Continued from EC 2.1.1.251 to EC 2.1.1.396
EC 2.1.2 Hydroxymethyl-, Formyl- and Related Transferases
EC 2.1.3 Carboxy- and Carbamoyltransferases
EC 2.1.4 Amidinotransferases
EC 2.2 Transferring Aldehyde or Ketonic Groups
EC 2.2.1 Transketolases and Transaldolases
('Hydroxymethyltransferase', 'formyltransferase', 'formiminotransferase' may be replaced by 'transhydroxymethylase', 'transformylase' and 'trans-formiminase', respectively).
Accepted name: glycine hydroxymethyltransferase
Reaction: 5,10-methylenetetrahydrofolate + glycine + H2O = tetrahydrofolate + L-serine
For diagram of reaction click here.
Other name(s): serine aldolase; threonine aldolase; serine hydroxymethylase; serine hydroxymethyltransferase; allothreonine aldolase; L-serine hydroxymethyltransferase; L-threonine aldolase; serine hydroxymethyltransferase; serine transhydroxymethylase
Systematic name: 5,10-methylenetetrahydrofolate:glycine hydroxymethyltransferase
Comments: A pyridoxal-phosphate protein. Also catalyses the reaction of glycine with acetaldehyde to form L-threonine, and with 4-trimethylammoniobutanal to form 3-hydroxy-N6,N6,N6-trimethyl-L-lysine.
Links to other databases: BRENDA, EXPASY, GTD, KEGG, Metacyc, PDB, CAS registry number: 9029-83-8
References:
1. Akhtar, M. and El-Obeid, H.A. Inactivation of serine transhydroxymethylase and threonine aldolase activities. Biochim. Biophys. Acta 258 (1972) 791-799. [PMID: 5017703]
2. Blakley, R.L. A spectrophotometric study of the reaction catalysed by serine transhydroxymethylase. Biochem. J. 77 (1960) 459-465.
3. Fujioka, M. Purification and properties of serine hydroxymethylase from soluble and mitochondrial fractions of rabbit liver. Biochim. Biophys. Acta 185 (1969) 338-349. [PMID: 5808700]
4. Kumagai, H., Nagate, T., Yoshida, H. and Yamada, H. Threonine aldolase from Candida humicola. II. Purification, crystallization and properties. Biochim. Biophys. Acta 258 (1972) 779-790. [PMID: 5017702]
5. Schirch, L.V. and Gross, T. Serine transhydroxymethylase. Identification as the threonine and allothreonine aldolases. J. Biol. Chem. 243 (1968) 5651-5655. [PMID: 5699057]
Accepted name: phosphoribosylglycinamide formyltransferase 1
Reaction: 10-formyltetrahydrofolate + N1-(5-phospho-D-ribosyl)glycinamide = tetrahydrofolate + N2-formyl-N1-(5-phospho-D-ribosyl)glycinamide
For diagram of reaction click here
Other name(s): 2-amino-N-ribosylacetamide 5'-phosphate transformylase; GAR formyltransferase; GAR transformylase; glycinamide ribonucleotide transformylase; GAR TFase; 5,10-methenyltetrahydrofolate:2-amino-N-ribosylacetamide ribonucleotide transformylase; purN (gene name); ADE8 (gene name); GART (gene name); 5'-phosphoribosylglycinamide transformylase; phosphoribosylglycinamide formyltransferase (ambiguous)
Systematic name: 10-formyltetrahydrofolate:5'-phosphoribosylglycinamide N-formyltransferase
Comments: Two enzymes are known to catalyse the third step in de novo purine biosynthesis. This enzyme utilizes 10-formyltetrahydrofolate as the formyl donor, while the other enzyme, EC 6.3.1.21, phosphoribosylglycinamide formyltransferase 2, utilizes formate. In vertebrates this activity is catalysed by a trifunctional enzyme that also catalyses the activities of EC 6.3.4.13, phosphoribosylamine—glycine ligase and EC 6.3.3.1, phosphoribosylformylglycinamidine cyclo-ligase.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 9032-02-4
References:
1. Hartman, S.C. and Buchanan, J.M. Biosynthesis of the purines. XXVI. The identification of the formyl donors of the transformylation reaction. J. Biol. Chem. 234 (1959) 1812-1816. [PMID: 13672969]
2. Smith, G.K., Benkovic, P.A. and Benkovic, S.J. L(–)-10-Formyltetrahydrofolate is the cofactor for glycinamide ribonucleotide transformylase from chicken liver. Biochemistry 20 (1981) 4034-4036. [PMID: 7284307]
3. Warren, L. and Buchanan, J.M. Biosynthesis of the purines. XIX. 2-Amino-N-ribosylacetamide 5'-phosphate (glycinamide ribotide) transformylase. J. Biol. Chem. 229 (1957) 613-626. [PMID: 13502326]
4. Schild, D., Brake, A.J., Kiefer, M.C., Young, D. and Barr, P.J. Cloning of three human multifunctional de novo purine biosynthetic genes by functional complementation of yeast mutations. Proc. Natl. Acad. Sci. USA 87 (1990) 2916-2920. [PMID: 2183217]
5. Zhang, Y., Desharnais, J., Greasley, S.E., Beardsley, G.P., Boger, D.L. and Wilson, I.A. Crystal structures of human GAR Tfase at low and high pH and with substrate β-GAR. Biochemistry 41 (2002) 14206-14215. [PMID: 12450384]
Accepted name: phosphoribosylaminoimidazolecarboxamide formyltransferase
Reaction: 10-formyltetrahydrofolate + 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide = tetrahydrofolate + 5-formamido-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide
For reaction pathway click here.
Other name(s): 5-amino-4-imidazolecarboxamide ribonucleotide transformylase; AICAR transformylase; 10-formyltetrahydrofolate:5'-phosphoribosyl-5-amino-4-imidazolecarboxamide formyltransferase; 5'-phosphoribosyl-5-amino-4-imidazolecarboxamide formyltransferase; 5-amino-1-ribosyl-4-imidazolecarboxamide 5'-phosphate transformylase; 5-amino-4-imidazolecarboxamide ribotide transformylase; AICAR formyltransferase; aminoimidazolecarboxamide ribonucleotide transformylase
Systematic name: 10-formyltetrahydrofolate:5'-phosphoribosyl-5-amino-4-imidazole-carboxamide N-formyltransferase
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 9032-03-5
References:
1. Hartman, S.C. and Buchanan, J.M. Biosynthesis of the purines. XXVI. The identification of the formyl donors of the transformylation reaction. J. Biol. Chem. 234 (1959) 1812-1816.
Accepted name: glycine formimidoyltransferase
Reaction: 5-formimidoyltetrahydrofolate + glycine = tetrahydrofolate + N-formimidoylglycine
For diagram of reaction click here.
Other name(s): formiminoglycine formiminotransferase; FIG formiminotransferase; glycine formiminotransferase
Systematic name: 5-formimidoyltetrahydrofolate:glycine N-formimidoyltransferase
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 9029-84-9
References:
1. Rabinowitz, J.C. and Pricer, W.E. Formiminotetrahydrofolic acid and methenyltetrahydrofolic acid as intermediates in the formation of N10-formyltetrahydrofolic acid. J. Am. Chem. Soc. 78 (1956) 5702-5704.
2. Rabinowitz, J.C. and Pricer, W.E. Formation, isolation and properties of 5-formiminotetrahydrofolic acid. Fed. Proc. 16 (1957) 236 only.
3. Sagers, R.D., Beck, J.V., Gruber, W. and Gunsalus, I.C. A tetrahydrofolic acid linked formimino transfer enzyme. J. Am. Chem. Soc. 78 (1956) 694-695.
Accepted name: glutamate formimidoyltransferase
Reaction: 5-formimidoyltetrahydrofolate + L-glutamate = tetrahydrofolate + N-formimidoyl-L-glutamate
For diagram click here.
Other name(s): FTCD (gene name); glutamate formyltransferase; formiminoglutamic acid transferase; formiminoglutamic formiminotransferase; glutamate formiminotransferase
Systematic name: 5-formimidoyltetrahydrofolate:L-glutamate N-formimidoyltransferase
Comments: The enzyme also catalyses formyl transfer from 5-formyltetrahydrofolate to L-glutamate (a reaction formerly listed as EC 2.1.2.6). In eukaryotes, it occurs as a bifunctional enzyme that also has formimidoyltetrahydrofolate cyclodeaminase (EC 4.3.1.4) activity.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 9032-83-1
References:
1. Miller, A. and Waelsch, H. Formimino transfer from formamidinoglutaric acid to tetrahydrofolic acid. J. Biol. Chem. 228 (1957) 397-417.
