See separate file for EC 2.5.1.100 to EC 2.5.1.160
EC 2.5.1.101 to EC 2.5.1.160
Accepted name: β-pyrazolylalanine synthase
Reaction: O-acetyl-L-serine + pyrazole = 3-(pyrazol-1-yl)-L-alanine + acetate
For diagram of reaction click here.
Glossary: O-acetyl-L-serine = (2S)-3-acetyloxy-2-aminopropanoic acid
Other name(s): β-(1-pyrazolyl)alanine synthase; β-pyrazolealanine synthase; β-pyrazolylalanine synthase (acetylserine); O3-acetyl-L-serine acetate-lyase (adding pyrazole); BPA-synthase; pyrazolealanine synthase; pyrazolylalaninase
Systematic name: O-acetyl-L-serine:pyrazole 1-(2-amino-2-carboxyethyl)transferase
Comments: The enzyme is highly specific for acetylserine and pyrazole. Not identical with EC 2.5.1.52 L-mimosine synthase.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 37290-81-6
References:
1. Murakoshi, I., Ikegami, F., Hinuma, Y. and Hanma, Y. Purification and characterization of β-(pyrazol-1-yl)-L-alanine synthase from Citrullus vulgaris. Phytochemistry 23 (1984) 973-977.
2. Murakoshi, I., Ikegami, F., Hinuma, Y. and Hanma, Y. Purification and characterization of L-mimosine synthase from Leucaena leucocephala. Phytochemistry 23 (1984) 1905-1908.
3. Murakoshi, I., Kuramoto, H. and Haginiwa, J. The enzymic synthesis of β-substituted alanines. Phytochemistry 11 (1972) 177-182.
4. Noji, M., Murakoshi, I. and Saito K. Evidence for identity of β-pyrazolealanine synthase with cysteine synthase in watermelon: formation of β-pyrazole-alanine by cloned cysteine synthase in vitro and in vivo. Biochem. Biophys. Res. Commun. 197 (1993) 1111-1117. [PMID: 8280125]
Accepted name: L-mimosine synthase
Reaction: O-acetyl-L-serine + 3,4-dihydroxypyridine = 3-(3,4-dihydroxypyridin-1-yl)-L-alanine + acetate
For diagram of reaction click here.
Glossary: O-acetyl-L-serine = (2S)-3-acetyloxy-2-aminopropanoic acid
L-mimosine = (2S)-2-amino-3-(3-hydroxy-4-oxopyridin-1(4H)-yl)propanoic acid
Other name(s): O3-acetyl-L-serine acetate-lyase (adding 3,4-dihydroxypyridin-1-yl)
Systematic name: O-acetyl-L-serine:3,4-dihydroxypyridine 1-(2-amino-2-carboxyethyl)transferase
Comments: Brings about the biosynthesis of L-mimosine in Mimosa and Leucaena sp. Not identical with EC 2.5.1.51 β-pyrazolylalanine synthase.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 93229-75-5
References:
1. Murakoshi, I., Ikegami, F., Hinuma, Y. and Hanma, Y. Purification and characterization of L-mimosine synthase from Leucaena leucocephala. Phytochemistry 23 (1984) 1905-1908.
Accepted name: uracilylalanine synthase
Reaction: O-acetyl-L-serine + uracil = 3-(uracil-1-yl)-L-alanine + acetate
For diagram of reaction click here.
Glossary: O-acetyl-L-serine = (2S)-3-acetyloxy-2-aminopropanoic acid
3-(uracil-1-yl)-L-alanine = L-willardiine
3-(uracil-3-yl)-L-alanine = L-isowillardiine
Other name(s): O3-acetyl-L-serine acetate-lyase (adding uracil); isowillardiine synthase; willardiine synthase; O3-acetyl-L-serine:uracil 1-(2-amino-2-carboxyethyl)transferase
Systematic name: O-acetyl-L-serine:uracil 1-(2-amino-2-carboxyethyl)transferase
Comments: Both L-willardiine and L-isowillardiine are produced in the reaction. Not identical with EC 2.5.1.47 cysteine synthase.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 113573-73-2
References:
1. Ahmmad, M.A.S., Maskall, C.S. and Brown, E.G. Partial-purification and properties of willardiine and synthase activity from Pisum sativum. Phytochemistry 23 (1984) 265-270.
2. Ikegami, F., Kaneko, M., Lambein, F., Kuo, Y.-H. and Murakoshi, I. Difference between uracilylalanine synthases and cysteine synthases in Pisum sativum. Phytochemistry 26 (1987) 2699-2704.
3. Murakoshi, I., Ikegami, F., Ookawa, N., Ariki, T., Haginiwa, J., Kuo, Y.-H. and Lambein, F. Biosynthesis of the uracilylalanines willardiine and isowillardiine in higher plants. Phytochemistry 17 (1978) 1571-1576.
Accepted name: 3-deoxy-7-phosphoheptulonate synthase
Reaction: phosphoenolpyruvate + D-erythrose 4-phosphate + H2O = 3-deoxy-D-arabino-hept-2-ulosonate 7-phosphate + phosphate
For diagram click here and mechanism here.
Other name(s): 2-dehydro-3-deoxy-phosphoheptonate aldolase; 2-keto-3-deoxy-D-arabino-heptonic acid 7-phosphate synthetase; 3-deoxy-D-arabino-2-heptulosonic acid 7-phosphate synthetase; 3-deoxy-D-arabino-heptolosonate-7-phosphate synthetase; 3-deoxy-D-arabino-heptulosonate 7-phosphate synthetase; 7-phospho-2-keto-3-deoxy-D-arabino-heptonate D-erythrose-4-phosphate lyase (pyruvate-phosphorylating); 7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate D-erythrose-4-phosphate lyase (pyruvate-phosphorylating); D-erythrose-4-phosphate-lyase; D-erythrose-4-phosphate-lyase (pyruvate-phosphorylating); DAH7-P synthase; DAHP synthase; DS-Co; DS-Mn; KDPH synthase; KDPH synthetase; deoxy-D-arabino-heptulosonate-7-phosphate synthetase; phospho-2-dehydro-3-deoxyheptonate aldolase; phospho-2-keto-3-deoxyheptanoate aldolase; phospho-2-keto-3-deoxyheptonate aldolase; phospho-2-keto-3-deoxyheptonic aldolase; phospho-2-oxo-3-deoxyheptonate aldolase
Systematic name: phosphoenolpyruvate:D-erythrose-4-phosphate C-(1-carboxyvinyl)transferase (phosphate-hydrolysing, 2-carboxy-2-oxoethyl-forming)
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 9026-94-2
References:
1. Srinivasan, P.R. and Sprinson, D.B. 2-Keto-3-deoxy-D-arabo-heptonic acid 7-phosphate synthetase. J. Biol. Chem. 234 (1959) 716-722.
2. Jossek, R., Bongaerts, J. and Sprenger, G.A. Characterization of a new feedback-resistant 3-deoxy-D-arabino-heptulosonate 7-phosphate synthase AroF of Escherichia coli. FEMS Microbiol. Lett. 202 (2001) 145-148. [PMID: 11506923]
3. Schneider, T.R., Hartmann, M. and Braus, G.H. Crystallization and preliminary X-ray analysis of D-arabino-heptulosonate-7-phosphate synthase (tyrosine inhibitable) from Saccharomyces cerevisiae. Acta Crystallogr. D Biol. Crystallogr. 55 (1999) 1586-1588. [PMID: 10489454]
Accepted name: 3-deoxy-8-phosphooctulonate synthase
Reaction: phosphoenolpyruvate + D-arabinose 5-phosphate + H2O = 3-deoxy-D-manno-octulosonate 8-phosphate + phosphate
Other name(s): 2-dehydro-3-deoxy-D-octonate-8-phosphate D-arabinose-5-phosphate-lyase (pyruvate-phosphorylating); 2-dehydro-3-deoxy-phosphooctonate aldolase; 2-keto-3-deoxy-8-phosphooctonic synthetase; 3-deoxy-D-manno-octulosonate-8-phosphate synthase; 3-deoxy-D-mannooctulosonate-8-phosphate synthetase; 3-deoxyoctulosonic 8-phosphate synthetase; KDOP synthase; phospho-2-keto-3-deoxyoctonate aldolase
Systematic name: phosphoenolpyruvate:D-arabinose-5-phosphate C-(1-carboxyvinyl)transferase (phosphate-hydrolysing, 2-carboxy-2-oxoethyl-forming)
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 9026-96-4
References:
1. Levin, D.H. and Racker, E. Condensation of arabinose 5-phosphate and phosphorylenol pyruvate by 2-keto-3-deoxy-8-phosphooctonic acid synthetase. J. Biol. Chem. 234 (1959) 2532-25339.
