of nitrogenase by reversible mono-ADP-ribosylation. Curr. Top. Microbiol. Immunol. 384 (2015) 89-106. [PMID: 24934999]
Accepted name: glycoprotein 2-β-D-xylosyltransferase
Reaction: UDP-α-D-xylose + N4-{β-D-GlcNAc-(1→2)-α-D-Man-(1→3)-[β-D-GlcNAc-(1→2)-α-D-Man-(1→6)]-β-D-Man-(1→4)-β-D-GlcNAc-(1→4)-β-D-GlcNAc}-L-asparaginyl-[protein] = UDP + N4-{β-D-GlcNAc-(1→2)-α-D-Man-(1→3)-[β-D-GlcNAc-(1→2)-α-D-Man-(1→6)]-[β-D-Xyl-(1→2)]-β-D-Man-(1→4)-β-D-GlcNAc-(1→4)-β-D-GlcNAc}-L-asparaginyl-[protein]
For diagram click here.
Other name(s): β1,2-xylosyltransferase
Systematic name: UDP-α-D-xylose:N4-{β-D-GlcNAc-(1→2)-α-D-mannosyl-(1→3)-[β-D-GlcNAc-(1→2)-α-D-mannosyl-(1→6)]-β-D-mannosyl-(1→4)-β-D-GlcNAc-(1→4)-β-D-GlcNAc}-L-asparaginyl-[protein] 2-β-D-xylosyltransferase (configuration-inverting)
Comments: Specific for N-linked oligosaccharides (N-glycans).
Links to other databases:
BRENDA,
EXPASY,
KEGG,
Metacyc,
CAS registry number: 141256-56-6
References:
1. Zeng, Y., Bannon, G., Thomas, V.H., Rice, K., Drake, R. and Elbein, A. Purification and specificity of β1,2-xylosyltransferase, an enzyme that contributes to the allergenicity of some plant proteins. J. Biol. Chem. 272 (1997) 31340-31347. [PMID: 9395463]
2. Strasser, R., Mucha, J., Mach, L., Altmann, F., Wilson, I.B., Glössl, J. and Steinkellner, H. Molecular cloning and functional expression of β1,2-xylosyltransferase cDNA from Arabidopsis thaliana. FEBS Lett. 472 (2000) 105-108. [PMID: 10781814]
Accepted name: xyloglucan 6-xylosyltransferase
Reaction: Transfers an α-D-xylosyl residue from UDP-D-xylose to a glucose residue in xyloglucan, forming an α-(1→6)-D-xylosyl-D-glucose linkage
Other name(s): uridine diphosphoxylose-xyloglucan 6α-xylosyltransferase; xyloglucan 6-α-D-xylosyltransferase
Systematic name: UDP-D-xylose:xyloglucan 1,6-α-D-xylosyltransferase
Comments: In association with EC 2.4.1.168 (xyloglucan 4-glucosyltransferase), this enzyme brings about the synthesis of xyloglucan; concurrent transfers of glucose and xylose are necessary for this synthesis.
Links to other databases:
BRENDA,
EXPASY,
KEGG,
Metacyc,
PDB,
CAS registry number: 80238-01-3
References:
1. Hayashi, T. and Matsuda, K. Biosynthesis of xyloglucan in suspension-cultured soybean cells. Occurrence and some properties of xyloglucan 4-β-D-glucosyltransferase and 6-α-D-xylosyltransferase. J. Biol. Chem. 256 (1981) 11117-11122. [PMID: 6457048]
2. Hayashi, T. and Matsuda, K. Biosynthesis of xyloglucan in suspension-cultured soybean cells-synthesis of xyloglucan from UDP-glucose and UDP-xylose in the cell-free system. Plant Cell Physiol. 22 (1981) 517-523.
Accepted name: zeatin O-β-D-xylosyltransferase
Reaction: UDP-D-xylose + zeatin = UDP + O-β-D-xylosylzeatin
Glossary: zeatin
Other name(s): uridine diphosphoxylose-zeatin xylosyltransferase; zeatin O-xylosyltransferase
Systematic name: UDP-D-xylose:zeatin O-β-D-xylosyltransferase
Comments: Does not act on UDP-glucose (cf. EC 2.4.1.103 alizarin 2-β-glucosyltransferase).
Links to other databases:
BRENDA,
EXPASY,
KEGG,
Metacyc,
CAS registry number: 110541-22-5
References:
1. Turner, J.E., Mok, D.W.S., Mok, M.C. and Shaw, G. Isolation and partial-purification of an enzyme catalyzing the formation of O-xylosylzeatin in Phaseolus vulgaris embryos. Proc. Natl. Acad. Sci. USA 84 (1987) 3714-3717.
Accepted name: xylogalacturonan β-1,3-xylosyltransferase
Reaction: Transfers a xylosyl residue from UDP-D-xylose to a D-galactose residue in xylogalacturonan, forming a β-1,3-D-xylosyl-D-galactose linkage.
Other name(s): xylogalacturonan xylosyltransferase; XGA xylosyltransferase
Systematic name: UDP-D-xylose:xylogalacturonan β-1,3-xylosyltransferase
Comments: Involved in plant cell wall synthesis. The enzyme from Arabidopsis thaliana also transfers D-xylose from UDP-D-xylose onto oligogalacturonide acceptors. The enzyme did not show significant activity with UDP-glucose, UDP-galactose, or UDP-N-acetyl-D-glucosamine as sugar donors.
Links to other databases:
BRENDA,
EXPASY,
KEGG,
Metacyc,
CAS registry number:
References:
1. Jensen, J.K., Sorensen, S.O., Harholt, J., Geshi, N., Sakuragi, Y., Moller, I., Zandleven, J., Bernal, A.J., Jensen, N.B., Sorensen, C., Pauly, M., Beldman, G., Willats, W.G. and Scheller, H.V. Identification of a xylogalacturonan xylosyltransferase involved in pectin biosynthesis in Arabidopsis. Plant Cell 20 (2008) 1289-1302. [PMID: 18460606]
Accepted name: UDP-D-xylose:β-D-glucoside α-1,3-D-xylosyltransferase
Reaction: UDP-α-D-xylose + [protein with EGF-like domain]-3-O-(β-D-glucosyl)-L-serine = UDP + [protein with EGF-like domain]-3-O-[α-D-xylosyl-(1→3)-β-D-glucosyl]-L-serine
Other name(s): β-glucoside α-1,3-xylosyltransferase; UDP-α-D-xylose:β-D-glucoside 3-α-D-xylosyltransferase; GXYLT1 (gene name); GXYLT2 (gene name)
Systematic name: UDP-α-D-xylose:[EGF-like domain protein]-3-O-(β-D-glucosyl)-L-serine 3-α-D-xylosyltransferase (configuration-retaining)
Comments: The enzyme, found in animals and insects, is involved in the biosynthesis of the α-D-xylosyl-(1→3)-α-D-xylosyl-(1→3)-β-D-glucosyl trisaccharide on epidermal growth factor-like (EGF-like) domains [2,3]. When present on Notch proteins, the trisaccharide functions as a modulator of the signalling activity of this protein.