2. Silverman, M., Keresztesy, J.C., Koval, G.J. and Gardiner, R.C. Citrovorium factor and the synthesis of formylglutamic acid. J. Biol. Chem. 226 (1957) 83-94.
3. Tabor, H. and Wyngarden, L. The enzymatic formation of formiminotetrahydrofolic acid, 5,10-methenyltetrahydrofolic acid, and 10-formyltetrahydrofolic acid in the metabolism of formiminoglutamic acid. J. Biol. Chem. 234 (1959) 1830-1849.
4. Kohls, D., Sulea, T., Purisima, E.O., MacKenzie, R.E. and Vrielink, A. The crystal structure of the formiminotransferase domain of formiminotransferase-cyclodeaminase: implications for substrate channeling in a bifunctional enzyme. Structure 8 (2000) 35-46. [PMID: 10673422]
5. Mao, Y., Vyas, N.K., Vyas, M.N., Chen, D.H., Ludtke, S.J., Chiu, W. and Quiocho, F.A. Structure of the bifunctional and Golgi-associated formiminotransferase cyclodeaminase octamer. EMBO J. 23 (2004) 2963-2971. [PMID: 15272307]
6. Jeanguenin, L., Lara-Nunez, A., Pribat, A., Mageroy, M.H., Gregory, J.F., 3rd, Rice, K.C., de Crecy-Lagard, V. and Hanson, A.D. Moonlighting glutamate formiminotransferases can functionally replace 5-formyltetrahydrofolate cycloligase. J. Biol. Chem 285 (2010) 41557-41566. [PMID: 20952389]
[EC 2.1.2.6 Deleted entry: glutamate formyltransferase. Now included with EC 2.1.2.5 glutamate formiminotransferase. (EC 2.1.2.6 created 1965, deleted 1984)]
Accepted name: D-alanine 2-hydroxymethyltransferase
Reaction: 5,10-methylenetetrahydrofolate + D-alanine + H2O = tetrahydrofolate + 2-methylserine
Other name(s): 2-methylserine hydroxymethyltransferase
Systematic name: 5,10-methylenetetrahydrofolate:D-alanine 2-hydroxymethyltransferase
Comments: Also acts on 2-hydroxymethylserine.
Links to other databases: BRENDA, EXPASY, GTD, KEGG, Metacyc, CAS registry number: 9075-76-7
References:
1. Wilson, E.M. and Snell, E.E. Metabolism of α-methylserine. I. α-Methylserine hydroxymethyltransferase. J. Biol. Chem. 237 (1962) 3171-3179.
Accepted name: deoxycytidylate 5-hydroxymethyltransferase
Reaction: 5,10-methylenetetrahydrofolate + H2O + deoxycytidylate = tetrahydrofolate + 5-hydroxymethyldeoxycytidylate
Other name(s): dCMP hydroxymethylase; d-cytidine 5'-monophosphate hydroxymethylase; deoxyCMP hydroxymethylase; deoxycytidylate hydroxymethylase; deoxycytidylic hydroxymethylase
Systematic name: 5,10-methylenetetrahydrofolate:deoxycytidylate 5-hydroxymethyltransferase
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 9012-68-4
References:
1. Mathews, C.K., Brown, F. and Cohen, S.S. Virus-induced acquisition of metabolic function. VII. Biosynthesis de novo of deoxycytidylate hydroxymethylase. J. Biol. Chem. 239 (1964) 2957-2963.
Accepted name: methionyl-tRNA formyltransferase
Reaction: 10-formyltetrahydrofolate + L-methionyl-tRNAfMet = tetrahydrofolate + N-formylmethionyl-tRNAfMet
For diagram of reaction click here
Other name(s): N10-formyltetrahydrofolic-methionyl-transfer ribonucleic transformylase; formylmethionyl-transfer ribonucleic synthetase; methionyl ribonucleic formyltransferase; methionyl-tRNA Met formyltransferase; methionyl-tRNA transformylase; methionyl-transfer RNA transformylase; methionyl-transfer ribonucleate methyltransferase; methionyl-transfer ribonucleic transformylase
Systematic name: 10-formyltetrahydrofolate:L-methionyl-tRNA N-formyltransferase
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 9015-76-3
References:
1. Dickerman, H.W., Steers, E., Jr., Redfield, B.G. and Weissbach, H. Methionyl soluble ribonucleic acid transformylase. I. Purification and partial characterization. J. Biol. Chem. 242 (1967) 1522-1525. [PMID: 5337045]
Accepted name: aminomethyltransferase
Reaction: [protein]-S8-aminomethyldihydrolipoyllysine + tetrahydrofolate = [protein]-dihydrolipoyllysine + 5,10-methylenetetrahydrofolate + NH3
For diagram, click here
Glossary: dihydrolipoyl group
Other name(s): S-aminomethyldihydrolipoylprotein:(6S)-tetrahydrofolate aminomethyltransferase (ammonia-forming); T-protein; glycine synthase; tetrahydrofolate aminomethyltransferase
Systematic name: [protein]-S8-aminomethyldihydrolipoyllysine:tetrahydrofolate aminomethyltransferase (ammonia-forming)
Comments: A component, with EC 1.4.4.2 glycine dehydrogenase (decarboxylating) and EC 1.8.1.4, dihydrolipoyl dehydrogenanse, of the glycine cleavage system, formerly known as glycine synthase. The glycine cleavage system is composed of four components that only loosely associate: the P protein (EC 1.4.4.2), the T protein (EC 2.1.2.10), the L protein (EC 1.8.1.4) and the lipoyl-bearing H protein [3]
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 37257-08-2
References:
1. Okamura-Ikeda, J., Fujiwara, K. and Motokawa, Y. Purification and characterization of chicken liver T protein, a component of the glycine cleavage system. J. Biol. Chem. 257 (1982) 135-139.
2. Perham, R.N. Swinging arms and swinging domains in multifunctional enzymes: catalytic machines for multistep reactions. Annu. Rev. Biochem. 69 (2000) 961-1004. [PMID: 10966480]
3. Nesbitt, N.M., Baleanu-Gogonea, C., Cicchillo, R.M., Goodson, K., Iwig, D.F., Broadwater, J.A., Haas, J.A., Fox, B.G. and Booker, S.J. Expression, purification, and physical characterization of Escherichia coli lipoyl(octanoyl)transferase. Protein Expr. Purif. 39 (2005) 269-282. [PMID: 15642479]
Accepted name: 3-methyl-2-oxobutanoate hydroxymethyltransferase
Reaction: 5,10-methylenetetrahydrofolate + 3-methyl-2-oxobutanoate + H2O = tetrahydrofolate + 2-dehydropantoate
For diagram of reaction click here.
Other name(s): α-ketoisovalerate hydroxymethyltransferase; dehydropantoate hydroxymethyltransferase; ketopantoate hydroxymethyltransferase; oxopantoate hydroxymethyltransferase; 5,10-methylene tetrahydrofolate:α-ketoisovalerate hydroxymethyltransferase
Systematic name: 5,10-methylenetetrahydrofolate:3-methyl-2-oxobutanoate hydroxymethyltransferase
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 56093-17-5
References:
1. Powers, S.G. and Snell, E.E. Ketopantoate hydroxymethyltransferase. II. Physical, catalytic, and regulatory properties. J. Biol. Chem. 251 (1976) 3786-3793. [PMID: 6463]
2. Teller, J.H., Powers, S.G. and Snell, E.E. Ketopantoate hydroxymethyltransferase. I. Purification and role in pantothenate biosynthesis. J. Biol. Chem. 251 (1976) 3780-3785. [PMID: 776976]
[EC 2.1.2.12 Deleted entry: now EC 2.1.1.74 methylenetetrahydrofolate-tRNA-(uracil-5-)-methyltransferase (FADH2-oxidizing) (EC 2.1.2.12 created 1983, deleted 1984)]
Accepted name: UDP-4-amino-4-deoxy-L-arabinose formyltransferase
Reaction: 10-formyltetrahydrofolate + UDP-4-amino-4-deoxy-β-L-arabinopyranose = 5,6,7,8-tetrahydrofolate + UDP-4-deoxy-4-formamido-β-L-arabinopyranose
For diagram of reaction click here.