2. Krosky, D.J., Alm, R., Berg, M., Carmel, G., Tummino, P.J., Xu, B. and Yang, W. Helicobacter pylori 3-deoxy-D-manno-octulosonate-8-phosphate (KDO-8-P) synthase is a zinc-metalloenzyme. Biochim. Biophys. Acta 1594 (2002) 297-306. [PMID: 11904225]
3. Asojo, O., Friedman, J., Adir, N., Belakhov, V., Shoham, Y. and Baasov, T. Crystal structures of KDOP synthase in its binary complexes with the substrate phosphoenolpyruvate and with a mechanism-based inhibitor. Biochemistry 40 (2001) 6326-6334. [PMID: 11371194]
Accepted name: N-acetylneuraminate synthase
Reaction: phosphoenolpyruvate + N-acetyl-D-mannosamine + H2O = phosphate + N-acetylneuraminate
For diagram of reaction click here and mechanism click here.
Other name(s): (NANA)condensing enzyme; N-acetylneuraminate pyruvate-lyase (pyruvate-phosphorylating); NeuAc synthase
Systematic name: phosphoenolpyruvate:N-acetyl-D-mannosamine C-(1-carboxyvinyl)transferase (phosphate-hydrolysing, 2-carboxy-2-oxoethyl-forming)
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 37290-66-7
References:
1. Blacklow, R.S. and Warren, L. Biosynthesis of sialic acids by Neisseria meningitidis. J. Biol. Chem. 237 (1962) 3520-3526.
2. Komaki, E., Ohta, Y. and Tsukada, Y. Purification and characterization of N-acetylneuraminate synthase from Escherichia coli K1-M12. Biosci. Biotechnol. Biochem. 61 (1997) 2046-2050. [PMID: 9438985]
Accepted name: N-acylneuraminate-9-phosphate synthase
Reaction: phosphoenolpyruvate + N-acyl-D-mannosamine 6-phosphate + H2O = N-acylneuraminate 9-phosphate + phosphate
For diagram of reaction click here and mechanism click here.
Other name(s): N-acetylneuraminate 9-phosphate lyase; N-acetylneuraminate 9-phosphate sialic acid 9-phosphate synthase; N-acetylneuraminate 9-phosphate synthetase; N-acylneuraminate-9-phosphate pyruvate-lyase (pyruvate-phosphorylating); sialic acid 9-phosphate synthetase
Systematic name: phosphoenolpyruvate:N-acyl-D-mannosamine-6-phosphate 1-(2-carboxy-2-oxoethyl)transferase
Comments: Acts on N-glycoloyl and N-acetyl-derivatives.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 9031-58-7
References:
1. Roseman, S., Jourdian, G.W., Watson, D. and Rood, R. Enzymatic synthesis of sialic acid 9-phosphates. Proc. Natl. Acad. Sci. USA 47 (1961) 958-961.
2. Watson, D.R., Jourdian, G.W. and Roseman, S. The sialic acids. 8. Sialic acid 9-phosphate synthetase. J. Biol. Chem. 241 (1966) 5627-5636. [PMID: 5928202]
3. Nakata, D., Close, B.E., Colley, K.J., Matsuda, T. and Kitajima, K. Molecular cloning and expression of the mouse N-acetylneuraminic acid 9-phosphate synthase which does not have deaminoneuraminic acid (KDN) 9-phosphate synthase activity. Biochem. Biophys. Res. Commun. 273 (2000) 642-648. [PMID: 10873658]
Accepted name: protein farnesyltransferase
Reaction: farnesyl diphosphate + protein-cysteine = S-farnesyl protein + diphosphate
Other name(s): FTase
Systematic name: farnesyl-diphosphate:protein-cysteine farnesyltransferase
Comments: This enzyme, along with protein geranylgeranyltransferase types I (EC 2.5.1.59) and II (EC 2.5.1.60), constitutes the protein prenyltransferase family of enzymes. Catalyses the formation of a thioether linkage between the C-1 of an isoprenyl group and a cysteine residue fourth from the C-terminus of the protein. These protein acceptors have the C-terminal sequence CA1A2X, where the terminal residue, X, is preferably serine, methionine, alanine or glutamine; leucine makes the protein a substrate for EC 2.5.1.59. The enzymes are relaxed in specificity for A1, but cannot act if A2 is aromatic. Substrates of the prenyltransferases include Ras, Rho, Rab, other Ras-related small GTP-binding proteins, γ-subunits of heterotrimeric G-proteins, nuclear lamins, centromeric proteins and many proteins involved in visual signal transduction. A zinc metalloenzyme that requires Mg2+ for activity.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 131384-38-8
References:
1. Furfine, E.S., Leban, J.J., Landavazo, A., Moomaw, J.F. and Casey, P.J. Protein farnesyltransferase: kinetics of farnesyl pyrophosphate binding and product release. Biochemistry 34 (1995) 6857-6862. [PMID: 7756316]
2. Casey, P.J. and Seabra, M.C. Protein prenyltransferases. J. Biol. Chem. 271 (1996) 5289-5292. [PMID: 8621375]
3. Long, S.B., CASey, P.J. and Beese, L.S. Cocrystal structure of protein farnesyltransferase complexed with a farnesyl diphosphate substrate. Biochemistry 37 (1998) 9612-9618. [PMID: 9657673]
4. Micali, E., Chehade, K.A., Isaacs, R.J., Andres, D.A. and Spielmann, H.P. Protein farnesyltransferase isoprenoid substrate discrimination is dependent on isoprene double bonds and branched methyl groups. Biochemistry 40 (2001) 12254-12265. [PMID: 11591144]
5. Long, S.B., CASey, P.J. and Beese, L.S. Reaction path of protein farnesyltransferase at atomic resolution. Nature 419 (2002) 645-650. [PMID: 12374986]
6. Gibbs, R.A. Prenyl transfer and the enzymes of terpenoid and steroid biosynthesis. In: Sinnott, M. (Ed.), Comprehensive Biological Catalysis. A Mechanistic Reference., vol. 1, Academic Press, San Diego, CA, 1998, pp. 31-118.
Accepted name: protein geranylgeranyltransferase type I
Reaction: geranylgeranyl diphosphate + protein-cysteine = S-geranylgeranyl-protein + diphosphate
Other name(s): GGTase-I; GGTaseI
Systematic name: geranylgeranyl-diphosphate:protein-cysteine geranyltransferase
Comments: This enzyme, along with protein farnesyltransferase (EC 2.5.1.58) and protein geranylgeranyltransferase type II (EC 2.5.1.60), constitutes the protein prenyltransferase family of enzymes. Catalyses the formation of a thioether linkage between the C-1 atom of the geranylgeranyl group and a cysteine residue fourth from the C-terminus of the protein. These protein acceptors have the C-terminal sequence CA1A2X, where the terminal residue, X, is preferably leucine; serine, methionine, alanine or glutamine makes the protein a substrate for EC 2.5.1.58. The enzymes are relaxed in specificity for A1, but cannot act if A2 is aromatic. Known targets of this enzyme include most γ-subunits of heterotrimeric G proteins and Ras-related GTPases such as members of the Ras and Rac/Rho families. A zinc metalloenzyme. The Zn2+ is required for peptide, but not for isoprenoid, substrate binding.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 135371-29-8 (same as EC 2.5.1.60)
References:
1. Casey, P.J. and Seabra, M.C. Protein prenyltransferases. J. Biol. Chem. 271 (1996) 5289-5292. [PMID: 8621375]
2. Zhang, F.L. and Casey, P.J. Influence of metal ions on substrate binding and catalytic activity of mammalian protein geranylgeranyltransferase type-I. Biochem. J. 320 (1996) 925-932. [PMID: 9003382]
3. Gibbs, R.A. Prenyl transfer and the enzymes of terpenoid and steroid biosynthesis. In: Sinnott, M. (Ed.), Comprehensive Biological Catalysis. A Mechanistic Reference., vol. 1, Academic Press, San Diego, 1998, pp. 31-118.