Links to other databases:
BRENDA,
EXPASY,
KEGG,
MetaCyc,
CAS registry number:
References:
1. Omichi, K., Aoki, K., Minamida, S. and Hase, S. Presence of UDP-D-xylose: β-D-glucoside α-1,3-D-xylosyltransferase involved in the biosynthesis of the Xyl α 1-3Glc β-Ser structure of glycoproteins in the human hepatoma cell line HepG2. Eur. J. Biochem. 245 (1997) 143-146. [PMID: 9128735]
2. Ishimizu, T., Sano, K., Uchida, T., Teshima, H., Omichi, K., Hojo, H., Nakahara, Y. and Hase, S. Purification and substrate specificity of UDP-D-xylose:β-D-glucoside α-1,3-D-xylosyltransferase involved in the biosynthesis of the Xyl α1-3Xyl α1-3Glc β1-O-Ser on epidermal growth factor-like domains. J. Biochem. 141 (2007) 593-600. [PMID: 17317689]
3. Sethi, M.K., Buettner, F.F., Krylov, V.B., Takeuchi, H., Nifantiev, N.E., Haltiwanger, R.S., Gerardy-Schahn, R. and Bakker, H. Identification of glycosyltransferase 8 family members as xylosyltransferases acting on O-glucosylated notch epidermal growth factor repeats. J. Biol. Chem. 285 (2010) 1582-1586. [PMID: 19940119]
Accepted name: lipid IVA 4-amino-4-deoxy-L-arabinosyltransferase
Reaction: (1) 4-amino-4-deoxy-α-L-arabinopyranosyl ditrans,octacis-undecaprenyl phosphate + α-Kdo-(2→4)-α-Kdo-(2→6)-lipid A = α-Kdo-(2→4)-Kdo-(2→6)-[4-P-L-Ara4N]-lipid A + ditrans,octacis-undecaprenyl phosphate
For diagram of reaction click here.
Glossary: lipid IVA = 2-deoxy-2-{[(3R)-3-hydroxytetradecanoyl]amino}-3-O-[(3R)-3-hydroxytetradecanoyl]-4-O-phospho-β-D-glucopyranosyl-(1→6)-2-deoxy-3-O-[(3R)-3-hydroxytetradecanoyl]-2-{[(3R)-3-hydroxytetradecanoyl]amino}-1-O-phospho-α-D-glucopyranose
Other name(s): undecaprenyl phosphate-α-L-Ara4N transferase; 4-amino-4-deoxy-L-arabinose lipid A transferase; polymyxin resistance protein PmrK, arnT (gene name)
Systematic name: 4-amino-4-deoxy-α-L-arabinopyranosyl ditrans,octacis-undecaprenyl phosphate:lipid IVA 4-amino-4-deoxy-L-arabinopyranosyltransferase
Comments: Integral membrane protein present in the inner membrane of certain Gram negative endobacteria. In strains that do not produce 3-deoxy-D-manno-octulosonic acid (Kdo), the enzyme adds a single arabinose unit to the 1-phosphate moiety of the tetra-acylated lipid A precursor, lipid IVA. In the presence of a Kdo disaccharide, the enzyme primarily adds an arabinose unit to the 4-phosphate of lipid A molecules. The Salmonella typhimurium enzyme can add arabinose units to both positions.
Links to other databases:
BRENDA,
EXPASY,
KEGG,
Metacyc,
PDB,
CAS registry number:
References:
1. Trent, M.S., Ribeiro, A.A., Lin, S., Cotter, R.J. and Raetz, C.R. An inner membrane enzyme in Salmonella and Escherichia coli that transfers 4-amino-4-deoxy-L-arabinose to lipid A: induction on polymyxin-resistant mutants and role of a novel lipid-linked donor. J. Biol. Chem. 276 (2001) 43122-43131. [PMID: 11535604]
2. Trent, M.S., Ribeiro, A.A., Doerrler, W.T., Lin, S., Cotter, R.J. and Raetz, C.R. Accumulation of a polyisoprene-linked amino sugar in polymyxin-resistant Salmonella typhimurium and Escherichia coli: structural characterization and transfer to lipid A in the periplasm. J. Biol. Chem. 276 (2001) 43132-43144. [PMID: 11535605]
3. Zhou, Z., Ribeiro, A.A., Lin, S., Cotter, R.J., Miller, S.I. and Raetz, C.R. Lipid A modifications in polymyxin-resistant Salmonella typhimurium: PMRA-dependent 4-amino-4-deoxy-L-arabinose, and phosphoethanolamine incorporation. J. Biol. Chem. 276 (2001) 43111-43121. [PMID: 11535603]
4. Bretscher, L.E., Morrell, M.T., Funk, A.L. and Klug, C.S. Purification and characterization of the L-Ara4N transferase protein ArnT from Salmonella typhimurium. Protein Expr. Purif. 46 (2006) 33-39. [PMID: 16226890]
5. Impellitteri, N.A., Merten, J.A., Bretscher, L.E. and Klug, C.S. Identification of a functionally important loop in Salmonella typhimurium ArnT. Biochemistry 49 (2010) 29-35. [PMID: 19947657]
Accepted name: S-methyl-5'-thioinosine phosphorylase
Reaction: S-methyl-5'-thioinosine + phosphate = hypoxanthine + S-methyl-5-thio-α-D-ribose 1-phosphate
Other name(s): MTIP; MTI phosphorylase; methylthioinosine phosphorylase
Systematic name: S-methyl-5'-thioinosine:phosphate S-methyl-5-thio-α-D-ribosyl-transferase
Comments: No activity with S-methyl-5'-thioadenosine. The catabolism of of 5'-methylthioadenosine in Pseudomonas aeruginosa involves deamination to S-methyl-5'-thioinosine (EC 3.5.4.31, S-methyl-5'-thioadenosine deaminase) and phosphorolysis to hypoxanthine [1].
Links to other databases:
BRENDA,
EXPASY,
KEGG,
Metacyc,
PDB,
CAS registry number:
References:
1. Guan, R., Ho, M.C., Almo, S.C. and Schramm, V.L. Methylthioinosine phosphorylase from Pseudomonas aeruginosa. Structure and annotation of a novel enzyme in quorum sensing. Biochemistry 50 (2011) 1247-1254. [PMID: 21197954]
EC 2.4.2.45
Accepted name: decaprenyl-phosphate phosphoribosyltransferase
Reaction: trans,octacis-decaprenyl phosphate + 5-phospho-α-D-ribose 1-diphosphate = trans,octacis-decaprenylphospho-β-D-ribofuranose 5-phosphate + diphosphate
For diagram of reaction click here.