Other name(s): UDP-L-Ara4N formyltransferase; ArnAFT
Systematic name: 10-formyltetrahydrofolate:UDP-4-amino-4-deoxy-β-L-arabinose N-formyltransferase
Comments: The activity is part of a bifunctional enzyme also performing the reaction of EC 1.1.1.305 [UDP-glucuronic acid dehydrogenase (UDP-4-keto-hexauronic acid decarboxylating)].
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number:
References:
1. 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]
2. Gatzeva-Topalova, P.Z., May, A.P. and Sousa, M.C. Crystal structure and mechanism of the Escherichia coli ArnA (PmrI) transformylase domain. An enzyme for lipid A modification with 4-amino-4-deoxy-L-arabinose and polymyxin resistance. Biochemistry 44 (2005) 5328-5338. [PMID: 15807526]
3. Williams, G.J., Breazeale, S.D., Raetz, C.R.H. and Naismith, J.H. Structure and function of both domains of ArnA, a dual function decarboxylase and a formyltransferase, involved in 4-amino-4-deoxy-L-arabinose biosynthesis. J. Biol. Chem. 280 (2005) 23000-23008. [PMID: 15809294]
4. Gatzeva-Topalova, P.Z., May, A.P. and Sousa, M.C. Structure and mechanism of ArnA: conformational change implies ordered dehydrogenase mechanism in key enzyme for polymyxin resistance. Structure 13 (2005) 929-942. [PMID: 15939024]
5. Yan, A., Guan, Z. and Raetz, C.R.H. An undecaprenyl phosphate-aminoarabinose flippase required for polymyxin resistance in Escherichia coli. J. Biol. Chem. 282 (2007) 36077-36089. [PMID: 17928292]
Accepted name: GDP-perosamine N-formyltransferase
Reaction: 10-formyltetrahydrofolate + GDP-α-D-perosamine = tetrahydrofolate + GDP-N-formyl-α-D-perosamine
Glossary: GDP-α-D-perosamine = GDP-4-amino-4,6-dideoxy-α-D-mannose
Other name(s): wbkC (gene name)
Systematic name: 10-formyltetrahydrofolate:GDP-α-D-perosamine N-formyltransferase
Comments: The enzyme, characterized from the bacterium Brucella melitensis, synthesizes a building block of the O antigen produced by Brucella species.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number:
References:
1. Godfroid, F., Cloeckaert, A., Taminiau, B., Danese, I., Tibor, A., de Bolle, X., Mertens, P. and Letesson, J.J. Genetic organisation of the lipopolysaccharide O-antigen biosynthesis region of Brucella melitensis 16M (wbk). Res. Microbiol. 151 (2000) 655-668. [PMID: 11081580]
2. Riegert, A.S., Chantigian, D.P., Thoden, J.B., Tipton, P.A. and Holden, H.M. Biochemical Characterization of WbkC, an N-Formyltransferase from Brucella melitensis. Biochemistry 56 (2017) 3657-3668. [PMID: 28636341]
('Carboxytransferase' and 'carbamoyltransferase' may be replaced by 'transcarboxylase' and 'transcarbamoylase' respectively).
Accepted name: methylmalonyl-CoA carboxytransferase
Reaction: (S)-methylmalonyl-CoA + pyruvate = propanoyl-CoA + oxaloacetate
Other name(s): transcarboxylase; methylmalonyl coenzyme A carboxyltransferase; methylmalonyl-CoA transcarboxylase; oxalacetic transcarboxylase; methylmalonyl-CoA carboxyltransferase; methylmalonyl-CoA carboxyltransferase; (S)-2-methyl-3-oxopropanoyl-CoA:pyruvate carboxyltransferase; (S)-2-methyl-3-oxopropanoyl-CoA:pyruvate carboxytransferase carboxytransferase [incorrect]
Systematic name: (S)-methylmalonyl-CoA:pyruvate carboxytransferase
Comments: A biotinyl-protein, containing cobalt and zinc. The enzyme, described from the bacterium Propionibacterium shermanii, is unique among the biotin-dependent enzymes in that it catalyses carboxyl transfer between two organic molecules, utilizing two separate carboxyltransferase domains. The enzyme is a very large complex, consisting of a hexameric central core of 12S subunits surrounded by six 5S subunit dimers, each connected to the central core by twelve 1.3S biotin carrier subunits.
Links to other databases: BRENDA, EAWAG-BBD, EXPASY, GTD, KEGG, Metacyc, PDB, CAS registry number: 9029-86-1
References:
1. Swick, R.W. and Wood, H.G. The role of transcarboxylation in propionic acid fermentation. Proc. Natl. Acad. Sci. USA 46 (1960) 28-41. [PMID: 16590594]
2. Wood, H.G. and Kumar, G.K. Transcarboxylase: its quaternary structure and the role of the biotinyl subunit in the assembly of the enzyme and in catalysis. Ann. N.Y. Acad. Sci. 447 (1985) 1-22. [PMID: 3893281]
3. Peikert, C., Seeger, K., Bhat, R.K. and Berger, S. Determination of the binding specificity of the 12S subunit of the transcarboxylase by saturation transfer difference NMR. Org. Biomol. Chem. 2 (2004) 1777-1781. [PMID: 15188046]
4. Kumar Bhat, R. and Berger, S. New and easy strategy for cloning, expression, purification, and characterization of the 5S subunit of transcarboxylase from Propionibacterium f. shermanii. Prep Biochem Biotechnol 37 (2007) 13-26. [PMID: 17134979]
5. Carey, P.R., Sonnichsen, F.D. and Yee, V.C. Transcarboxylase: one of nature’s early nanomachines. IUBMB Life 56 (2004) 575-583. [PMID: 15814455]
Accepted name: aspartate carbamoyltransferase
Reaction: carbamoyl phosphate + L-aspartate = phosphate + N-carbamoyl-L-aspartate
For diagram click here.
Other name(s): carbamylaspartotranskinase; aspartate transcarbamylase; aspartate carbamyltransferase; aspartic acid transcarbamoylase; aspartic carbamyltransferase; aspartic transcarbamylase; carbamylaspartotranskinase; L-aspartate transcarbamoylase; L-aspartate transcarbamylase; carbamoylaspartotranskinase; aspartate transcarbamylase; aspartate transcarbamoylase; ATCase
Systematic name: carbamoyl-phosphate:L-aspartate carbamoyltransferase
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 9012-49-1
References:
1. Lowenstein, J.M. and Cohen, P.P. Studies on the biosynthesis of carbamylaspartic acid. J. Biol. Chem. 220 (1956) 57-70.
2. Reichard, P. and Hanshoff, G. Aspartate carbamyl transferase from Escherichia coli. Acta Chem. Scand. 10 (1956) 548-566.
3. Shepherson, M. and Pardee, A.B. Production and crystallization of aspartate transcarbamylase. J. Biol. Chem. 235 (1960) 3233-3237.
Accepted name: ornithine carbamoyltransferase
Reaction: carbamoyl phosphate + L-ornithine = phosphate + L-citrulline
For diagram click here.
Other name(s): citrulline phosphorylase; ornithine transcarbamylase; OTC; carbamylphosphate-ornithine transcarbamylase; L-ornithine carbamoyltransferase; L-ornithine carbamyltransferase; L-ornithine transcarbamylase; ornithine carbamyltransferase
Systematic name: carbamoyl-phosphate:L-ornithine carbamoyltransferase
Comments: The plant enzyme also catalyses the reactions of EC 2.1.3.6 putrescine carbamoyltransferase, EC 2.7.2.2 carbamate kinase and EC 3.5.3.12 agmatine deiminase, thus acting as putrescine synthase, converting agmatine [(4-aminobutyl)guanidine] and ornithine into putrescine and citrulline, respectively.
Links to other databases: BRENDA, EXPASY, GTD, KEGG, Metacyc, PDB, CAS registry number: 9001-69-8
References:
1. Bishop, S.H. and Grisolia, S. Crystalline ornithine transcarbamylase. Biochim. Biophys. Acta 139 (1967) 344-348.
2. Marshall, M. and Cohen, P.P. Ornithine transcarbamylase from Streptococcus faecalis and bovine liver. I. Isolation and subunit structure. J. Biol. Chem. 247 (1972) 1641-1653. [PMID: 4622303]
3. Marshall, M. and Cohen, P.P. Ornithine transcarbamylase from Streptococcus faecalis and bovine liver. II. Multiple binding sites for carbamyl-P and L-norvaline, correlation with steady state kinetics. J. Biol. Chem. 247 (1972) 1654-1668. [PMID: 4622304]
4. Marshall, M. and Cohen, P.P. Ornithine transcarbamylase from Streptococcus faecalis and bovine liver. 3. Effects of chemical modifications of specific residues on ligand binding and enzymatic activity. J. Biol. Chem. 247 (1972) 1669-1682. [PMID: 4622305]
[EC 2.1.3.4 Deleted entry: malonyl-CoA carboxyltransferase. (EC 2.1.3.4 created 1965, deleted 1972)]
Accepted name: oxamate carbamoyltransferase
Reaction: carbamoyl phosphate + oxamate = phosphate + N-carbamoyl-2-oxoglycine
For diagram click here.