Accepted name: protein geranylgeranyltransferase type II
Reaction: geranylgeranyl diphosphate + protein-cysteine = S-geranylgeranyl-protein + diphosphate
Other name(s): GGTaseII; Rab geranylgeranyltransferase; RabGGTase
Systematic name: geranylgeranyl-diphosphate:protein-cysteine geranyltransferase
Comments: This enzyme, along with protein farnesyltransferase (EC 2.5.1.58) and protein geranylgeranyltransferase type I (EC 2.5.1.59), constitutes the protein prenyltransferase family of enzymes. Attaches geranylgeranyl groups to two C-terminal cysteines in Ras-related GTPases of a single family, the Rab family (Ypt/Sec4 in lower eukaryotes) that terminate in XXCC, XCXC and CCXX motifs. Reaction is entirely dependent on the Rab substrate being bound to Rab escort protein (REP). Post-translational modification with the geranylgeranyl moiety is essential for Rab GTPases to be able to control the processes of membrane docking and fusion [5].
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 135371-29-8 (same as EC 2.5.1.59)
References:
1. Casey, P.J. and Seabra, M.C. Protein prenyltransferases. J. Biol. Chem. 271 (1996) 5289-5292. [PMID: 8621375]
2. Wilson, A.L., Erdman, R.A., CAStellano, F. and Maltese, W.A. Prenylation of Rab8 GTPase by type I and type II geranylgeranyl transferases. Biochem. J. 333 (1998) 497-504. [PMID: 9677305]
3. Zhang, H., Seabra, M.C. and Deisenhofer, J. Crystal structure of Rab geranylgeranyltransferase at 2.0 Å resolution. Structure Fold. Des. 8 (2000) 241-251. [PMID: 10745007]
4. Thomä, N.H., Niculae, A., Goody, R.S. and Alexandrov, K. Double prenylation by RabGGTase can proceed without dissociation of the mono-prenylated intermediate. J. Biol. Chem. 276 (2001) 48631-48636. [PMID: 11591706]
5. Rak, A., Niculae, A., Kalinin, A., Thomä, N.H., Sidorovitch, V., Goody, R.S. and Alexandrov, K. In vitro assembly, purification, and crystallization of the Rab geranylgeranyl transferase:substrate complex. Protein Expr. Purif. 25 (2002) 23-30. [PMID: 12071695]
6. Gibbs, R.A. Prenyl transfer and the enzymes of terpenoid and steroid biosynthesis. In: Sinnott, M. (Ed.), Comprehensive Biological Catalysis. A Mechanistic Reference., vol. 1, Academic Press, San Diego, CA, 1998, pp. 31-118.
Accepted name: hydroxymethylbilane synthase
Reaction: 4 porphobilinogen + H2O = hydroxymethylbilane + 4 NH3
For diagram click here.
Other name(s): HMB-synthase; porphobilinogen deaminase; pre-uroporphyrinogen synthase; uroporphyrinogen I synthase; uroporphyrinogen I synthetase; uroporphyrinogen synthase; uroporphyrinogen synthetase; porphobilinogen ammonia-lyase (polymerizing); (4-[2-carboxyethyl]-3-[carboxymethyl]pyrrol-2-yl)methyltransferase (hydrolysing)
Systematic name: porphobilinogen:(4-[2-carboxyethyl]-3-[carboxymethyl]pyrrol-2-yl)methyltransferase (hydrolysing)
Comments: The enzyme works by stepwise addition of pyrrolylmethyl groups until a hexapyrrole is present at the active centre. The terminal tetrapyrrole is then hydrolysed to yield the product, leaving a cysteine-bound dipyrrole on which assembly continues. In the presence of a second enzyme, EC 4.2.1.75 uroporphyrinogen-III synthase, which is often called cosynthase, the product is cyclized to form uroporphyrinogen-III. If EC 4.2.1.75 is absent, the hydroxymethylbilane cyclizes spontaneously to form uroporphyrinogen I.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 9074-91-3
References:
1. Battersby, A.R., Fookes, C.J.R., Matcham, G.W.J. and McDonald, E. Biosynthesis of the pigments of life: formation of the macrocycle. Nature 285 (1980) 17-21. [PMID: 6769048]
2. Frydman, R.B. and Feinstein, G. Studies on porphobilinogen deaminase and uroporphyrinogen 3 cosynthase from human erythrocytes. Biochim. Biophys. Acta 350 (1974) 358-373. [PMID: 4847568]
3. Levin, E.Y. and Coleman, D.L. The enzymatic conversion of porphobilinogen to uroporphyrinogen catalyzed by extracts of hematopoietic mouse spleen. J. Biol. Chem. 242 (1967) 4247-4253. [PMID: 6061709]
4. Warren, M.J. and Jordan P.M. Investigation into the nature of substrate binding to the dipyrromethane cofactor of Escherichia coli porphobilinogen deaminase. Biochemistry 27 (1988) 9020-9030. [PMID: 3069132]
5. Miller, A.D., Hart, G.J., Packman, L.C. and Battersby, A.R. Evidence that the pyrromethane cofactor of hydroxymethylbilane synthase (porphobilinogen deaminase) is bound to the protein through the sulphur atom of cysteine-242. Biochem. J. 254 (1988) 915-918. [PMID: 3196304]
6. Battersby, A.R. Tetrapyrroles: the pigments of life. Nat. Prod. Rep. 17 (2000) 507-526. [PMID: 11152419]
Accepted name: chlorophyll synthase
Reaction: chlorophyllide a + phytyl diphosphate = chlorophyll a + diphosphate
For diagram of reaction click here or click here.
Systematic name: chlorophyllide-a:phytyl-diphosphate phytyltransferase
Comments: Requires Mg2+. The enzyme is modified by binding of the first substrate, phytyl diphosphate, before reaction of the modified enzyme with the second substrate, chlorophyllide a, can occur. The reaction also occurs when phytyl diphosphate is replaced by geranylgeranyl diphosphate.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 9077-08-1
References:
1. Schmid, H.C., Rassadina, V., Oster, U., Schoch, S. and Rüdiger, W. Pre-loading of chlorophyll synthase with tetraprenyl diphosphate is an obligatory step in chlorophyll biosynthesis. Biol. Chem. 383 (2002) 1769-1778. [PMID: 12530542]
2. Oster, U., Bauer, C.E. and Rüdiger, W. Characterization of chlorophyll a and bacteriochlorophyll a synthases by heterologous expression in Escherichia coli. J. Biol. Chem. 272 (1997) 9671-9676. [PMID: 9092496]
3. Rüdiger, W., Benz, J. and Guthoff. C. Detection and partial characterization of activity of chlorophyll synthetase in etioplast membranes. Eur. J. Biochem. 109 (1980) 193-200. [PMID: 7408876]
Accepted name: adenosyl-fluoride synthase
Reaction: S-adenosyl-L-methionine + fluoride = 5'-deoxy-5'-fluoroadenosine + L-methionine
Other name(s): fluorinase
Systematic name: S-adenosyl-L-methionine:fluoride adenosyltransferase
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 438583-16-5
References:
1. O'Hagan, D., Schaffrath, C., Cobb, S.L., Hamilton, J.T. and Murphy, C.D. Biosynthesis of an organofluorine molecule. Nature 416 (2002) 279 only. [PMID: 11907567]
2. Dong, C., Huang, F., Deng, H., Schaffrath, C., Specner, J.B., O'Hagan, D. and Naismith, J.H. Crystal structure and mechanism of a bacterial fluorinating enzyme. Nature 427 (2004) 561-565. [PMID: 14765200]
[EC 2.5.1.64 Transferred entry: 2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase. The reaction that was attributed to this enzyme is now known to be catalysed by two separate enzymes: EC 2.2.1.9 EC 2.2.1.9 (2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carboxylic-acid synthase) and EC 4.2.99.20 (2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase). (EC 2.5.1.64 created 2003, deleted 2008)]
Accepted name: O-phosphoserine sulfhydrylase
Reaction: O-phospho-L-serine + hydrogen sulfide = L-cysteine + phosphate
Other name(s): O-phosphoserine(thiol)-lyase
Systematic name: O-phospho-L-serine:hydrogen-sulfide 2-amino-2-carboxyethyltransferase
Comments: A pyridoxal-phosphate protein. The enzyme from Aeropyrum pernix acts on both O-phospho-L-serine and O3-acetyl-L-serine, in contrast with EC 2.5.1.47, cysteine synthase, which acts only on O3-acetyl-L-serine.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 1071505-11-7
References:
1. Mino, K. and Ishikawa, K. A novel O-phospho-L-serine sulfhydrylation reaction catalyzed by O-acetylserine sulfhydrylase from Aeropyrum pernix K1. FEBS Lett. 551 (2003) 133-138. [PMID: 12965218]
2. Mino, K. and Ishikawa, K. Characterization of a novel thermostable O-acetylserine sulfhydrylase from Aeropyrum pernix K1. J. Bacteriol. 185 (2003) 2277-2284. [PMID: 12644499]
3. Mino, K. and Ishikawa, K. Crystallization and preliminary X-ray diffraction analysis of O-acetylserine sulfhydrylase from Aeropyrum pernix K1. Acta Crystallogr. D Biol. Crystallogr. 59 (2003) 338-340. [PMID: 12554945]
Accepted name: N2-(2-carboxyethyl)arginine synthase
Reaction: D-glyceraldehdye 3-phosphate + L-arginine = N2-(2-carboxyethyl)-L-arginine + phosphate
For diagram click here.