Other name(s): 5-phospho-α-D-ribose-1-diphosphate:decaprenyl-phosphate 5-phosphoribosyltransferase; 5-phospho-α-D-ribose 1-pyrophosphate:decaprenyl phosphate 5-phosphoribosyltransferase; DPPR synthase; Rv3806
Systematic name: trans,octacis-decaprenylphospho-β-D-ribofuranose 5-phosphate:diphosphate phospho-α-D-ribosyltransferase
Comments: Requires Mg2+. Isolated from Mycobacterium tuberculosis. Has some activity with other polyprenyl phosphates.
Links to other databases:
BRENDA,
EXPASY,
KEGG,
Metacyc,
PDB,
CAS registry number:
References:
1. Huang, H., Scherman, M.S., D'Haeze, W., Vereecke, D., Holsters, M., Crick, D.C. and McNeil, M.R. Identification and active expression of the Mycobacterium tuberculosis gene encoding 5-phospho-α-D-ribose-1-diphosphate: decaprenyl-phosphate 5-phosphoribosyltransferase, the first enzyme committed to decaprenylphosphoryl-D-arabinose synthesis. J. Biol. Chem. 280 (2005) 24539-24543. [PMID: 15878857]
Accepted name: galactan 5-O-arabinofuranosyltransferase
Reaction: Adds an α-D-arabinofuranosyl group from trans,octacis-decaprenylphospho-β-D-arabinofuranose at the 5-O-position of the eighth, tenth and twelfth galactofuranose unit of the galactofuranan chain of [β-D-galactofuranosyl-(1→5)-β-D-galactofuranosyl-(1→6)]14-β-D-galactofuranosyl-(1→5)-β-D-galactofuranosyl-(1→4)-α-L-rhamnopyranosyl-(1→3)-N-acetyl-α-D-glucosaminyl-diphospho-trans,octacis-decaprenol
For diagram of reaction click here.
Other name(s): AftA; Rv3792
Systematic name: galactofuranan:trans,octacis-decaprenylphospho-β-D-arabinofuranose 5-O-α-D-arabinofuranosyltransferase
Comments: Isolated from Mycobacterium tuberculosis and Corynebacterium glutamicum. These arabinofuranosyl groups form the start of an arabinofuranan chain as part of the of the cell wall in mycobacteria.
Links to other databases:
BRENDA,
EXPASY,
KEGG,
Metacyc,
PDB,
CAS registry number:
References:
1. Alderwick, L.J., Seidel, M., Sahm, H., Besra, G.S. and Eggeling, L. Identification of a novel arabinofuranosyltransferase (AftA) involved in cell wall arabinan biosynthesis in Mycobacterium tuberculosis. J. Biol. Chem. 281 (2006) 15653-15661. [PMID: 16595677]
Accepted name: arabinofuranan 3-O-arabinosyltransferase
Reaction: Adds an α-D-arabinofuranosyl group from trans,octacis-decaprenylphospho-β-D-arabinofuranose at the 3-O-position of an α-(1→5)-arabinofuranan chain attached to a β-(1→5)-galactofuranan chain
For diagram of reaction click here.
Other name(s): AftC
Systematic name: α-(1→5)-arabinofuranan:trans,octacis-decaprenylphospho-β-D-arabinofuranose 3-O-α-D-arabinofuranosyltransferase
Comments: Isolated from Mycobacterium smegmatis. Involved in the formation of the cell wall in mycobacteria.
Links to other databases:
BRENDA,
EXPASY,
KEGG,
Metacyc,
CAS registry number:
References:
1. Birch, H.L., Alderwick, L.J., Bhatt, A., Rittmann, D., Krumbach, K., Singh, A., Bai, Y., Lowary, T.L., Eggeling, L. and Besra, G.S. Biosynthesis of mycobacterial arabinogalactan: identification of a novel α(1-→3) arabinofuranosyltransferase. Mol. Microbiol. 69 (2008) 1191-1206. [PMID: 18627460]
2. Zhang, J., Angala, S.K., Pramanik, P.K., Li, K., Crick, D.C., Liav, A., Jozwiak, A., Swiezewska, E., Jackson, M. and Chatterjee, D. Reconstitution of functional mycobacterial arabinosyltransferase AftC proteoliposome and assessment of decaprenylphosphorylarabinose analogues as arabinofuranosyl donors. ACS Chem. Biol. 6 (2011) 819-828. [PMID: 21595486]
Accepted name: tRNA-guanine15 transglycosylase
Reaction: guanine15 in tRNA + 7-cyano-7-carbaguanine = 7-cyano-7-carbaguanine15 in tRNA + guanine
Glossary: 7-cyano-7-carbaguanine = preQ0 = 7-cyano-7-deazaguanine
Other name(s): tRNA transglycosylase (ambiguous); transfer ribonucleate glycosyltransferase (ambiguous); tRNA guanine15 transglycosidase; TGT (ambiguous); transfer ribonucleic acid guanine15 transglycosylase
Systematic name: tRNA-guanine15:7-cyano-7-carbaguanine tRNA-D-ribosyltransferase
Comments: Archaeal tRNAs contain the modified nucleoside archaeosine at position 15. This archaeal enzyme catalyses the exchange of guanine at position 15 of tRNA with the base preQ0, which is ultimately modified to form the nucleoside archaeosine (cf. EC 2.6.1.97) [1].
Links to other databases:
BRENDA,
EXPASY,
KEGG,
Metacyc,
CAS registry number:
References:
1. Bai, Y., Fox, D.T., Lacy, J.A., Van Lanen, S.G. and Iwata-Reuyl, D. Hypermodification of tRNA in thermophilic archaea. Cloning, overexpression, and characterization of tRNA-guanine transglycosylase from Methanococcus jannaschii. J. Biol. Chem. 275 (2000) 28731-28738. [PMID: 10862614]
Accepted name: neamine phosphoribosyltransferase
Reaction: neamine + 5-phospho-α-D-ribose 1-diphosphate = 5''-phosphoribostamycin + diphosphate
For diagram of reaction click here.
Glossary: neamine = (2R,3S,4R,5R,6R)-5-amino-2-(aminomethyl)-6-{[(1R,2R,3S,4R,6S)-4,6-diamino-2,3-dihydroxycyclohexyl]oxy}oxane-3,4-diol
Other name(s): btrL (gene name); neoM (gene name)
Systematic name: neamine:5-phospho-α-D-ribose 1-diphosphate phosphoribosyltransferase
Comments: Involved in the biosynthetic pathways of several clinically important aminocyclitol antibiotics, including ribostamycin, neomycin and butirosin. The enzyme requires a divalent metal ion, optimally Mg2+, Ni2+ or Co2+.