Other name(s): oxamic transcarbamylase
Systematic name: carbamoyl-phosphate:oxamate carbamoyltransferase
Links to other databases: BRENDA, EXPASY, GTD, KEGG, Metacyc, CAS registry number: 62213-52-9
References:
1. Bojanowski, R., Gaudy, E., Valentine, R.C. and Wolfe, R.S. Oxamic transcarbamylase of Streptococcus allantoicus. J. Bacteriol. 87 (1964) 75-80.
Accepted name: putrescine carbamoyltransferase
Reaction: carbamoyl phosphate + putrescine = phosphate + N-carbamoylputrescine
Other name(s): PTCase; putrescine synthase; putrescine transcarbamylase
Systematic name: carbamoyl-phosphate:putrescine carbamoyltransferase
Comments: The plant enzyme also catalyses the reactions of EC 2.1.3.3 ornithine carbamoyltransferase, EC 2.7.2.2 carbamate kinase and EC 3.5.3.12 agmatine deiminase, thus acting as putrescine synthase, converting agmatine [(4-aminobutyl)guanidine] and ornithine into putrescine and citrulline, respectively.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 9076-55-5
References:
1. Roon, R.J. and Barker, H.A. Fermentation of agmatine in Streptococcus faecalis: occurrence of putrescine transcarbamoylase. J. Bacteriol. 109 (1972) 44-50. [PMID: 4621632]
2. Srivenugopal, K.S. and Adiga, P.R. Enzymic conversion of agmatine to putrescine in Lathyrus sativus seedlings. Purification and properties of a multifunctional enzyme (putrescine synthase). J. Biol. Chem. 256 (1981) 9532-9541. [PMID: 6895223]
Accepted name: 3-hydroxymethylcephem carbamoyltransferase
Reaction: carbamoyl phosphate + a 3-hydroxymethylceph-3-em-4-carboxylate = phosphate + a 3-carbamoyloxymethylcephem
Systematic name: carbamoyl-phosphate:3-hydroxymethylceph-3-em-4-carboxylate carbamoyltransferase
Comments: Acts on a wide range of 3-hydroxymethylcephems (a subclass of the cephalosporin antibiotics). Activated by ATP.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 74315-96-1
References:
1. Brewer, S.J., Taylor, P.M. and Turner, M.K. An adenosine triphosphate-dependent carbamoylphosphate--3-hydroxymethylcephem O-carbamoyltransferase from Streptomyces clavuligerus. Biochem. J. 185 (1980) 555-564.
Accepted name: lysine carbamoyltransferase
Reaction: carbamoyl phosphate + L-lysine = phosphate + L-homocitrulline
Other name(s): lysine transcarbamylase
Systematic name: carbamoyl-phosphate:L-lysine carbamoyltransferase
Comments: Not identical with EC 2.1.3.3 ornithine carbamoyltransferase.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 86352-19-4
References:
1. Hommes, F.A., Eller, A.G., Scott, D.F. and Carter, A.L. Separation of ornithine and lysine activities of the ornithine-transcarbamylase-catalyzed reaction. Enzyme 29 (1983) 271-277. [PMID: 6409607]
Accepted name: N-acetylornithine carbamoyltransferase
Reaction: carbamoyl phosphate + N2-acetyl-L-ornithine = phosphate + N-acetyl-L-citrulline
Glossary: N-acetyl-L-citrulline = N5-acetylcarbamoyl-L-ornithine
Other name(s): acetylornithine transcarbamylase; N-acetylornithine transcarbamylase; AOTC
Systematic name: carbamoyl-phosphate:N2-acetyl-L-ornithine carbamoyltransferase
Comments: Differs from EC 2.1.3.3, ornithine carbamoyltransferase. This enzyme replaces EC 2.1.3.3 in the canonic arginine biosynthetic pathway of several Eubacteria and has no catalytic activity with L-ornithine as substrate.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 890853-54-0
References:
1. Shi, D., Morizono, H., Yu, X., Roth, L., Caldovic, L., Allewell, N.M., Malamy, M.H. and Tuchman, M. Crystal structure of N-acetylornithine transcarbamylase from Xanthomonas campestris: a novel enzyme in a new arginine biosynthetic pathway found in several Eubacteria. J. Biol. Chem. 280 (2005) 14366-14369. [PMID: 15731101]
2. Morizono, H., Cabrera-Luque, J., Shi, D., Gallegos, R., Yamaguchi, S., Yu, X., Allewell, N.M., Malamy, M.H. and Tuchman, M. Acetylornithine transcarbamylase: a novel enzyme in arginine biosynthesis. J. Bacteriol. 188 (2006) 2974-2982. [PMID: 16585758]
Accepted name: malonyl-S-ACP:biotin-protein carboxyltransferase
Reaction: a malonyl-[acyl-carrier protein] + a biotinyl-[protein] = an acetyl-[acyl-carrier protein] + a carboxybiotinyl-[protein]
For diagram of reaction click here
Other name(s): malonyl-S-acyl-carrier protein:biotin-protein carboxyltransferase; MadC/MadD; MadC,D; malonyl-[acyl-carrier protein]:biotinyl-[protein] carboxyltransferase
Systematic name: malonyl-[acyl-carrier protein]:biotinyl-[protein] carboxytransferase
Comments: Derived from the components MadC and MadD of the anaerobic bacterium Malonomonas rubra, this enzyme is a component of EC 7.2.4.4, biotin-dependent malonate decarboxylase. The carboxy group is transferred from malonate to the prosthetic group of the biotin protein (MadF) with retention of configuration [2]. Similar to EC 4.1.1.87, malonyl-S-ACP decarboxylase, which forms part of the biotin-independent malonate decarboxylase (EC 4.1.1.88), this enzyme also follows on from EC 2.3.1.187, acetyl-S-ACP:malonate ACP transferase, and results in the regeneration of the acetyl-[acyl-carrier protein] [3].
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number:
References:
1. Berg, M., Hilbi, H. and Dimroth, P. Sequence of a gene cluster from Malonomonas rubra encoding components of the malonate decarboxylase Na+ pump and evidence for their function. Eur. J. Biochem. 245 (1997) 103-115. [PMID: 9128730]
2. Micklefield, J., Harris, K.J., Gröger, S., Mocek, U., Hilbi, H., Dimroth, P. and Floss, H.G. Stereochemical course of malonate decarboxylase in Malonomonas rubra has biotin decarboxylation with retention. J. Am. Chem. Soc. 117 (1995) 1153-1154.
3. Dimroth, P. and Hilbi, H. Enzymic and genetic basis for bacterial growth on malonate. Mol. Microbiol. 25 (1997) 3-10. [PMID: 11902724]
Accepted name: N-succinylornithine carbamoyltransferase
Reaction: carbamoyl phosphate + N2-succinyl-L-ornithine = phosphate + N-succinyl-L-citrulline
Glossary: N-acetyl-L-citrulline = N5-acetylcarbamoyl-L-ornithine
Other name(s): succinylornithine transcarbamylase; N-succinyl-L-ornithine transcarbamylase; SOTCase
Systematic name: carbamoyl phosphate:N2-succinyl-L-ornithine carbamoyltransferase
Comments: This enzyme is specific for N-succinyl-L-ornithine and cannot use either L-ornithine (see EC 2.1.3.3, ornithine carbamoyltransferase) or N-acetyl-L-ornithine (see EC 2.1.3.9, N-acetylornithine carbamoyltransferase) as substrate. However, a single amino-acid substitution (Pro90 → Glu90) is sufficient to switch the enzyme to one that uses N-acetyl-L-ornithine as substrate. It is essential for de novo arginine biosynthesis in the obligate anaerobe Bacteroides fragilis, suggesting that this organism uses an alternative pathway for synthesizing arginine.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number:
References:
1. Shi, D., Morizono, H., Cabrera-Luque, J., Yu, X., Roth, L., Malamy, M.H., Allewell, N.M. and Tuchman, M. Structure and catalytic mechanism of a novel N-succinyl-L-ornithine transcarbamylase in arginine biosynthesis of Bacteroides fragilis. J. Biol. Chem. 281 (2006) 20623-20631. [PMID: 16704984]
2. Shi, D., Yu, X., Cabrera-Luque, J., Chen, T.Y., Roth, L., Morizono, H., Allewell, N.M. and Tuchman, M. A single mutation in the active site swaps the substrate specificity of N-acetyl-L-ornithine transcarbamylase and N-succinyl-L-ornithine transcarbamylase. <>Protein Sci. 16 (2007) 1689-1699. [PMID: 17600144]
Accepted name: decarbamoylnovobiocin carbamoyltransferase
Reaction: carbamoyl phosphate + decarbamoylnovobiocin = phosphate + novobiocin
For diagram of reaction click here.