Other name(s): CEAS; N2-(2-carboxyethyl)arginine synthetase; CEA synthetase
Systematic name: glyceraldehyde-3-phosphate:L-arginine N2-(2-hydroxy-3-oxopropyl) transferase (2-carboxyethyl-forming)
Comments: The enzyme requires thiamine diphosphate and catalyses the first step in the clavulanic-acid-biosynthesis pathway. The 2-hydroxy-3-oxo group transferred from glyceraldehyde 3-phosphate is isomerized during transfer to form the 2-carboxyethyl group.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 250207-48-8
References:
1. Caines, M.E.C., Elkins, J.M., Hewitson, K.S. and Schofield, C.J. Crystal structure and mechanistic implications of N2-(2-carboxyethyl)arginine synthase, the first enzymes in the clavulanic acid biosynthesis pathway. J. Biol. Chem. 279 (2004) 5685-5692. [PMID: 14623876]
2. Khaleeli, N., Li, R. and Townsend, C.A. Origin of the β-lactam carbons in clavulanic acid from an unusual thiamine pyrophosphate-mediated reaction. J. Am. Chem. Soc. 121 (1999) 9223-9224.
Accepted name: chrysanthemyl diphosphate synthase
Reaction: 2 dimethylallyl diphosphate = diphosphate + chrysanthemyl diphosphate
For diagram of reaction click here
Other name(s): CPPase
Systematic name: dimethylallyl-diphosphate:dimethylallyl-diphosphate dimethylallyltransferase (chrysanthemyl-diphosphate-forming)
Comments: Requires a divalent metal ion for activity, with Mg2+ being better than Mn2+ [1]. Chrysanthemyl diphosphate is a monoterpenoid with a non-head-to-tail linkage. It is unlike most monoterpenoids, which are derived from geranyl diphosphate and have isoprene units that are linked head-to-tail. The mechanism of its formation is similar to that of the early steps of squalene and phytoene biosynthesis. Chrysanthemyl diphosphate is the precursor of chrysanthemic acid, the acid half of the pyrethroid insecticides found in chrysanthemums.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number:
References:
1. Rivera, S.B., Swedlund, B.D., King, G.J., Bell, R.N., Hussey, C.E., Jr., Shattuck-Eidens, D.M., Wrobel, W.M., Peiser, G.D. and Poulter, C.D. Chrysanthemyl diphosphate synthase: isolation of the gene and characterization of the recombinant non-head-to-tail monoterpene synthase from Chrysanthemum cinerariaefolium. Proc. Natl. Acad. Sci. USA 98 (2001) 4373-4378. [PMID: 11287653]
2. Erickson, H.K. and Poulter, C.D. Chrysanthemyl diphosphate synthase. The relationship among chain elongation, branching, and cyclopropanation reactions in the isoprenoid biosynthetic pathway. J. Am. Chem. Soc. 125 (2003) 6886-6888. [PMID: 12783539]
Accepted name: (2Z,6E)-farnesyl diphosphate synthase
Reaction: geranyl diphosphate + isopentenyl diphosphate = diphosphate + (2Z,6E)-farnesyl diphosphate
For diagram of reaction, click here.
Other name(s): (Z)-farnesyl diphosphate synthase; Z-farnesyl diphosphate synthase
Systematic name: geranyl-diphosphate:isopentenyl-diphosphate geranylcistransferase
Comments: Requires Mg2+ or Mn2+ for activity. The product of this reaction is an intermediate in the synthesis of decaprenyl phosphate, which plays a central role in the biosynthesis of most features of the mycobacterial cell wall, including peptidoglycan, linker unit galactan and arabinan. Neryl diphosphate can also act as substrate.
Links to other databases: BRENDA, EXPASY, KEGG Metacyc, PDB, CAS registry number:
References:
1. Schulbach, M.C., Mahapatra, S., Macchia, M., Barontini, S., Papi, C., Minutolo, F., Bertini, S., Brennan, P.J. and Crick, D.C. Purification, enzymatic characterization, and inhibition of the Z-farnesyl diphosphate synthase from Mycobacterium tuberculosis. J. Biol. Chem. 276 (2001) 11624-11630. [PMID: 11152452]
Accepted name: lavandulyl diphosphate synthase
Reaction: 2 dimethylallyl diphosphate = diphosphate + lavandulyl diphosphate
For diagram of reaction click here
Other name(s): FDS-5
Systematic name: dimethylallyl-diphosphate:dimethylallyl-diphosphate dimethylallyltransferase (lavandulyl-diphosphate-forming)
Comments: Lavandulyl diphosphate is a monoterpenoid with a non-head-to-tail linkage. It is unlike most monoterpenoids, which are derived from geranyl diphosphate and have isoprene units that are linked head-to-tail. When this enzyme is incubated with dimethylallyl diphosphate and isopentenyl diphosphate, it also forms the regular monoterpene geranyl diphosphate [2]. The enzyme from Artemisia tridentata (big sagebrush) forms both lavandulyl diphosphate and chrysanthemyl diphosphate (see EC 2.5.1.67, chrysanthemyl diphosphate synthase) when dimethylally diphosphate is the sole substrate.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number:
References:
1. Erickson, H.K. and Poulter, C.D. Chrysanthemyl diphosphate synthase. The relationship among chain elongation, branching, and cyclopropanation reactions in the isoprenoid biosynthetic pathway. J. Am. Chem. Soc. 125 (2003) 6886-6888. [PMID: 12783539]
2. Hemmerlin, A., Rivera, S.B., Erickson, H.K. and Poulter, C.D. Enzymes encoded by the farnesyl diphosphate synthase gene family in the Big Sagebrush Artemisia tridentata ssp. spiciformis. J. Biol. Chem. 278 (2003) 32132-32140. [PMID: 12782626]
Accepted name: naringenin 8-dimethylallyltransferase
Reaction: dimethylallyl diphosphate + (–)-(2S)-naringenin = diphosphate + sophoraflavanone B
For diagram of reaction, click here
Glossary: (–)-(2S)-naringenin = (–)-(2S)-5,7-dihydroxy-2-(4-hydroxyphenyl)chroman-4-one
sophoraflavanone B = (–)-(2S)-8-dimethylallylnaringenin = (–)-(2S)-5,7-dihydroxy-2-(4-hydroxyphenyl)-8-(3-methylbut-2-enyl)chroman-4-one
Other name(s): N8DT
Systematic name: dimethylallyl-diphosphate:naringenin 8-dimethylallyltransferase
Comments: Requires Mg2+. This membrane-bound protein is located in the plastids [2]. In addition to naringenin, the enzyme can prenylate several other flavanones at the C-8 position, but more slowly. Along with EC 1.14.13.103 (8-dimethylallylnaringenin 2'-hydroxylase) and EC 2.5.1.71 (leachianone G 2"-dimethylallyltransferase), this enzyme forms part of the sophoraflavanone-G-biosynthesis pathway.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:
References:
1. Yamamoto, H., Senda, M. and Inoue, K. Flavanone 8-dimethylallyltransferase in Sophora flavescens cell suspension cultures. Phytochemistry 54 (2000) 649-655. [PMID: 10975499]
2. Zhao, P., Inoue, K., Kouno, I. and Yamamoto, H. Characterization of leachianone G 2"-dimethylallyltransferase, a novel prenyl side-chain elongation enzyme for the formation of the lavandulyl group of sophoraflavanone G in Sophora flavescens Ait. cell suspension cultures. Plant Physiol. 133 (2003) 1306-1313. [PMID: 14551337]
Accepted name: leachianone-G 2"-dimethylallyltransferase
Reaction: dimethylallyl diphosphate + leachianone G = diphosphate + sophoraflavanone G
For diagram of reaction, click here
Glossary: leachianone G = (–-)-(2S)-2′-hydroxy-8-dimethylallylnaringenin = (–)-(2S)-2-(2,4-dihydroxyphenyl)-5,7-dihydroxy-8-(3-methylbut-2-en-1-yl)chroman-4-one
sophoraflavanone G = (2S)-2-(2,4-dihydroxyphenyl)-5,7-dihydroxy-8-[(2R)-2-(prop-1-en-2-yl)hex-4-en-1-yl]chroman-4-one
Other name(s): LG 2"-dimethylallyltransferase; leachianone G 2"-dimethylallyltransferase; LGDT
Systematic name: dimethylallyl-diphosphate:leachianone-G 2"-dimethylallyltransferase
Comments: This membrane-bound enzyme is located in the plastids and requires Mg2+ for activity. The reaction forms the lavandulyl sidechain of sophoraflavanone G by transferring a dimethylallyl group to the 2" position of another dimethylallyl group attached at postiion 8 of leachianone G. The enzyme is specific for dimethylallyl diphosphate as the prenyl donor, as it cannot be replaced by isopentenyl diphosphate or geranyl diphosphate. Euchrenone a7 (a 5-deoxy derivative of leachianone G) and kenusanone I (a 7-methoxy derivative of leachianone G) can also act as substrates, but more slowly. Along with EC 1.14.13.103 (8-dimethylallylnaringenin 2'-hydroxylase) and EC 2.5.1.70 (naringenin 8-dimethylallyltransferase), this enzyme forms part of the sophoraflavanone-G biosynthesis pathway.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:
References:
1. Zhao, P., Inoue, K., Kouno, I. and Yamamoto, H. Characterization of leachianone G 2"-dimethylallyltransferase, a novel prenyl side-chain elongation enzyme for the formation of the lavandulyl group of sophoraflavanone G in Sophora flavescens Ait. cell suspension cultures. Plant Physiol. 133 (2003) 1306-1313. [PMID: 14551337]
Accepted name: quinolinate synthase
Reaction: glycerone phosphate + iminosuccinate = pyridine-2,3-dicarboxylate + 2 H2O + phosphate
For diagram of reaction click here.