Links to other databases:
BRENDA,
EXPASY,
KEGG,
Metacyc,
CAS registry number:
References:
1. Kudo, F., Fujii, T., Kinoshita, S. and Eguchi, T. Unique O-ribosylation in the biosynthesis of butirosin. Bioorg. Med. Chem. 15 (2007) 4360-4368. [PMID: 17482823]
Accepted name: cyanidin 3-O-galactoside 2''-O-xylosyltransferase
Reaction: UDP-α-D-xylose + cyanidin 3-O-β-D-galactoside = UDP + cyanidin 3-O-(β-D-xylosyl-(1→2)-β-D-galactoside)
For diagram of reaction click here.
Glossary: cyanidin = 3,3',4',5,7-pentahydroxyflavylium
Other name(s): CGXT
Systematic name: UDP-α-D-xylose:cyanidin-3-O-β-D-galactoside 2''-O-xylosyltransferase
Comments: Isolated from the plant Daucus carota (Afghan cultivar carrot).
Links to other databases:
BRENDA,
EXPASY,
KEGG,
Metacyc,
CAS registry number:
References:
1. Rose, A., Glassgen, W.E., Hopp, W. and Seitz, H.U. Purification and characterization of glycosyltransferases involved in anthocyanin biosynthesis in cell-suspension cultures of Daucus carota L. Planta 198 (1996) 397-403. [PMID: 8717136]
Accepted name: anthocyanidin 3-O-glucoside 2'''-O-xylosyltransferase
Reaction: UDP-α-D-xylose + an anthocyanidin 3-O-β-D-glucoside = UDP + an anthocyanidin 3-O-β-D-sambubioside
For diagram of reaction click here.
Glossary: anthocyanidin 3-O-β-D-sambubioside = anthocyanidin 3-O-(β-D-xylosyl-(1→2)-β-D-glucoside)
Other name(s): uridine 5'-diphosphate-xylose:anthocyanidin 3-O-glucose-xylosyltransferase; UGT79B1
Systematic name: UDP-α-D-xylose:anthocyanidin-3-O-β-D-glucoside 2'''-O-xylosyltransferase
Comments: Isolated from the plants Matthiola incana (stock) [1] and Arabidopsis thaliana (mouse-eared cress) [2]. The enzyme has similar activity with the 3-glucosides of pelargonidin, cyanidin, delphinidin, quercetin and kaempferol as well as with cyanidin 3-O-rhamnosyl-(1→6)-glucoside and cyanidin 3-O-(6-acylglucoside). There is no activity with other UDP-sugars or with cyanidin 3,5-diglucoside.
Links to other databases:
BRENDA,
EXPASY,
KEGG,
Metacyc,
CAS registry number:
References:
1. Teusch, M. Uridine 5'-diphosphate-xylose:anthocyanidin 3-O-glucose-xylosyltransferase from petals of Matthiola incana R.Br. Planta 169 (1986) 559-563.
2. Yonekura-Sakakibara, K., Fukushima, A., Nakabayashi, R., Hanada, K., Matsuda, F., Sugawara, S., Inoue, E., Kuromori, T., Ito, T., Shinozaki, K., Wangwattana, B., Yamazaki, M. and Saito, K. Two glycosyltransferases involved in anthocyanin modification delineated by transcriptome independent component analysis in Arabidopsis thaliana. Plant J. 69 (2012) 154-167. [PMID: 21899608]
Accepted name: triphosphoribosyl-dephospho-CoA synthase
Reaction: ATP + 3'-dephospho-CoA = 2'-(5-triphospho-α-D-ribosyl)-3'-dephospho-CoA + adenine
For diagram of reaction click here.
Other name(s): 2'-(5''-triphosphoribosyl)-3-dephospho-CoA synthase; ATP:dephospho-CoA 5-triphosphoribosyl transferase; CitG; ATP:dephospho-CoA 5'-triphosphoribosyl transferase; MdcB; ATP:3-dephospho-CoA 5''-triphosphoribosyltransferase; MadG
Systematic name: ATP:3'-dephospho-CoA 5-triphosphoribosyltransferase
Comments: ATP cannot be replaced by GTP, CTP, UTP, ADP or AMP. The reaction involves the formation of a new α (1''→2') glycosidic bond between the two ribosyl moieties, with concomitant displacement of the adenine moiety of ATP [1,4]. The 2'-(5-triphosphoribosyl)-3'-dephospho-CoA produced can be transferred by EC 2.7.7.61, citrate lyase holo-[acyl-carrier protein] synthase, to the apo-acyl-carrier protein subunit (γ-subunit) of EC 4.1.3.6, citrate (pro-3S) lyase, thus converting it from an apo-enzyme into a holo-enzyme [1,3]. Alternatively, it can be transferred to the apo-ACP subunit of malonate decarboxylase by the action of EC 2.7.7.66, malonate decarboxylase holo-[acyl-carrier protein] synthase [4].
Links to other databases:
BRENDA,
EXPASY,
KEGG,
Metacyc,
CAS registry number: 313345-38-9
References:
1. Schneider, K., Dimroth, P. and Bott, M. Biosynthesis of the prosthetic group of citrate lyase. Biochemistry 39 (2000) 9438-9450. [PMID: 10924139]
2. Schneider, K., Dimroth, P. and Bott, M. Identification of triphosphoribosyl-dephospho-CoA as precursor of the citrate lyase prosthetic group. FEBS Lett. 483 (2000) 165-168. [PMID: 11042274]
3. Schneider, K., Kästner, C.N., Meyer, M., Wessel, M., Dimroth, P. and Bott, M. Identification of a gene cluster in Klebsiella pneumoniae which includes citX, a gene required for biosynthesis of the citrate lyase prosthetic group. J. Bacteriol. 184 (2002) 2439-2446. [PMID: 11948157]
4. Hoenke, S., Wild, M.R. and Dimroth, P. Biosynthesis of triphosphoribosyl-dephospho-coenzyme A, the precursor of the prosthetic group of malonate decarboxylase. Biochemistry 39 (2000) 13223-13232. [PMID: 11052675]
Accepted name: undecaprenyl-phosphate 4-deoxy-4-formamido-L-arabinose transferase
Reaction: UDP-4-deoxy-4-formamido-β-L-arabinopyranose + ditrans,octacis-undecaprenyl phosphate = UDP + 4-deoxy-4-formamido-α-L-arabinopyranosyl ditrans,octacis-undecaprenyl phosphate
For diagram of reaction click here.