Glossary: decarbamoylnovobiocin = N-{7-[(6-deoxy-5-methyl-4-O-methyl-β-D-gulopyranosyl)oxy]4-hydroxy-8-methyl-2-oxo-2H-chromen-3-yl}-4-hydroxy-3-(3-methyl-2-buten-1-yl)benzamide
Other name(s): novN (gene name)
Systematic name: carbamoyl phosphate:decarbamoylnovobiocin 3''-O-carbamoyltransferase
Comments: The enzyme catalyses the last step in the biosynthesis of the aminocoumarin antibiotic novobiocin. The reaction is activated by ATP [1].
Links to other databases: BRENDA, EXPASY, KEGG Metacyc, CAS registry number:
References:
1. Freel Meyers, C.L., Oberthur, M., Xu, H., Heide, L., Kahne, D. and Walsh, C.T. Characterization of NovP and NovN: completion of novobiocin biosynthesis by sequential tailoring of the noviosyl ring. Angew. Chem. Int. Ed. Engl. 43 (2004) 67-70. [PMID: 14694473]
2. Gomez Garcia, I., Freel Meyers, C.L., Walsh, C.T. and Lawson, D.M. Crystallization and preliminary X-ray analysis of the O-carbamoyltransferase NovN from the novobiocin-biosynthetic cluster of Streptomyces spheroides. Acta Crystallogr. Sect. F Struct. Biol. Cryst. Commun. 64 (2008) 1000-1002. [PMID: 18997325]
[EC 2.1.3.13 Deleted entry: ATP carbamoyltransferase. The enzyme has been replaced by EC 6.1.2.2, nebramycin 5' synthase (EC 2.1.3.13 created 2013, deleted 2014)]
[EC 2.1.3.14 Deleted entry: tobramycin carbamoyltransferase. The enzyme has been replaced by EC 6.1.2.2, nebramycin 5' synthase (EC 2.1.3.14 created 2013, deleted 2014)]
Accepted name: acetyl-CoA carboxytransferase
Reaction: [biotin carboxyl-carrier protein]-N6-carboxybiotinyl-L-lysine + acetyl-CoA = [biotin carboxyl-carrier protein]-N6-biotinyl-L-lysine + malonyl-CoA
Other name(s): accAD (gene names)
Systematic name: [biotin carboxyl-carrier protein]-N6-carboxybiotinyl-L-lysine:acetyl-CoA:carboxytransferase
Comments: The enzyme catalyses the transfer of a carboxyl group carried on a biotinylated biotin carboxyl carrier protein (BCCP) to acetyl-CoA, forming malonyl-CoA. In some organisms this activity is part of a multi-domain polypeptide that includes the carrier protein and EC 6.3.4.14, biotin carboxylase (see EC 6.4.1.2, acetyl-CoA carboxylase). Some enzymes can also carboxylate propanonyl-CoA and butanoyl-CoA (cf. EC 6.4.1.3, propionyl-CoA carboxylase).
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number:
References:
1. Bilder, P., Lightle, S., Bainbridge, G., Ohren, J., Finzel, B., Sun, F., Holley, S., Al-Kassim, L., Spessard, C., Melnick, M., Newcomer, M. and Waldrop, G.L. The structure of the carboxyltransferase component of acetyl-coA carboxylase reveals a zinc-binding motif unique to the bacterial enzyme. Biochemistry 45 (2006) 1712-1722. [PMID: 16460018]
2. Chuakrut, S., Arai, H., Ishii, M. and Igarashi, Y. Characterization of a bifunctional archaeal acyl coenzyme A carboxylase. J. Bacteriol. 185 (2003) 938-947. [PMID: 12533469]
Accepted name: ureidoglycine carbamoyltransferase
Reaction: carbamoyl phosphate + (S)-(carbamoylamino)glycine = phosphate + allantoate
Other name(s): UGTCase
Systematic name: carbamoyl phosphate:(S)-(carbamoylamino)glycine carbamoyltransferase
Comments: The enzyme, characterized from the bacterium Rubrobacter xylanophilus, is involved in a purine degradation pathway.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number:
References:
1. Barba, M., Dutoit, R., Legrain, C. and Labedan, B. Identifying reaction modules in metabolic pathways: bioinformatic deduction and experimental validation of a new putative route in purine catabolism. BMC Syst Biol 7 (2013) 99. [PMID: 24093154]
('Amidinotransferase' may be replaced by 'transamidinase')
EC 2.1.4.3 L-arginine:L-lysine amidinotransferase
Accepted name: glycine amidinotransferase
Reaction: L-arginine + glycine = L-ornithine + guanidinoacetate
For diagram of reaction click here.
Other name(s): arginine-glycine amidinotransferase; arginine-glycine transamidinase; glycine transamidinase
Systematic name: L-arginine:glycine amidinotransferase
Comments: Canavanine can act instead of arginine. Formerly EC 2.6.2.1.
Links to other databases: BRENDA, EXPASY, GTD, KEGG, Metacyc, PDB, CAS registry number: 9027-35-4
References:
1. Borsook, H. and Dubnoff, J.W. The formation of glycocyamine in animal tissues. J. Biol. Chem. 138 (1941) 389-403.
2. Conconi, F. and Grazi, E. Transamidinase of hog kidney. I. Purification and properties. J. Biol. Chem. 240 (1965) 2461-2464.
3. McGuire, D.M., Tormanen, C.D., Segal, I.S. and van Pilsum, J.F. The effect of growth hormone and thyroxine on the amount of L-arginine:glycine amidinotransferase in kidneys of hypophysectomized rats, purification and some properties of rat kidney transamidinase. J. Biol. Chem. 255 (1980) 1152-1159.
4. Ratner, S. Transamidination. In: Boyer, P.D., Lardy, H. and Myrbäck, K. (Eds.), The Enzymes, 2nd ed., vol. 6, Academic Press, New York, 1962, pp. 267-275.
5. Ratner, S. and Rochovansky, O. Biosynthesis of guanidinoacetic acid. I. Purification and properties of transamidinase. Arch. Biochem. Biophys. 63 (1956) 277-295.
6. Ratner, S. and Rochovansky, O. Biosynthesis of guanidinoacetic acid. II. Mechanism of amidine group transfer. Arch. Biochem. Biophys. 63 (1956) 296-315.
7. Walker, J.B. Biosynthesis of arginine from canavanine and ornithine in kidney. J. Biol. Chem. 218 (1956) 549-556.
8. Walker, J.B. Studies on the mechanism of action of kidney transamidinase. J. Biol. Chem. 224 (1957) 57-66.
Accepted name: scyllo-inosamine-4-phosphate amidinotransferase
Reaction: L-arginine + 1-amino-1-deoxy-scyllo-inositol 4-phosphate = L-ornithine + 1-guanidino-1-deoxy-scyllo-inositol 4-phosphate
Other name(s): L-arginine:inosamine-P-amidinotransferase; inosamine-P amidinotransferase; L-arginine:inosamine phosphate amidinotransferase; inosamine-phosphate amidinotransferase
Systematic name: L-arginine:1-amino-1-deoxy-scyllo-inositol-4-phosphate amidinotransferase
Comments: 1D-1-Guanidino-3-amino-1,3-dideoxy-scyllo-inositol 6-phosphate, streptamine phosphate and 2-deoxystreptamine phosphate can also act as acceptors; canavanine can act as donor.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 52227-63-1
References:
1. Walker, M.S. and Walker, J.B. Enzymic studies on the biosynthesis of streptomycin, transamidation of inosamine and streptamine derivatives. J. Biol. Chem. 241 (1966) 1262-1269.