Glossary: quinolinate = pyridine-2,3-dicarboxylate
glycerone phosphate = dihydroxyacetone phosphate = 3-hydroxy-2-oxopropyl phosphate
Other name(s): NadA; QS; quinolinate synthetase
Systematic name: glycerone-phosphate:iminosuccinate alkyltransferase (cyclizing)
Comments: An iron-sulfur protein that requires a [4Fe-4S] cluster for activity [1]. Quinolinate synthase catalyses the second step in the de novo biosynthesis of NAD+ from aspartate in some bacteria, with EC 1.4.3.16 (L-aspartate oxidase) catalysing the first step and EC 2.4.2.19 [nicotinate-nucleotide diphosphorylase (carboxylating)] the third step. In Escherichia coli, two of the residues that are involved in the [4Fe-4S] cluster binding appear to undergo reversible disulfide-bond formation that regulates the activity of the enzyme [5].
Links to other databases: BRENDA, EXPASY, KEGG, PDB, Metacyc, PDB, CAS registry number:
References:
1. Ollagnier-de Choudens, S., Loiseau, L., Sanakis, Y., Barras, F. and Fontecave, M. Quinolinate synthetase, an iron-sulfur enzyme in NAD biosynthesis. FEBS Lett. 579 (2005) 3737-3743. [PMID: 15967443]
2. 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]
3. Sakuraba, H., Tsuge, H., Yoneda, K., Katunuma, N. and Ohshima, T. Crystal structure of the NAD biosynthetic enzyme quinolinate synthase. J. Biol. Chem. 280 (2005) 26645-26648. [PMID: 15937336]
4. Rousset, C., Fontecave, M. and Ollagnier de Choudens, S. The [4Fe-4S] cluster of quinolinate synthase from Escherichia coli: Investigation of cluster ligands. FEBS Lett. 582 (2008) 2937-2944. [PMID: 18674537]
5. Saunders, A.H. and Booker, S.J. Regulation of the activity of Escherichia coli quinolinate synthase by reversible disulfide-bond formation. Biochemistry 47 (2008) 8467-8469. [PMID: 18651751]
Accepted name: O-phospho-L-seryl-tRNA:Cys-tRNA synthase
Reaction: O-phospho-L-seryl-tRNACys + sulfide = L-cysteinyl-tRNACys + phosphate
Other name(s): SepCysS; Sep-tRNA:Cys-tRNA synthase
Systematic name: O-phospho-L-seryl-tRNACys:hydrogen sulfide 2-aminopropanoate transferase
Comments: In organisms like Archaeoglobus fulgidus lacking EC 6.1.1.16 (cysteine—tRNA ligase) for the direct Cys-tRNACys formation, Cys-tRNACys is produced by an indirect pathway, in which EC 6.1.1.27 (O-phosphoseryl-tRNA ligase) ligates O-phosphoserine to tRNACys, and EC 2.5.1.73 converts the produced O-phospho-L-seryl-tRNACys to Cys-tRNACys. The SepRS/SepCysS pathway is the sole route for cysteine biosynthesis in the organism [1]. Methanosarcina mazei can use both pathways, the direct route using EC 6.1.1.16 (cysteine—tRNA ligase) and the indirect pathway with EC 6.1.1.27 (O-phosphoseryl-tRNA ligase) and EC 2.5.1.73 [2].
Links to other databases: BRENDA, EXPASY, KEGG, PDB, Metacyc, PDB, CAS registry number: 1239229-21-0
References:
1. Fukunaga, R. and Yokoyama, S. Structural insights into the second step of RNA-dependent cysteine biosynthesis in archaea: crystal structure of Sep-tRNA:Cys-tRNA synthase from Archaeoglobus fulgidus. J. Mol. Biol. 370 (2007) 128-141. [PMID: 17512006]
2. Hauenstein, S.I. and Perona, J.J. Redundant synthesis of cysteinyl-tRNACys in Methanosarcina mazei. J. Biol. Chem. 283 (2008) 22007-22017. [PMID: 18559341]
3. Yuan, J., Palioura, S., Salazar, J.C., Su, D., O'Donoghue, P., Hohn, M.J., Cardoso, A.M., Whitman, W.B. and Soll, D. RNA-dependent conversion of phosphoserine forms selenocysteine in eukaryotes and archaea. Proc. Natl. Acad. Sci. USA 103 (2006) 18923-18927. [PMID: 17142313]
Accepted name: 1,4-dihydroxy-2-naphthoate polyprenyltransferase
Reaction: an all-trans-polyprenyl diphosphate + 1,4-dihydroxy-2-naphthoate = a demethylmenaquinol + diphosphate + CO2
For diagram of reaction click here.
Glossary: menaquinone = vitamin K2
Systematic name: all-trans-polyprenyl-diphosphate:1,4-dihydroxy-2-naphthoate polyprenyltransferase
Comments: This enzyme catalyses a step in the synthesis of menaquinone, in which the prenyl chain synthesized by polyprenyl diphosphate synthase is transferred to 1,4-dihydroxy-2-naphthoate (DHNA). The bacterial enzyme is an inner membrane protein [1], with the C-terminus located in the periplasm [3]. It is highly specific for DHNA but not for a specific length of the prenyl chain [2].
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:
References:
1. Shineberg, B. and Young, I.G. Biosynthesis of bacterial menaquinones: the membrane-associated 1,4-dihydroxy-2-naphthoate octaprenyltransferase of Escherichia coli. Biochemistry 15 (1976) 2754-2758. [PMID: 949474]
2. Saito, Y. and Ogura, K. Biosynthesis of menaquinones. Enzymatic prenylation of 1,4-dihydroxy-2-naphthoate by Micrococcus luteus membrane fractions. J. Biochem. 89 (1981) 1445-1452. [PMID: 7275947]
3. Suvarna, K., Stevenson, D., Meganathan, R. and Hudspeth, M.E. Menaquinone (vitamin K2) biosynthesis: localization and characterization of the menA gene from Escherichia coli. J. Bacteriol. 180 (1998) 2782-2787. [PMID: 9573170]
4. Daley, D.O., Rapp, M., Granseth, E., Melen, K., Drew, D. and von Heijne, G. Global topology analysis of the Escherichia coli inner membrane proteome. Science 308 (2005) 1321-1323. [PMID: 15919996]
Accepted name: tRNA dimethylallyltransferase
Reaction: prenyl diphosphate + adenine37 in tRNA = diphosphate + N6-prenyladenine37 in tRNA
For diagram of reaction click here.