Other name(s): undecaprenyl-phosphate Ara4FN transferase; Ara4FN transferase; polymyxin resistance protein PmrF; UDP-4-amino-4-deoxy-α-L-arabinose:ditrans,polycis-undecaprenyl phosphate 4-amino-4-deoxy-α-L-arabinosyltransferase
Systematic name: UDP-4-amino-4-deoxy-α-L-arabinose:ditrans,octacis-undecaprenyl phosphate 4-amino-4-deoxy-α-L-arabinosyltransferase
Comments: The enzyme shows no activity with UDP-4-amino-4-deoxy-β-L-arabinose.
Links to other databases:
BRENDA,
EXPASY,
KEGG,
Metacyc,
CAS registry number:
References:
1. Breazeale, S.D., Ribeiro, A.A. and Raetz, C.R. Oxidative decarboxylation of UDP-glucuronic acid in extracts of polymyxin-resistant Escherichia coli. Origin of lipid a species modified with 4-amino-4-deoxy-L-arabinose. J. Biol. Chem. 277 (2002) 2886-2896. [PMID: 11706007]
2. Breazeale, S.D., Ribeiro, A.A., McClerren, A.L. and Raetz, C.R.H. A formyltransferase required for polymyxin resistance in Escherichia coli and the modification of lipid A with 4-amino-4-deoxy-L-arabinose. Identification and function of UDP-4-deoxy-4-formamido-L-arabinose. J. Biol. Chem. 280 (2005) 14154-14167. [PMID: 15695810]
Accepted name: β-ribofuranosylphenol 5'-phosphate synthase
Reaction: 5-phospho-α-D-ribose 1-diphosphate + 4-hydroxybenzoate = 4-(β-D-ribofuranosyl)phenol 5'-phosphate + CO2 + diphosphate
For diagram of reaction click here.
Other name(s): β-RFAP synthase (incorrect); β-RFA-P synthase (incorrect); AF2089 (gene name); MJ1427 (gene name); 4-(β-D-ribofuranosyl)aminobenzene 5'-phosphate synthase (incorrect); β-ribofuranosylaminobenzene 5'-phosphate synthase (incorrect); 5-phospho-α-D-ribose 1-diphosphate:4-aminobenzoate 5-phospho-β-D-ribofuranosyltransferase (decarboxylating) (incorrect)
Systematic name: 5-phospho-α-D-ribose-1-diphosphate:4-hydroxybenzoate 5-phospho-β-D-ribofuranosyltransferase (decarboxylating)
Comments: The enzyme is involved in biosynthesis of tetrahydromethanopterin in archaea. It can utilize both 4-hydroxybenzoate and 4-aminobenzoate as substrates, but only the former is known to be produced by methanogenic archaea [4]. The activity is dependent on Mg2+ or Mn2+ [1]
Links to other databases:
BRENDA,
EXPASY,
KEGG,
MetaCyc,
CAS registry number:
References:
1. Rasche, M.E. and White, R.H. Mechanism for the enzymatic formation of 4-(β-D-ribofuranosyl)aminobenzene 5'-phosphate during the biosynthesis of methanopterin. Biochemistry 37 (1998) 11343-11351. [PMID: 9698382]
2. Scott, J.W. and Rasche, M.E. Purification, overproduction, and partial characterization of β-RFAP synthase, a key enzyme in the methanopterin biosynthesis pathway. J. Bacteriol. 184 (2002) 4442-4448. [PMID: 12142414]
3. Dumitru, R.V. and Ragsdale, S.W. Mechanism of 4-(β-D-ribofuranosyl)aminobenzene 5'-phosphate synthase, a key enzyme in the methanopterin biosynthetic pathway. J. Biol. Chem. 279 (2004) 39389-39395. [PMID: 15262968]
4. White, R.H. The conversion of a phenol to an aniline occurs in the biochemical formation of the 1-(4-aminophenyl)-1-deoxy-D-ribitol moiety in methanopterin. Biochemistry 50 (2011) 6041-6052. [PMID: 21634403]
5. Bechard, M.E., Farahani, P., Greene, D., Pham, A., Orry, A. and Rasche, M.E. Purification, kinetic characterization, and site-directed mutagenesis of Methanothermobacter thermautotrophicus RFAP synthase produced in Escherichia coli. AIMS Microbiol 5 (2019) 186–204. [PMID: 31663056]
Accepted name: nicotinate D-ribonucleotide:phenol phospho-D-ribosyltransferase
Reaction: nicotinate D-ribonucleotide + phenol = nicotinate + phenyl 5-phospho-α-D-ribofuranoside
Other name(s): ArsAB
Systematic name: nicotinate D-ribonucleotide:phenol phospho-D-ribosyltransferase
Comments: The enzyme is involved in the biosynthesis of phenolic cobamides in the Gram-positive bacterium Sporomusa ovata. It can also transfer the phospho-D-ribosyl group to 4-methylphenol and 5,6-dimethylbenzimidazole. The related EC 2.4.2.21, nicotinate-nucleotide dimethylbenzimidazole phosphoribosyltransferase, also transfers the phospho-D-ribosyl group from nicotinate D-ribonucleotide to 5,6-dimethylbenzimidazole, but shows no activity with 4-methylphenol or phenol.
Links to other databases:
BRENDA,
EXPASY,
KEGG,
Metacyc,
CAS registry number:
References:
1. Chan, C.H. and Escalante-Semerena, J.C. ArsAB, a novel enzyme from Sporomusa ovata activates phenolic bases for adenosylcobamide biosynthesis. Mol. Microbiol. 81 (2011) 952-967. [PMID: 21696461]
Accepted name: kaempferol 3-O-xylosyltransferase
Reaction: UDP-α-D-xylose + kaempferol = UDP + kaempferol 3-O-β-D-xyloside
For diagram of reaction, click here
Other name(s): F3XT; UDP-D-xylose:flavonol 3-O-xylosyltransferase; flavonol 3-O-xylosyltransferase
Systematic name: UDP-α-D-xylose:kaempferol 3-O-D-xylosyltransferase
Comments: The enzyme from the plant Euonymus alatus also catalyses the 3-O-D-xylosylation of other flavonols (e.g. quercetin, isorhamnetin, rhamnetin, myricetin, fisetin) with lower activity.
Links to other databases:
BRENDA,
EXPASY,
KEGG,
Metacyc,
CAS registry number:
References:
1. Ishikura, N. and Yang, Z.Q. UDP-D-xylose: flavonol 3-O-xylosyltransferase from young leaves of Euonymus alatus f. ciliato-dentatus. Z. Naturforsch. C: Biosci. 46 (1991) 1003-1010.
Accepted name: AMP phosphorylase
Reaction: (1) AMP + phosphate = adenine + α-D-ribose 1,5-bisphosphate
For diagram of reaction click here.
Other name(s): AMPpase; nucleoside monophosphate phosphorylase; deoA (gene name)
Systematic name: AMP:phosphate α-D-ribosyl 5'-phosphate-transferase
Comments: The enzyme from archaea is involved in AMP metabolism and CO2 fixation through type III RubisCO enzymes. The activity with CMP and UMP requires activation by cAMP [2].