Accepted name: L-arginine:L-lysine amidinotransferase
Reaction: L-arginine + L-lysine = L-ornithine + L-homoarginine
Glossary: phaseolotoxin = N5-[amino(sulfoamino)phosphoryl]-L-ornithyl-L-alanyl-L-arginine
Other name(s): amtA (gene name)
Systematic name: L-arginine:L-lysine amidinotransferase
Comments: The enzyme, characterized from the bacterium Pseudomonas savastanoi pv. phaseolicola, is involved in the biosynthesis of the toxin phaseolotoxin, a modified tripeptide that causes the 'halo blight' disease of beans.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:
References:
1. Hernandez-Guzman, G. and Alvarez-Morales, A. Isolation and characterization of the gene coding for the amidinotransferase involved in the biosynthesis of phaseolotoxin in Pseudomonas syringae pv. phaseolicola. Mol. Plant Microbe Interact. 14 (2001) 545-554. [PMID: 11310742]
2. Li, M., Chen, L., Deng, Z. and Zhao, C. Characterization of AmtA, an amidinotransferase involved in the biosynthesis of phaseolotoxins. FEBS Open Bio 6 (2016) 603-609. [PMID: 27419063]
EC 2.1.5.1
Accepted name: sesamin methylene transferase
Reaction: (1) (+)-sesamin + tetrahydrofolate = (+)-demethylpiperitol + 5,10-methylenetetrahydrofolate
For diagram of reaction click here.
Glossary: (+)-sesamin = 5,5′-[(1S,3aR,4S,6aR)-tetrahydro-1H,3H-furo[3,4-c]furan-1,4-diyl]bis(1,3-benzodioxole)
Other name(s): sesA (gene name)
Systematic name: (+)-sesamin:tetrahydrofolate N-methylenetransferase
Comments: This enzyme was characterized from the bacterium Sinomonas sp. No.22. It catalyses a cleavage of a methylene bridge, followed by the transfer of the methylene group to tetrahydrofolate. The enzyme is also active with (+)-episesamin, (–)-asarinin, (+)-sesaminol, (+)-sesamolin, and piperine.
Links to other databases:
BRENDA,
EXPASY,
KEGG,
MetaCyc,
CAS registry number:
References:
1. Kumano, T., Fujiki, E., Hashimoto, Y. and Kobayashi, M. Discovery of a sesamin-metabolizing microorganism and a new enzyme. Proc. Natl. Acad. Sci. USA 113 (2016) 9087-9092. [PMID: 27444012]
(2) (+)-demethylpiperitol + tetrahydrofolate = (+)-didemethylpinoresinol + 5,10-methylenetetrahydrofolate
(+)-demethylpiperitol = 4-[(1S,3aR,4S,6aR)-4-(1,3-benzodioxol-5-yl)tetrahydro-1H,3H-furo[3,4-c]furan-1-yl]benzene-1,2-diol
(+)-didemethylpinoresinol = 4-[(1S,3aR,4S,6aR)-4-(3,4-dihydroxyphenyl)tetrahydro-1H,3H-furo[3,4-c]furan-1-yl]benzene-1,2-diol
EC 2.2 Transferring Aldehyde or Ketonic Groups
EC 2.2.1 Transketolases and Transaldolases
Accepted name: transketolase
Reaction: sedoheptulose 7-phosphate + D-glyceraldehyde 3-phosphate = D-ribose 5-phosphate + D-xylulose 5-phosphate
For diagram click here (mechanism), another example click here or here.
Glossary: thiamine diphosphate
Other name(s): glycolaldehydetransferase
Systematic name: sedoheptulose-7-phosphate:D-glyceraldehyde-3-phosphate glycolaldehydetransferase
Comments: A thiamine-diphosphate protein. Wide specificity for both reactants, e.g. converts hydroxypyruvate and R-CHO into CO2 and R-CHOH-CO-CH2OH. The enzyme from the bacterium Alcaligenes faecalis shows high activity with D-erythrose 4-phosphate as acceptor.
Links to other databases: BRENDA, EXPASY, GTD, KEGG, Metacyc, PDB, CAS registry number: 9014-48-6
References:
1. de la Haba, G., Leder, I.G. and Racker, E. Crystalline transketolase from bakers' yeast: isolation and properties. J. Biol. Chem. 214 (1955) 409-426.
2. Domagk, G.F. and Horecker, B.L. Fructose and erythrose metabolism in Alcaligenes faecalis. Arch. Biochem. Biophys. 109 (1965) 342-349.
3. Horecker, B.L., Smyrniotis, P.Z. and Hurwitz, J. The role of xylulose 5-phosphate in the transketolase reaction. J. Biol. Chem. 223 (1956) 1009-1019.
4. Racker, E. Transketolase. In: Boyer, P.D., Lardy, H. and Myrbäck, K. (Eds.), The Enzymes, 2nd ed., vol. 5, Academic Press, New York, 1961, pp. 397-412.
Accepted name: transaldolase
Reaction: sedoheptulose 7-phosphate + D-glyceraldehyde 3-phosphate = D-erythrose 4-phosphate + D-fructose 6-phosphate
For diagram of reaction click here (mechanism), another example click here.
Other name(s): dihydroxyacetonetransferase; dihydroxyacetone synthase (incorrect); formaldehyde transketolase (incorrect)
Systematic name: sedoheptulose-7-phosphate:D-glyceraldehyde-3-phosphate glyceronetransferase
Links to other databases: BRENDA, EXPASY, GTD, KEGG, Metacyc, PDB, CAS registry number: 9014-46-4
References:
1. Horecker, B.L. and Smyrniotis, P.Z. Purification and properties of yeast transaldolase. J. Biol. Chem. 212 (1955) 811-825.
2. Racker, E. Transaldolase. In: Boyer, P.D., Lardy, H. and Myrbäck, K. (Eds.), The Enzymes, 2nd ed., vol. 5, Academic Press, New York, 1961, pp. 407-412.
3. Tsolas, O. and Horecker, B.L. Transaldolase. In: Boyer, P.D. (Ed.), The Enzymes, 3rd ed., vol. 7, Academic Press, New York, 1972, pp. 259-280.
Accepted name: formaldehyde transketolase
Reaction: D-xylulose 5-phosphate + formaldehyde = D-glyceraldehyde 3-phosphate + glycerone
For diagram click here.
Glossary: thiamine diphosphate
Other name(s): dihydroxyacetone synthase
Systematic name: D-xylulose-5-phosphate:formaldehyde glycolaldehydetransferase
Comments: A thiamine-diphosphate protein. Not identical with EC 2.2.1.1 transketolase. Also converts hydroxypyruvate and formaldehyde into glycerone and CO2.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 124566-23-0
References:
1. Bystrykh, L.V., Sokolov, A.P. and Trotsenko, Yu.A. Separation of transketolase and dihydroxyacetone synthase from methylotrophic yeasts. Dokl. Akad. Nauk S.S.S.R. 258 (1981) 499-501 [in Russian].
2. Kato, N., Higuchi, T., Sakazawa, C., Nishizawa, T., Tani, Y. and Yamada, H. Purification and properties of a transketolase responsible for formaldehyde fixation in a methanol-utilizing yeast, Candida boidinii (Kloeckera sp.) No. 2201. Biochim. Biophys. Acta 715 (1982) 143-150.
3. Waites, M.J. and Quayle, J.R. The interrelation between transketolase and dihydroxyacetone synthase activities in the methylotrophic yeast Candida boidinii. J. Gen. Microbiol. 124 (1981) 309-316.
Accepted name: acetoin—ribose-5-phosphate transaldolase
Reaction: 3-hydroxybutan-2-one + D-ribose 5-phosphate = acetaldehyde + 1-deoxy-D-altro-heptulose 7-phosphate
For diagram click here.
Glossary: thiamine diphosphate
Other name(s): 1-deoxy-D-altro-heptulose-7-phosphate synthetase; 1-deoxy-D-altro-heptulose-7-phosphate synthase; 3-hydroxybutan-2-one:D-ribose-5-phosphate aldehydetransferase [wrong substrate name]
Systematic name: 3-hydroxybutan-2-one:D-ribose-5-phosphate aldehydetransferase
Comments: A thiamine-diphosphate protein.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 87843-76-3
References:
1. Yokota, A. and Sasajima, K. Enzymatic formation of a new monosaccharide, 1-deoxy-D-altro-heptulose phosphate, from DL-acetoin and D-ribose 5-phosphate by a transketolase mutant of Bacillus pumilus. Agric. Biol. Chem. 47 (1983) 1545-1553.