Other name(s): tRNA prenyltransferase, MiaA, transfer ribonucleate isopentenyltransferase (incorrect); Δ2-isopentenyl pyrophosphate:tRNA-Δ2-isopentenyl transferase (incorrect); Δ2-isopentenyl pyrophosphate:transfer ribonucleic acid Δ2-isopentenyltransferase (incorrect); dimethylallyl-diphosphate: tRNA dimethylallyltransferase; dimethylallyl-diphosphate:adenine37 in tRNA dimethylallyltransferase
Systematic name: prenyl-diphosphate:adenine37 in tRNA dimethylallyltransferase
Comments: Formerly known as tRNA isopentenyltransferase EC 2.5.1.8, but it is now known that dimethyallyl diphosphate, rather than isopentenyl diphosphate, is the substrate,
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number:
References:
1. Leung, H.C., Chen, Y. and Winkler, M.E. Regulation of substrate recognition by the MiaA tRNA prenyltransferase modification enzyme of Escherichia coli K-12. J. Biol. Chem. 272 (1997) 13073-13083. [PMID: 9148919]
2. Soderberg, T. and Poulter, C.D. Escherichia coli dimethylallyl diphosphate:tRNA dimethylallyltransferase: essential elements for recognition of tRNA substrates within the anticodon stem-loop. Biochemistry 39 (2000) 6546-6553. [PMID: 10828971]
3. Moore, J.A., Mathis, J.R. and Poulter, C.D. Escherichia coli dimethylallyl diphosphate:tRNA dimethylallyltransferase: pre-steady-state kinetic studies. Biochim. Biophys. Acta 1479 (2000) 166-174. [PMID: 11004538]
Accepted name: cysteate synthase
Reaction: O-phospho-L-serine + sulfite = L-cysteate + phosphate
Other name(s): sulfite:O-phospho-L-serine sulfotransferase (phosphate-hydrolysing, L-cysteate-forming).
Systematic name: sulfite:O-phospho-L-serine sulfonotransferase (phosphate-hydrolysing, L-cysteate-forming).
Comments: A pyridoxal-phosphate protein. It is highly specific for O-phospho-L-serine and sulfite. The reaction proceeds through a dehydroalanine (2-aminoacrylic acid) intermediate. The enzyme from Methanosarcina acetivorans is evolutionarily related to threonine synthase (EC 4.2.3.1), but the reaction is more similar to that of O-phosphoserine sulfhydrylase (EC 2.5.1.65).
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:
References:
1. Graham, D.E., Taylor, S.M., Wolf, R.Z. and Namboori, S.C. Convergent evolution of coenzyme M biosynthesis in the Methanosarcinales: cysteate synthase evolved from an ancestral threonine synthase. Biochem. J. 424 (2009) 467-478. [PMID: 19761441]
[EC 2.5.1.77 Transferred entry: 7,8-didemethyl-8-hydroxy-5-deazariboflavin synthase. Now EC 2.5.1.147, 5-amino-6-(D-ribitylamino)uracil—L-tyrosine 4-methylphenol transferase and EC 4.3.1.32, 7,8-didemethyl-8-hydroxy-5-deazariboflavin synthase. (EC 2.5.1.77 created 2010, deleted 2017)]
Accepted name: 6,7-dimethyl-8-ribityllumazine synthase
Reaction: 1-deoxy-L-glycero-tetrulose 4-phosphate + 5-amino-6-(D-ribitylamino)uracil = 6,7-dimethyl-8-(D-ribityl)lumazine + 2 H2O + phosphate
For reaction click here and mechanism click here
Glossary: 5-amino-6-(1-D-ribitylamino)pyrimidine-2,4(1H,3H)-dione = 5-amino-6-(1-D-ribitylamino)-2,4-dihydroxypyrimidine = 6-(1-D-ribitylamino)-5-amino-2,4-dihydroxypyrimidine = 6-(1-D-ribitylamino)-5-aminouracil = 5-amino-6-ribitylamino-2,4(1H,3H)-pyrimidinedione
6,7-dimethyl-8-(1-D-ribityl)lumazine = 1-deoxy-1-(6,7-dimethyl-2,4-dioxo-3,4-dihydropteridin-8(2H)-yl)-D-ribitol
(S)-2-hydroxy-3-oxobutyl dihydrogen phosphate = (3S)-3-hydroxy-4-(phosphonooxy)butan-2-one = (2S)-2-hydroxy-3-oxobutyl phosphate = L-3,4-dihydroxybutan-2-one 4-phosphate = (S)-3-hydroxy-4-(phosphonooxy)-2-butanone
Other name(s): lumazine synthase, 6,7-dimethyl-8-ribityllumazine synthase 2; 6,7-dimethyl-8-ribityllumazine synthase 1; lumazine synthase 2; lumazine synthase 1; type I lumazine synthase; type II lumazine synthase; RIB4; MJ0303; RibH; Pbls; MbtLS; RibH1 protein; RibH2 protein; RibH1; RibH2
Systematic name: 5-amino-6-(D-ribitylamino)uracil butanedionetransferase
Comments: Involved in riboflavin biosynthesis.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number:
References:
1. Kis, K., Volk, R. and Bacher, A. Biosynthesis of riboflavin. Studies on the reaction mechanism of 6,7-dimethyl-8-ribityllumazine synthase. Biochemistry 34 (1995) 2883-2892. [PMID: 7893702]
2. Garcia-Ramirez, J.J., Santos, M.A. and Revuelta, J.L. The Saccharomyces cerevisiae RIB4 gene codes for 6,7-dimethyl-8-ribityllumazine synthase involved in riboflavin biosynthesis. Molecular characterization of the gene and purification of the encoded protein. J. Biol. Chem. 270 (1995) 23801-23807. [PMID: 7559556]
3. Bacher, A., Fischer, M., Kis, K., Kugelbrey, K., Mörtl, S., Scheuring, J., Weinkauf, S., Eberhardt, S., Schmidt-Bäse, K., Huber, R., Ritsert, K., Cushman, M., Ladenstein, R. Biosynthesis of riboflavin: structure and mechanism of lumazine synthase. Biochem. Soc. Trans. 24 (1996) 89-94. [PMID: 8674771]
4. Mortl, S., Fischer, M., Richter, G., Tack, J., Weinkauf, S. and Bacher, A. Biosynthesis of riboflavin. Lumazine synthase of Escherichia coli. J. Biol. Chem. 271 (1996) 33201-33207. [PMID: 8969176]
5. Bacher, A., Eberhardt, S., Fischer, M., Mortl, S., Kis, K., Kugelbrey, K., Scheuring, J. and Schott, K. Biosynthesis of riboflavin: lumazine synthase and riboflavin synthase. Methods Enzymol. 280 (1997) 389-399. [PMID: 9211334]
6. Goldbaum, F.A., Velikovsky, C.A., Baldi, P.C., Mortl, S., Bacher, A. and Fossati, C.A. The 18-kDa cytoplasmic protein of Brucella species - an antigen useful for diagnosis- is a lumazine synthase. J Med Microbiol 48 (1999) 833-839. [PMID: 10482294]
7. Jordan, D.B., Bacot, K.O., Carlson, T.J., Kessel, M. and Viitanen, P.V. Plant riboflavin biosynthesis. Cloning, chloroplast localization, expression, purification, and partial characterization of spinach lumazine synthase. J. Biol. Chem. 274 (1999) 22114-22121. [PMID: 10419541]
8. Zhang, X., Meining, W., Fischer, M., Bacher, A. and Ladenstein, R. X-ray structure analysis and crystallographic refinement of lumazine synthase from the hyperthermophile Aquifex aeolicus at 1.6 Å resolution: determinants of thermostability revealed from structural comparisons. J. Mol. Biol. 306 (2001) 1099-1114. [PMID: 11237620]
9. Fischer, M., Haase, I., Feicht, R., Richter, G., Gerhardt, S., Changeux, J.P., Huber, R. and Bacher, A. Biosynthesis of riboflavin: 6,7-dimethyl-8-ribityllumazine synthase of Schizosaccharomyces pombe. Eur. J. Biochem. 269 (2002) 519-526. [PMID: 11856310]
10. Cushman, M., Yang, D., Gerhardt, S., Huber, R., Fischer, M., Kis, K. and Bacher, A. Design, synthesis, and evaluation of 6-carboxyalkyl and 6-phosphonoxyalkyl derivatives of 7-oxo-8-ribitylaminolumazines as inhibitors of riboflavin synthase and lumazine synthase. J. Org. Chem. 67 (2002) 5807-5816. [PMID: 12153285]
11. Haase, I., Mortl, S., Kohler, P., Bacher, A. and Fischer, M. Biosynthesis of riboflavin in archaea. 6,7-dimethyl-8-ribityllumazine synthase of Methanococcus jannaschii. Eur. J. Biochem. 270 (2003) 1025-1032. [PMID: 12603336]
12. Morgunova, E., Meining, W., Illarionov, B., Haase, I., Jin, G., Bacher, A., Cushman, M., Fischer, M. and Ladenstein, R. Crystal structure of lumazine synthase from Mycobacterium tuberculosis as a target for rational drug design: binding mode of a new class of purinetrione inhibitors. Biochemistry 44 (2005) 2746-2758. [PMID: 15723519]
Accepted name: thermospermine synthase
Reaction: S-adenosyl 3-(methylsulfanyl)propylamine + spermidine = S-methyl-5'-thioadenosine + thermospermine + H+
Glossary: thermospermine = N1-[3-(3-aminopropylamino)propyl]butane-1,4-diamine
S-adenosyl 3-(methylsulfanyl)propylamine = (3-aminopropyl){[(2S,3S,4R,5R)-5-(6-amino-9H-purin-9-yl)-3,4-dihydroxytetrahydrofuran-2-yl]methyl}methylsulfonium
Other name(s): TSPMS; ACL5; SAC51; S-adenosyl 3-(methylthio)propylamine:spermidine 3-aminopropyltransferase (thermospermine synthesizing)
Systematic name: S-adenosyl 3-(methylsulfanyl)propylamine:spermidine 3-aminopropyltransferase (thermospermine forming)
Comments: This enzyme is crucial for the proper functioning of xylem vessel elements in the vascular tissues of plants [3].