Links to other databases:
BRENDA,
EXPASY,
KEGG,
MetaCyc,
PDB,
CAS registry number:
References:
1. Sato, T., Atomi, H. and Imanaka, T. Archaeal type III RuBisCOs function in a pathway for AMP metabolism. Science 315 (2007) 1003-1006. [PMID: 17303759]
2. Aono, R., Sato, T., Yano, A., Yoshida, S., Nishitani, Y., Miki, K., Imanaka, T. and Atomi, H. Enzymatic characterization of AMP phosphorylase and ribose-1,5-bisphosphate isomerase functioning in an archaeal AMP metabolic pathway. J. Bacteriol. 194 (2012) 6847-6855. [PMID: 23065974]
3. Nishitani, Y., Aono, R., Nakamura, A., Sato, T., Atomi, H., Imanaka, T. and Miki, K. Structure analysis of archaeal AMP phosphorylase reveals two unique modes of dimerization. J. Mol. Biol. (2013) . [PMID: 23659790]
Accepted name: hydroxyproline O-arabinosyltransferase
Reaction: UDP-β-L-arabinofuranose + [protein]-trans-4-hydroxy-L-proline = UDP + [protein]-O-(β-L-arabinofuranosyl)-trans-4-hydroxy-L-proline
Glossary: trans-4-hydroxy-L-proline = (2S,4R)-4-hydroxyproline = (4R)-4-hydroxy-L-proline
Other name(s): HPAT
Systematic name: UDP-β-L-arabinofuranose:[protein]-trans-4-hydroxy-L-proline L-arabinofuranosyl transferase (configuration-retaining)
Comments: The enzyme, found in plants and mosses, catalyses the O-arabinosylation of hydroxyprolines in hydroxyproline-rich glycoproteins. The enzyme acts on the first hydroxyproline in the motif Val-hydroxyPro-hydroxyPro-Ser.
Links to other databases:
BRENDA,
EXPASY,
KEGG,
MetaCyc,
CAS registry number:
References:
1. Ogawa-Ohnishi, M., Matsushita, W. and Matsubayashi, Y. Identification of three hydroxyproline O-arabinosyltransferases in Arabidopsis thaliana. Nat. Chem. Biol. 9 (2013) 726-730. [PMID: 24036508]
Accepted name: sulfide-dependent adenosine diphosphate thiazole synthase
Reaction: NAD+ + glycine + sulfide = nicotinamide + ADP-5-ethyl-4-methylthiazole-2-carboxylate + 3 H2O
Other name(s): Thi4 (ambiguous)
Systematic name: NAD+:glycine ADP-D-ribosyltransferase (sulfide-adding)
Comments: This iron dependent enzyme, found in most archaea, is involved in the biosynthesis of thiamine phosphate. The homologous enzyme from plants and fungi (EC 2.4.2.60, cysteine-dependent adenosine diphosphate thiazole synthase) uses an intrinsic cysteine as sulfur donor and, unlike the archaeal enzyme, is a single turn-over enzyme.
Links to other databases:
BRENDA,
EXPASY,
KEGG,
MetaCyc,
PDB,
CAS registry number:
References:
1. Zhang, X., Eser, B.E., Chanani, P.K., Begley, T.P. and Ealick, S.E. Structural basis for iron-mediated sulfur transfer in archael and yeast thiazole synthases. Biochemistry 55 (2016) 1826-1838. [PMID: 26919468]
2. Eser, B.E., Zhang, X., Chanani, P.K., Begley, T.P. and Ealick, S.E. From suicide enzyme to catalyst: the iron-dependent sulfide transfer in Methanococcus jannaschii thiamin thiazole biosynthesis. J. Am. Chem. Soc. 138 (2016) 3639-3642. [PMID: 26928142]
Accepted name: cysteine-dependent adenosine diphosphate thiazole synthase
Reaction: NAD+ + glycine + [ADP-thiazole synthase]-L-cysteine = nicotinamide + ADP-5-ethyl-4-methylthiazole-2-carboxylate + [ADP-thiazole synthase]-dehydroalanine + 3 H2O
Other name(s): THI4 (gene name) (ambiguous); THI1 (gene name); ADP-thiazole synthase
Systematic name: NAD+:glycine ADP-D-ribosyltransferase (dehydroalanine-producing)
Comments: This iron dependent enzyme, found in fungi, plants, and some archaea, is involved in the thiamine phosphate biosynthesis pathway. It is a single turn-over enzyme since the cysteine residue is not regenerated in vivo [3]. The homologous enzyme in archaea (EC 2.4.2.59, sulfide-dependent adenosine diphosphate thiazole synthase) uses sulfide as sulfur donor.
Links to other databases:
BRENDA,
EXPASY,
KEGG,
MetaCyc,
PDB,
CAS registry number:
References:
1. Godoi, P.H., Galhardo, R.S., Luche, D.D., Van Sluys, M.A., Menck, C.F. and Oliva, G. Structure of the thiazole biosynthetic enzyme THI1 from Arabidopsis thaliana. J. Biol. Chem. 281 (2006) 30957-30966. [PMID: 16912043]
2. Chatterjee, A., Abeydeera, N.D., Bale, S., Pai, P.J., Dorrestein, P.C., Russell, D.H., Ealick, S.E. and Begley, T.P. Saccharomyces cerevisiae THI4p is a suicide thiamine thiazole synthase. Nature 478 (2011) 542-546. [PMID: 22031445]
3. Zhang, X., Eser, B.E., Chanani, P.K., Begley, T.P. and Ealick, S.E. Structural basis for iron-mediated sulfur transfer in archael and yeast thiazole synthases. Biochemistry 55 (2016) 1826-1838. [PMID: 26919468]
4. Hwang, S., Cordova, B., Chavarria, N., Elbanna, D., McHugh, S., Rojas, J., Pfeiffer, F. and Maupin-Furlow, J.A. Conserved active site cysteine residue of archaeal THI4 homolog is essential for thiamine biosynthesis in Haloferax volcanii. BMC Microbiol. 14 (2014) 260. [PMID: 25348237]
Accepted name: α-dystroglycan β1,4-xylosyltransferase
Reaction: UDP-α-D-xylose + 3-O-[Rib-ol-P-Rib-ol-P-3-β-D-GalNAc-(1→3)-β-D-GlcNAc-(1→4)-O-6-P-α-D-Man]-Ser/Thr-[protein] = UDP + 3-O-[β-D-Xyl-(1→4)-Rib-ol-P-Rib-ol-P-3-β-D-GalNAc-(1→3)-β-D-GlcNAc-(1→4)-O-6-P-α-D-Man]-Ser/Thr-[protein]
Other name(s): TMEM5 (gene name)
Systematic name: UDP-α-D-xylose:3-O-[Rib-ol-P-Rib-ol-P-3-β-D-GalNAc-(1→3)-β-D-GlcNAc-(1→4)-O-6-P-α-D-Man]-Ser/Thr-[protein] xylosyltransferase
Comments: This eukaryotic enzyme catalyses a step in the biosynthesis of the glycan moiety of the membrane protein α-dystroglycan. It is specific for the second ribitol 5-phosphate in the nascent glycan chain as acceptor.