Accepted name: 2-hydroxy-3-oxoadipate synthase
Reaction: 2-oxoglutarate + glyoxylate = 2-hydroxy-3-oxoadipate + CO2
For diagram click here.
Glossary: thiamine diphosphate
Other name(s): 2-hydroxy-3-oxoadipate glyoxylate-lyase (carboxylating); α-ketoglutaric-glyoxylic carboligase; oxoglutarate: glyoxylate carboligase
Systematic name: 2-oxoglutarate:glyoxylate succinaldehydetransferase (decarboxylating)
Comments: The bacterial enzyme requires thiamine diphosphate. The product decarboxylates to 5-hydroxy-4-oxopentanoate. The enzyme can decarboxylate 2-oxoglutarate. Acetaldehyde can replace glyoxylate.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 9054-72-2
References:
1. Schlossberg, M.A., Bloom, R.J., Richert, D.A. and Westerfield, W.W. Carboligase activity of α-ketoglutarate dehydrogenase. Biochemistry 9 (1970) 1148-1153. [PMID: 5418712]
2. Schlossberg, M.A., Richert, D.A., Bloom, R.J. and Westerfield, W.W. Isolation and identification of 5-hydroxy-4-ketovaleric acid as a product of α-ketoglutarate: glyoxylate carboligase. Biochemistry 7 (1968) 333-337. [PMID: 4320439]
3. Stewart, P.R. and Quayle, J.R. The synergistic decarboxylation of glyoxalate and 2-oxoglutarate by an enzyme system from pig-liver mitochondria. Biochem. J. 102 (1967) 885-897.
Accepted name: acetolactate synthase
Reaction: 2 pyruvate = 2-acetolactate + CO2
For diagram click here.
Glossary: thiamine diphosphate
Other name(s): α-acetohydroxy acid synthetase; α-acetohydroxyacid synthase; α-acetolactate synthase; α-acetolactate synthetase; acetohydroxy acid synthetase; acetohydroxyacid synthase; acetolactate pyruvate-lyase (carboxylating); acetolactic synthetase
Systematic name: pyruvate:pyruvate acetaldehydetransferase (decarboxylating)
Comments: This enzyme requires thiamine diphosphate. The reaction shown is in the pathway of biosynthesis of valine; the enzyme can also transfer the acetaldehyde from pyruvate to 2-oxobutanoate, forming 2-ethyl-2-hydroxy-3-oxobutanoate, also known as 2-aceto-2-hydroxybutanoate, a reaction in the biosynthesis of isoleucine.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 9027-45-6
References:
1. Bauerle, R.H., Freundlich, M., Størmer, F.C. and Umbarger, H.E. Control of isoleucine, valine and leucine biosynthesis. II. Endproduct inhibition by valine of acetohydroxy acid synthetase in Salmonella typhimurium. Biochim. Biophys. Acta 92 (1964) 142-149.
2. Huseby, N.E., Christensen, T.B., Olsen, B.R. and Størmer, F.C. The pH 6 acetolactate-forming enzyme from Aerobacter aerogenes. Subunit structure. Eur. J. Biochem. 20 (1971) 209-214. [PMID: 5560406]
3. Størmer, F.C., Solberg, Y. and Hovig, T. The pH 6 acetolactate-forming enzyme from Aerobacter aerogenes. Molecular properties. Eur. J. Biochem. 10 (1969) 251-260. [PMID: 5823101]
4. Barak, Z., Chipman, D.M. and Gollop, N. Physiological implications of the specificity of acetohydroxy acid synthase isozymes of enteric bacteria. J. Bacteriol. 169 (1987) 3750-3756. [PMID: 3301814]
Accepted name: 1-deoxy-D-xylulose-5-phosphate synthase
Reaction: pyruvate + D-glyceraldehyde 3-phosphate = 1-deoxy-D-xylulose 5-phosphate + CO2
For diagram click here and mechanism here
Glossary: thiamine diphosphate
Other name(s): 1-deoxy-D-xylulose-5-phosphate pyruvate-lyase (carboxylating); DXP-synthase
Systematic name: pyruvate:D-glyceraldehyde-3-phosphate acetaldehydetransferase (decarboxylating)
Comments: Requires thiamine diphosphate. The enzyme forms part of an alternative nonmevalonate pathway for terpenoid biosynthesis (for diagram, click here).
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 202218-79-9
References:
1. Sprenger, G.A., Schörken, U., Weigert, T., Grolle, S., deGraaf, A.A., Taylor, S.V., Begley, T.P., Bringer-Meyer, S. and Sahm, H. Identification of a thiamin-dependent synthase in Escherichia coli required for the formation of the 1-deoxy-D-xylulose 5-phosphate precursor to isoprenoids, thiamin, and pyridoxol. Proc. Natl. Acad. Sci. USA 94 (1997) 12857-12862. [PMID: 9371765]
2. Kuzuyama, T., Takagi, M., Takahashi, S. and Seto, H. Cloning and characterization of 1-deoxy-D-xylulose 5-phosphate synthase from Streptomyces sp. strain CL190, which uses both the mevalonate and nonmevalonate pathways for isopentenyl diphosphate biosynthesis. J. Bacteriol. 182 (2000) 891-897. [PMID: 10648511]
Accepted name: fluorothreonine transaldolase
Reaction: L-threonine + fluoroacetaldehyde = acetaldehyde + 4-fluoro-L-threonine
Systematic name: fluoroacetaldehyde:L-threonine aldehydetransferase
Comments: A pyridoxal phosphate protein. Can also convert chloroacetaldehyde into 4-chloro-L-threonine. Unlike EC 2.1.2.1, glycine hydroxymethyltransferase, does not use glycine as a substrate.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 403503-13-9
References:
1. Murphy, C.D., O'Hagan, D. and Schaffrath, C. Identification of a PLP-dependent threonine transaldolase: a novel enzyme involved in 4-fluorothreonine biosynthesis in Streptomyces cattleya. Angew. Chem. Int. Ed. Engl. 40 (2001) 4479-4481. [PMID: 12404452]
2. Murphy, C.D., Schaffrath, C. and O'Hagan, D. Fluorinated natural products: the biosynthesis of fluoroacetate and 4-fluorothreonine in Streptomyces cattleya. Chemosphere 52 (2003) 455-461. [PMID: 12738270]
Accepted name: 2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carboxylic-acid synthase
Reaction: isochorismate + 2-oxoglutarate = 5-enolpyruvoyl-6-hydroxy-2-succinylcyclohex-3-ene-1-carboxylate + CO2
For diagram of reaction, click here.
Other name(s): SEPHCHC synthase; MenD
Systematic name: isochorismate:2-oxoglutarate 4-oxopentanoatetransferase (decarboxylating)
Comments: Requires Mg2+ for maximal activity. This enzyme is involved in the biosynthesis of vitamin K2 (menaquinone). In most anaerobes and all Gram-positive aerobes, menaquinone is the sole electron transporter in the respiratory chain and is essential for their survival. It had previously been thought that the products of the reaction were (1R,6R)-6-hydroxy-2-succinylcyclohexa-2,4-diene-1-carboxylate (SHCHC), pyruvate and CO2 but it is now known that two separate enzymes are involved: this enzyme and EC 4.2.99.20, 2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase. Under basic conditions, the product can spontaneously lose pyruvate to form SHCHC.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 1112282-73-1
References:
1. Jiang, M., Cao, Y., Guo, Z.F., Chen, M., Chen, X. and Guo, Z. Menaquinone biosynthesis in Escherichia coli: identification of 2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carboxylate as a novel intermediate and re-evaluation of MenD activity. Biochemistry 46 (2007) 10979-10989. [PMID: 17760421]
Accepted name: 2-amino-3,7-dideoxy-D-threo-hept-6-ulosonate synthase
Reaction: L-aspartate 4-semialdehyde + 1-deoxy-D-threo-hexo-2,5-diulose 6-phosphate = 2-amino-3,7-dideoxy-D-threo-hept-6-ulosonate + 2,3-dioxopropyl phosphate
For diagram of reaction click here.