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number:
References:
1. Romer, P., Faltermeier, A., Mertins, V., Gedrange, T., Mai, R. and Proff, P. Investigations about N-aminopropyl transferases probably involved in biomineralization. J. Physiol. Pharmacol. 59 Suppl 5 (2008) 27-37. [PMID: 19075322]
2. Knott, J.M., Romer, P. and Sumper, M. Putative spermine synthases from Thalassiosira pseudonana and Arabidopsis thaliana synthesize thermospermine rather than spermine. FEBS Lett. 581 (2007) 3081-3086. [PMID: 17560575]
3. Muniz, L., Minguet, E.G., Singh, S.K., Pesquet, E., Vera-Sirera, F., Moreau-Courtois, C.L., Carbonell, J., Blazquez, M.A. and Tuominen, H. ACAULIS5 controls Arabidopsis xylem specification through the prevention of premature cell death. Development 135 (2008) 2573-2582. [PMID: 18599510]
Accepted name: 7-dimethylallyltryptophan synthase
Reaction: dimethylallyl diphosphate + L-tryptophan = diphosphate + 7-(3-methylbut-2-enyl)-L-tryptophan
Other name(s): 7-DMATS
Systematic name: dimethylallyl-diphosphate:L-tryptophan 7-dimethylallyltransferase
Comments: This enzyme is more flexible towards the aromatic substrate than EC 2.5.1.34 (4-dimethylallyltryptophan synthase), but similar to that enzyme, accepts only dimethylallyl diphosphate as the prenyl donor.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:
References:
1. Kremer, A. and Li, S.M. Potential of a 7-dimethylallyltryptophan synthase as a tool for production of prenylated indole derivatives. Appl. Microbiol. Biotechnol. 79 (2008) 951-961. [PMID: 18481055]
2. Kremer, A., Westrich, L. and Li, S.M. A 7-dimethylallyltryptophan synthase from Aspergillus fumigatus: overproduction, purification and biochemical characterization. Microbiology 153 (2007) 3409-3416. [PMID: 17906140]
Accepted name: geranylfarnesyl diphosphate synthase
Reaction: geranylgeranyl diphosphate + isopentenyl diphosphate = (2E,6E,10E,14E)-geranylfarnesyl diphosphate + diphosphate
For diagram of reaction, click here
Other name(s): FGPP synthase; (all-E) geranylfarnesyl diphosphate synthase; GFPS; Fgs
Systematic name: geranylgeranyl-diphosphate:isopentenyl-diphosphate transtransferase (adding 1 isopentenyl unit)
Comments: The enzyme from Methanosarcina mazei is involved in biosynthesis of the polyprenyl side-chain of methanophenazine, an electron carrier utilized for methanogenesis. It prefers geranylgeranyl diphosphate and farnesyl diphosphate as allylic substrate [1]. The enzyme from Aeropyrum pernix prefers farnesyl diphosphate as allylic substrate. The enzyme is involved in the biosynthesis of C25-C25 membrane lipids [2].
Links to other databases: BRENDA, EXPASY, KEGG, PDB, Metacyc, PDB, CAS registry number:
References:
1. Ogawa, T., Yoshimura, T. and Hemmi, H. Geranylfarnesyl diphosphate synthase from Methanosarcina mazei: Different role, different evolution. Biochem. Biophys. Res. Commun. 393 (2010) 16-20. [PMID: 20097171]
2. Tachibana, A., Yano, Y., Otani, S., Nomura, N., Sako, Y. and Taniguchi, M. Novel prenyltransferase gene encoding farnesylgeranyl diphosphate synthase from a hyperthermophilic archaeon, Aeropyrum pernix. Molecular evolution with alteration in product specificity. Eur. J. Biochem. 267 (2000) 321-328. [PMID: 10632701]
3. Tachibana, A. A novel prenyltransferase, farnesylgeranyl diphosphate synthase, from the haloalkaliphilic archaeon, Natronobacterium pharaonis. FEBS Lett. 341 (1994) 291-294. [PMID: 8137956]
4. Lee, P.C., Mijts, B.N., Petri, R., Watts, K.T. and Schmidt-Dannert, C. Alteration of product specificity of Aeropyrum pernix farnesylgeranyl diphosphate synthase (Fgs) by directed evolution. Protein Eng Des Sel 17 (2004) 771-777. [PMID: 15548566]
Accepted name: hexaprenyl diphosphate synthase [geranylgeranyl-diphosphate specific]
Reaction: geranylgeranyl diphosphate + 2 isopentenyl diphosphate = 2 diphosphate + all-trans-hexaprenyl diphosphate
For diagram of reaction, click here
Other name(s): HexPS(ambiguous); (all-E) hexaprenyl diphosphate synthase; (all-trans) hexaprenyl diphosphate synthase; hexaprenyl pyrophosphate synthase (ambiguous); HexPPs (ambiguous); hexaprenyl diphosphate synthase (ambiguous)
Systematic name: geranylgeranyl-diphosphate:isopentenyl-diphosphate transferase (adding 2 isopentenyl units)
Comments: The enzyme prefers geranylgeranyl diphosphate to farnesyl diphosphate as an allylic substrate and does not show activity for geranyl diphosphate and dimethylallyl diphosphate. Requires Mg2+ [1].