Links to other databases:
BRENDA,
EXPASY,
KEGG,
Metacyc,
CAS registry number:
References:
1. Vuillaumier-Barrot, S., Bouchet-Seraphin, C., Chelbi, M., Devisme, L., Quentin, S., Gazal, S., Laquerriere, A., Fallet-Bianco, C., Loget, P., Odent, S., Carles, D., Bazin, A., Aziza, J., Clemenson, A., Guimiot, F., Bonniere, M., Monnot, S., Bole-Feysot, C., Bernard, J.P., Loeuillet, L., Gonzales, M., Socha, K., Grandchamp, B., Attie-Bitach, T., Encha-Razavi, F. and Seta, N. Identification of mutations in TMEM5 and ISPD as a cause of severe cobblestone lissencephaly. Am J Hum Genet 91 (2012) 1135-1143. [PMID: 23217329]
2. Manya, H., Yamaguchi, Y., Kanagawa, M., Kobayashi, K., Tajiri, M., Akasaka-Manya, K., Kawakami, H., Mizuno, M., Wada, Y., Toda, T. and Endo, T. The muscular dystrophy gene TMEM5 encodes a ribitol β1,4-xylosyltransferase required for the functional glycosylation of dystroglycan. J. Biol. Chem. 291 (2016) 24618-24627. [PMID: 27733679]
Accepted name: xylosyl α-1,3-xylosyltransferase
Reaction: UDP-α-D-xylose + [protein with EGF-like domain]-3-O-[α-D-xylosyl-(1→3)-β-D-glucosyl]-L-serine = UDP + [protein with EGF-like domain]-3-O-[α-D-xylosyl-(1→3)-α-D-xylosyl-(1→3)-β-D-glucosyl]-L-serine
Other name(s): XXYLT1 (gene name)
Systematic name: UDP-α-D-xylose:[EGF-like domain protein]-3-O-[α-D-xylosyl-(1→3)-β-D-glucosyl]-L-serine 3-α-D-xylosyltransferase (configuration-retaining)
Comments: The enzyme, found in animals and insects, is involved in the biosynthesis of the α-D-xylosyl-(1→3)-α-D-xylosyl-(1→3)-β-D-glucosyl trisaccharide on epidermal growth factor-like (EGF-like) domains. When present on Notch proteins, the trisaccharide functions as a modulator of the signalling activity of this protein.
Links to other databases:
BRENDA,
EXPASY,
KEGG,
MetaCyc,
PDB,
CAS registry number:
References:
1. Minamida, S., Aoki, K., Natsuka, S., Omichi, K., Fukase, K., Kusumoto, S. and Hase, S. Detection of UDP-D-xylose: α-D-xyloside α 1-→3xylosyltransferase activity in human hepatoma cell line HepG2. J. Biochem. 120 (1996) 1002-1006. [PMID: 8982869]
2. Sethi, M.K., Buettner, F.F., Ashikov, A., Krylov, V.B., Takeuchi, H., Nifantiev, N.E., Haltiwanger, R.S., Gerardy-Schahn, R. and Bakker, H. Molecular cloning of a xylosyltransferase that transfers the second xylose to O-glucosylated epidermal growth factor repeats of notch. J. Biol. Chem. 287 (2012) 2739-2748. [PMID: 22117070]
3. Yu, H., Takeuchi, M., LeBarron, J., Kantharia, J., London, E., Bakker, H., Haltiwanger, R.S., Li, H. and Takeuchi, H. Notch-modifying xylosyltransferase structures support an SNi-like retaining mechanism. Nat. Chem. Biol. 11 (2015) 847-854. [PMID: 26414444]
Accepted name: EGF-domain serine xylosyltransferase
Reaction: UDP-α-D-xylose + [protein with EGF-like domain]-L-serine = UDP + [protein with EGF-like domain]-3-O-(β-D-xylosyl)-L-serine
Other name(s): POGLUT1 (gene name) (ambiguous); rumi (gene name) (ambiguous)
Systematic name: UDP-α-D-xylose:[protein with EGF-like domain]-L-serine O-β-xylosyltransferase (configuration-inverting)
Comments: The enzyme, found in animals and insects, xylosylates at the serine in the C-X-S-X-P-C motif of epidermal growth factor-like (EGF-like) domains. The enzyme is bifunctional also being active with UDP-α-glucose as donor (EC 2.4.1.376, EGF-domain serine glucosyltransferase).
Links to other databases:
BRENDA,
EXPASY,
KEGG,
MetaCyc,
PDB,
CAS registry number:
References:
1. Li, Z., Fischer, M., Satkunarajah, M., Zhou, D., Withers, S.G. and Rini, J.M. Structural basis of Notch O-glucosylation and O-xylosylation by mammalian protein-O-glucosyltransferase 1 (POGLUT1). Nat. Commun. 8 (2017) 185. [PMID: 28775322]
Accepted name: tRNA-guanosine34 queuine transglycosylase
Reaction: guanine34 in tRNA + queuine = queuine34 in tRNA + guanine
For diagram of reaction click here
Glossary: queuine = base Q = 2-amino-5-({[(1S,4S,5R)-4,5-dihydroxycyclopent-2-en-1-yl]amino}methyl)-1,7-dihydropyrrolo[3,2-e]pyrimidin-4-one
Other name(s): QTRT1 (gene name); QTRT2 (gene name); TGT (ambiguous); guanine insertion enzyme (ambiguous); tRNA transglycosylase (ambiguous); Q-insertase (ambiguous); queuine34 transfer ribonucleate ribosyltransferase; transfer ribonucleate glycosyltransferase (ambiguous); tRNA guanine34 transglycosidase (ambiguous); queuine tRNA-ribosyltransferase; [tRNA]-guanine34:queuine tRNA-D-ribosyltransferase; transfer ribonucleic acid guanine34 transglycosylase (ambiguous)
Systematic name: tRNA-guanosine34:queuine tRNA-D-ribosyltransferase
Comments: Certain prokaryotic and eukaryotic tRNAs contain the modified base queuine at position 34. In eukaryotes and a small number of prokaryotes queuine is salvaged and incorporated into tRNA directly via a base-exchange reaction, replacing guanine. cf. EC 2.4.2.29, tRNA-guanosine34 preQ1 transglycosylase.