Glossary: 1-deoxy-D-threo-hexo-2,5-diulose 6-phosphate = 6-deoxy-5-ketofructose 1-phosphate
2-amino-3,7-dideoxy-D-threo-hept-6-ulosonate = 2-amino-2,3,7-trideoxy-D-lyxo-hept-6-ulosonate
Other name(s): ADH synthase; ADHS; MJ0400 (gene name)
Systematic name: L-aspartate 4-semialdehyde:1-deoxy-D-threo-hexo-2,5-diulose 6-phosphate methylglyoxaltransferase
Comments: The enzyme plays a key role in an alternative pathway of the biosynthesis of 3-dehydroquinate (DHQ), which is involved in the canonical pathway for the biosynthesis of aromatic amino acids. The enzyme can also catalyse the reaction of EC 4.1.2.13, fructose-bisphosphate aldolase.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number:
References:
1. White, R.H. L-Aspartate semialdehyde and a 6-deoxy-5-ketohexose 1-phosphate are the precursors to the aromatic amino acids in Methanocaldococcus jannaschii. Biochemistry 43 (2004) 7618-7627. [PMID: 15182204]
2. Samland, A.K., Wang, M. and Sprenger, G.A. MJ0400 from Methanocaldococcus jannaschii exhibits fructose-1,6-bisphosphate aldolase activity. FEMS Microbiol. Lett. 281 (2008) 36-41. [PMID: 18318840]
3. Morar, M., White, R.H. and Ealick, S.E. Structure of 2-amino-3,7-dideoxy-D-threo-hept-6-ulosonic acid synthase, a catalyst in the archaeal pathway for the biosynthesis of aromatic amino acids. Biochemistry 46 (2007) 10562-10571. [PMID: 17713928]
Accepted name: 6-deoxy-5-ketofructose 1-phosphate synthase
Reaction: (1) methylglyoxal + D-fructose 1,6-bisphosphate = D-glyceraldehyde 3-phosphate + 1-deoxy-D-threo-hexo-2,5-diulose 6-phosphate
(2) methylglyoxal + D-fructose 1-phosphate = D-glyceraldehyde + 1-deoxy-D-threo-hexo-2,5-diulose 6-phosphate
For diagram of reaction click here.
Glossary: methylglyoxal = 2-oxopropanal
1-deoxy-D-threo-hexo-2,5-diulose 6-phosphate = 6-deoxy-5-ketofructose 1-phosphate
Other name(s): DKFP synthase; MJ1585 (gene name)
Systematic name: 2-oxopropanal:D-fructose 1,6-bisphosphate glycerone-phosphotransferase
Comments: The enzyme plays a key role in an alternative pathway of the biosynthesis of 3-dehydroquinate (DHQ), which is involved in the canonical pathway for the biosynthesis of aromatic amino acids. The enzyme can also catalyse the reaction of EC 4.1.2.13, fructose-bisphosphate aldolase.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:
References:
1. White, R.H. and Xu, H. Methylglyoxal is an intermediate in the biosynthesis of 6-deoxy-5-ketofructose-1-phosphate: a precursor for aromatic amino acid biosynthesis in Methanocaldococcus jannaschii. Biochemistry 45 (2006) 12366-12379. [PMID: 17014089]
2. Samland, A.K., Wang, M. and Sprenger, G.A. MJ0400 from Methanocaldococcus jannaschii exhibits fructose-1,6-bisphosphate aldolase activity. FEMS Microbiol. Lett. 281 (2008) 36-41. [PMID: 18318840]
Accepted name: 3-acetyloctanal synthase
Reaction: pyruvate + (E)-oct-2-enal = (S)-3-acetyloctanal + CO2
Other name(s): pigD (gene name)
Systematic name: pyruvate:(E)-oct-2-enal acetaldehydetransferase (decarboxylating)
Comments: Requires thiamine diphosphate. The enzyme, characterized from the bacterium Serratia marcescens, participates in the biosynthesis of the antibiotic prodigiosin. The enzyme decarboxylates pyruvate, followed by attack of the resulting two-carbon fragment on (E)-oct-2-enal, resulting in a Stetter reaction. In vitro the enzyme can act on a number of α,β-unsaturated carbonyl compounds, including aldehydes and ketones, and can catalyse both 1-2 and 1-4 carboligations depending on the substrate.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number:
References:
1. Williamson, N.R., Simonsen, H.T., Ahmed, R.A., Goldet, G., Slater, H., Woodley, L., Leeper, F.J. and Salmond, G.P. Biosynthesis of the red antibiotic, prodigiosin, in Serratia: identification of a novel 2-methyl-3-n-amyl-pyrrole (MAP) assembly pathway, definition of the terminal condensing enzyme, and implications for undecylprodigiosin biosynthesis in Streptomyces. Mol. Microbiol. 56 (2005) 971-989. [PMID: 15853884]
2. Dresen, C., Richter, M., Pohl, M., Ludeke, S. and Müller, M. The enzymatic asymmetric conjugate umpolung reaction. Angew Chem Int Ed Engl 49 (2010) 6600-6603. [PMID: 20669204]
3. Kasparyan, E., Richter, M., Dresen, C., Walter, L.S., Fuchs, G., Leeper, F.J., Wacker, T., Andrade, S.L., Kolter, G., Pohl, M. and Müller, M. Asymmetric Stetter reactions catalyzed by thiamine diphosphate-dependent enzymes. Appl. Microbiol. Biotechnol. 98 (2014) 9681-9690. [PMID: 24957249]
Accepted name: apulose-4-phosphate transketolase
Reaction: apulose 4-phosphate + D-glyceraldehyde 3-phosphate = D-xylulose 5-phosphate + glycerone phosphate
Glossary: apulose = 1,3,4-trihydroxy-3-(hydroxymethyl)butan-2-one
Other name(s): aptAB (gene names)
Systematic name: apulose-4-phosphate:D-glyceraldehyde-3-phosphate glycolaldehydetransferase
Comments: The enzyme, characterized from several bacterial species, is involved in a catabolic pathway for D-apiose.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number:
References:
1. Carter, M.S., Zhang, X., Huang, H., Bouvier, J.T., Francisco, B.S., Vetting, M.W., Al-Obaidi, N., Bonanno, J.B., Ghosh, A., Zallot, R.G., Andersen, H.M., Almo, S.C. and Gerlt, J.A. Functional assignment of multiple catabolic pathways for D-apiose. Nat. Chem. Biol. 14 (2018) 696-705. [PMID: 29867142]
Accepted name: 6-deoxy-6-sulfo-D-fructose transaldolase
Reaction: 6-deoxy-6-sulfo-D-fructose + D-glyceraldehyde 3-phosphate = (2S)-3-sulfolactaldehyde + β-D-fructofuranose 6-phosphate
Glossary: (2S)-3-sulfolactaldehyde = (2S)-2-hydroxy-3-oxopropane-1-sulfonate
Other name(s): sftT (gene name)
Systematic name: 6-deoxy-6-sulfo-D-fructose:D-glyceraldehyde-3-phosphate glyceronetransferase
Comments: The enzyme, characterized from the bacterium Bacillus aryabhattai SOS1, is involved in a degradation pathway for 6-sulfo-D-quinovose. The enzyme can also use D-erythrose 4-phosphate as the acceptor, forming D-sedoheptulose 7-phosphate.
References:
1. Frommeyer, B., Fiedler, A.W., Oehler, S.R., Hanson, B.T., Loy, A., Franchini, P., Spiteller, D. and Schleheck, D. Environmental and intestinal phylum Firmicutes bacteria metabolize the plant sugar sulfoquinovose via a 6-deoxy-6-sulfofructose transaldolase pathway. iScience 23 (2020) 101510. [PMID: 32919372]
Accepted name: 6-deoxy-6-sulfo-D-fructose transketolase
Reaction: (1) 6-deoxy-6-sulfo-D-fructose + D-glyceraldehyde-3-phosphate = D-xylulose-5-phosphate + 4-deoxy-4-sulfo-D-erythrose
(2) 4-deoxy-4-sulfo-D-erythrulose + D-glyceraldehyde-3-phosphate = D-xylulose-5-phosphate + sulfoacetaldehyde
Other name(s): 6-deoxy-6-sulfo-erythrulose transketolase; sqwGH (gene name)
Systematic name: 6-deoxy-6-sulfo-D-fructose:D-glyceraldehyde-3-phosphate glycolaldehydetransferase
Comments: The enzyme, characterized from the bacterium Clostridium sp. MSTE9, is involved in a D-sulfoquinovose degradation pathway.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number:
References:
1. Liu, J., Wei, Y., Ma, K., An, J., Liu, X., Liu, Y., Ang, E.L., Zhao, H. and Zhang, Y. Mechanistically diverse pathways for sulfoquinovose degradation in bacteria. ACS Catal. 11 (2021) 14740-14750.