Links to other databases:
BRENDA,
EXPASY,
KEGG,
MetaCyc,
CAS registry number:
References:
1. Howes, N.K. and Farkas, W.R. Studies with a homogeneous enzyme from rabbit erythrocytes catalyzing the insertion of guanine into tRNA. J. Biol. Chem. 253 (1978) 9082-9087. [PMID: 721832]
2. Shindo-Okada, N., Okada, N., Ohgi, T., Goto, T. and Nishimura, S. Transfer ribonucleic acid guanine transglycosylase isolated from rat liver. Biochemistry 19 (1980) 395-400. [PMID: 6986171]
3. Boland, C., Hayes, P., Santa-Maria, I., Nishimura, S. and Kelly, V.P. Queuosine formation in eukaryotic tRNA occurs via a mitochondria-localized heteromeric transglycosylase. J. Biol. Chem. 284 (2009) 18218-18227. [PMID: 19414587]
4. Yuan, Y., Zallot, R., Grove, T.L., Payan, D.J., Martin-Verstraete, I., Sepic, S., Balamkundu, S., Neelakandan, R., Gadi, V.K., Liu, C.F., Swairjo, M.A., Dedon, P.C., Almo, S.C., Gerlt, J.A. and de Crecy-Lagard, V. Discovery of novel bacterial queuine salvage enzymes and pathways in human pathogens. Proc. Natl. Acad. Sci. USA 116 (2019) 19126-19135. [PMID: 31481610]
β-D-apiose = (2R,3R,4R)-4-(hydroxymethyl)tetrahydrofuran-2,3,4-triol
7-cyano-7-carbaguanine = preQ0 = 7-cyano-7-deazaguanine
(2) 4-amino-4-deoxy-α-L-arabinopyranosyl ditrans,octacis-undecaprenyl phosphate + lipid IVA = lipid IIA + ditrans,octacis-undecaprenyl phosphate
(3) 4-amino-4-deoxy-α-L-arabinopyranosyl ditrans,octacis-undecaprenyl phosphate + α-Kdo-(2→4)-α-Kdo-(2→6)-lipid IVA = 4'-α-L-Ara4N-α-Kdo-(2→4)-α-Kdo-(2→6)-lipid IVA + ditrans,octacis-undecaprenyl phosphate
lipid IIA = 4-amino-4-deoxy-β-L-arabinopyranosyl 2-deoxy-2-{[(3R)-3-hydroxytetradecanoyl]amino}-3-O-[(3R)-3-hydroxytetradecanoyl]-4-O-phospho-β-D-glucopyranosyl-(1→6)-2-deoxy-3-O-[(3R)-3-hydroxytetradecanoyl]-2-{[(3R)-3-hydroxytetradecanoyl]amino}-α-D-glucopyranosyl phosphate
α-Kdo-(2→4)-α-Kdo-(2→6)-lipid IVA = (3-deoxy-α-D-manno-oct-2-ulopyranosylonate)-(2→4)-(3-deoxy-α-D-manno-oct-2-ulopyranosylonate)-(2→6)-2-deoxy-2-{[(3R)-3-hydroxytetradecanoyl]amino}-3-O-[(3R)-3-hydroxytetradecanoyl]-4-O-phosphono-β-D-glucopyranosyl-(1→6)-2-deoxy-3-O-[(3R)-3-hydroxytetradecanoyl]-2-{[(3R)-3-hydroxytetradecanoyl]amino}-1-O-phosphono-α-D-glucopyranose
4'-α-L-Ara4N-α-Kdo-(2→4)-α-Kdo-(2→6)-lipid IVA = 4-amino-4-deoxy-α-L-arabinopyranosyl 2-deoxy-2-[(3R)-3-hydroxytetradecanamido]-3-O-[(3R)-3-hydroxytetradecanoyl]-4-phospho-β-D-glucopyranosy-(1→6)-2-deoxy-2-[(3R)-3-hydroxytetradecanamido]-3-O-[(3R)-3-hydroxytetradecanoyl]-α-D-glucopyranosyl phosphate
lipid A = lipid A of Escherichia coli = 2-deoxy-2-{[(3R)-3-(dodecanoyloxy)tetradecanoyl]amino}-3-O-[(3R)-3-(tetradecanoyloxy)tetradecanoyl]-4-O-phospho-β-D-glucopyranosyl-(1→6)-2-deoxy-3-O-[(3R)-3-hydroxytetradecanoyl]-2-{[(3R)-3-hydroxytetradecanoyl]amino}-1-O-phospho-α-D-glucopyranose
α-Kdo-(2→4)-α-Kdo-(2→6)-lipid A = (3-deoxy-α-D-manno-oct-2-ulopyranosylonate)-(2→4)-(3-deoxy-α-D-manno-oct-2-ulopyranosylonate)-(2→6)-2-deoxy-2-{[(3R)-3-(dodecanoyloxy)tetradecanoyl]amino}-3-O-[(3R)-3-(tetradecanoyloxy)tetradecanoyl]-4-O-phospho-β-D-glucopyranosyl-(1→6)-2-deoxy-3-O-[(3R)-3-hydroxytetradecanoyl]-2-{[(3R)-3-hydroxytetradecanoyl]amino}-1-O-phospho-α-D-glucopyranose
α-Kdo-(2→4)-α-Kdo-(2→6)-[4'-P-α-L-Ara4N]-lipid A = (3-deoxy-α-D-manno-oct-2-ulopyranosylonate)-(2→4)-(3-deoxy-α-D-manno-oct-2-ulopyranosylonate)-(2→6)-2-deoxy-2-{[(3R)-3-(dodecanoyloxy)tetradecanoyl]amino}-3-O-[(3R)-3-(tetradecanoyloxy)tetradecanoyl]-4-O-(4-amino-4-deoxy-α-L-arabinopyranosyl)phospho-β-D-glucopyranosyl-(1→6)-2-deoxy-3-O-[(3R)-3-hydroxytetradecanoyl]-2-{[(3R)-3-hydroxytetradecanoyl]amino}-1-O-phospho-α-D-glucopyranose
archaeosine = G* = 7-amidino-7-deazaguanosine
ribostamycin = (2R,3S,4R,5R,6R)-5-amino-2-(aminomethyl)-6-{[(1R,2R,3S,4R,6S)-4,6-diamino-2-{[(2S,3R,4S,5R)-3,4-dihydroxy-5-(hydroxymethyl)oxolan-2-yl]oxy}-3-hydroxycyclohexyl]oxy}oxane-3,4-diol
(2) CMP + phosphate = cytosine + α-D-ribose 1,5-bisphosphate
(3) UMP + phosphate = uracil + α-D-ribose 1,5-bisphosphate
Continued with EC 2.4.3
Return to EC 2 home page
Return to Enzymes home page
Return to IUBMB Biochemical Nomenclature home page