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number:
References:
1. Hemmi, H., Ikejiri, S., Yamashita, S. and Nishino, T. Novel medium-chain prenyl diphosphate synthase from the thermoacidophilic archaeon Sulfolobus solfataricus. J. Bacteriol. 184 (2002) 615-620. [PMID: 11790729]
2. Hemmi, H., Noike, M., Nakayama, T. and Nishino, T. Change of product specificity of hexaprenyl diphosphate synthase from Sulfolobus solfataricus by introducing mimetic mutations. Biochem. Biophys. Res. Commun. 297 (2002) 1096-1101. [PMID: 12372398]
3. Sun, H.Y., Ko, T.P., Kuo, C.J., Guo, R.T., Chou, C.C., Liang, P.H. and Wang, A.H. Homodimeric hexaprenyl pyrophosphate synthase from the thermoacidophilic crenarchaeon Sulfolobus solfataricus displays asymmetric subunit structures. J. Bacteriol. 187 (2005) 8137-8148. [PMID: 16291686]
Accepted name: hexaprenyl diphosphate synthase [(2E,6E)-farnesyl-diphosphate specific]
Reaction: (2E,6E)-farnesyl diphosphate + 3 isopentenyl diphosphate = 3 diphosphate + all-trans-hexaprenyl diphosphate
For diagram of reaction, click here
Other name(s): HexPS (ambiguous); hexaprenyl pyrophosphate synthetase (ambiguous); hexaprenyl diphosphate synthase (ambiguous)
Systematic name: (2E,6E)-farnesyl-diphosphate:isopentenyl-diphosphate farnesyltranstransferase (adding 3 isopentenyl units)
Comments: The enzyme prefers farnesyl diphosphate to geranylgeranyl diphosphate as an allylic substrate and does not show activity for geranyl diphosphate and dimethylallyl diphosphate [1].
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number:
References:
1. Fujii, H., Koyama, T. and Ogura, K. Hexaprenyl pyrophosphate synthetase from Micrococcus luteus B-P 26. Separation of two essential components. J. Biol. Chem. 257 (1982) 14610-14612. [PMID: 7174655]
2. Shimizu, N., Koyama, T. and Ogura, K. Molecular cloning, expression, and characterization of the genes encoding the two essential protein components of Micrococcus luteus B-P 26 hexaprenyl diphosphate synthase. J. Bacteriol. 180 (1998) 1578-1581. [PMID: 9515931]
3. Nagaki, M., Kimura, K., Kimura, H., Maki, Y., Goto, E., Nishino, T. and Koyama, T. Artificial substrates of medium-chain elongating enzymes, hexaprenyl- and heptaprenyl diphosphate synthases. Bioorg. Med. Chem. Lett. 11 (2001) 2157-2159. [PMID: 11514159]
Accepted name: all-trans-nonaprenyl-diphosphate synthase [geranyl-diphosphate specific]
Reaction: geranyl diphosphate + 7 isopentenyl diphosphate = 7 diphosphate + all-trans-nonaprenyl diphosphate
For diagram of reaction, click here
Glossary: solanesyl diphosphate = all-trans-nonaprenyl diphosphate
Other name(s): nonaprenyl diphosphate synthase (ambiguous); solanesyl diphosphate synthase (ambiguous); SolPP synthase (ambiguous); SPP-synthase (ambiguous); SPP synthase (ambiguous); solanesyl-diphosphate synthase (ambiguous); OsSPS2
Systematic name: geranyl-diphosphate:isopentenyl-diphosphate transtransferase (adding 7 isopentenyl units)
Comments: (2E,6E)-Farnesyl diphosphate and geranylgeranyl diphosphate are less effective as substrates than geranyl diphosphate. The enzyme is involved in the synthesis of the side chain of menaquinone-9 [1]. In Oryza sativa the enzyme SPS2 is involved in providing solanesyl diphosphate for plastoquinone-9 formation [3].
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:
References:
1. Sagami, H., Ogura, K. and Seto, S. Solanesyl pyrophosphate synthetase from Micrococcus lysodeikticus. Biochemistry 16 (1977) 4616-4622. [PMID: 911777]
2. Fujii, H., Sagami, H., Koyama, T., Ogura, K., Seto, S., Baba, T. and Allen, C.M. Variable product specificity of solanesyl pyrophosphate synthetase. Biochem. Biophys. Res. Commun. 96 (1980) 1648-1653. [PMID: 7447947]
3. Ohara, K., Sasaki, K. and Yazaki, K. Two solanesyl diphosphate synthases with different subcellular localizations and their respective physiological roles in Oryza sativa. J. Exp. Bot. (2010) . [PMID: 20421194]
4. Ohnuma, S., Koyama, T. and Ogura, K. Purification of solanesyl-diphosphate synthase from Micrococcus luteus. A new class of prenyltransferase. J. Biol. Chem. 266 (1991) 23706-23713. [PMID: 1748647]
5. Gotoh, T., Koyama, T. and Ogura, K. Farnesyl diphosphate synthase and solanesyl diphosphate synthase reactions of diphosphate-modified allylic analogs: the significance of the diphosphate linkage involved in the allylic substrates for prenyltransferase. J. Biochem. 112 (1992) 20-27. [PMID: 1429508]
6. Teclebrhan, H., Olsson, J., Swiezewska, E. and Dallner, G. Biosynthesis of the side chain of ubiquinone:trans-prenyltransferase in rat liver microsomes. J. Biol. Chem. 268 (1993) 23081-23086. [PMID: 8226825]
Accepted name: all-trans-nonaprenyl diphosphate synthase [geranylgeranyl-diphosphate specific]
Reaction: geranylgeranyl diphosphate + 5 isopentenyl diphosphate = 5 diphosphate + all-trans-nonaprenyl diphosphate
For diagram of reaction, click here
Glossary: solanesyl diphosphate = all-trans-nonaprenyll diphosphate
Other name(s): nonaprenyl diphosphate synthase (ambiguous); solanesyl diphosphate synthase (ambiguous); At-SPS2; At-SPS1; SPS1; SPS2
Systematic name: geranylgeranyl-diphosphate:isopentenyl-diphosphate transtransferase (adding 5 isopentenyl units)
Comments: Geranylgeranyl diphosphate is preferred over farnesyl diphosphate as allylic substrate [1]. The plant Arabidopsis thaliana has two different enzymes that catalyse this reaction. SPS1 contributes to the biosynthesis of the ubiquinone side-chain while SPS2 supplies the precursor of the plastoquinone side-chains [2].
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number:
References:
1. Hirooka, K., Bamba, T., Fukusaki, E. and Kobayashi, A. Cloning and kinetic characterization of Arabidopsis thaliana solanesyl diphosphate synthase. Biochem. J. 370 (2003) 679-686. [PMID: 12437513]
2. Hirooka, K., Izumi, Y., An, C.I., Nakazawa, Y., Fukusaki, E. and Kobayashi, A. Functional analysis of two solanesyl diphosphate synthases from Arabidopsis thaliana. Biosci. Biotechnol. Biochem. 69 (2005) 592-601. [PMID: 15784989]
3. Jun, L., Saiki, R., Tatsumi, K., Nakagawa, T. and Kawamukai, M. Identification and subcellular localization of two solanesyl diphosphate synthases from Arabidopsis thaliana. Plant Cell Physiol. 45 (2004) 1882-1888. [PMID: 15653808]
Accepted name: trans,polycis-decaprenyl diphosphate synthase
Reaction: (2Z,6E)-farnesyl diphosphate + 7 isopentenyl diphosphate = 7 diphosphate + trans,octacis-decaprenyl diphosphate
For diagram of reaction, click here
Glossary: (2Z,6Z,10Z,14Z,18Z,22Z,26Z,30Z,34E)-decaprenyl diphosphate = trans,polycis-decaprenyl diphosphate
Other name(s): Rv2361c; (2Z,6Z,10Z,14Z,18Z,22Z,26Z,30Z,34E)-decaprenyl diphosphate synthase
Systematic name: (2Z,6E)-farnesyl-diphosphate:isopentenyl-diphosphate farnesylcistransferase (adding 7 isopentenyl units)
Comments: The enzyme is involved in the biosynthesis of decaprenyl phosphate, which plays a central role in the biosynthesis of essential mycobacterial cell wall components, such as the mycolyl-arabinogalactan-peptidoglycan complex and lipoarabinomannan [2].
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number:
References:
1. Kaur, D., Brennan, P.J. and Crick, D.C. Decaprenyl diphosphate synthesis in Mycobacterium tuberculosis. J. Bacteriol. 186 (2004) 7564-7570. [PMID: 15516568]
2. Wang, W., Dong, C., McNeil, M., Kaur, D., Mahapatra, S., Crick, D.C. and Naismith, J.H. The structural basis of chain length control in Rv1086. J. Mol. Biol. 381 (2008) 129-140. [PMID: 18597781]
3. Crick, D.C., Schulbach, M.C., Zink, E.E., Macchia, M., Barontini, S., Besra, G.S. and Brennan, P.J. Polyprenyl phosphate biosynthesis in Mycobacterium tuberculosis and Mycobacterium smegmatis. J. Bacteriol. 182 (2000) 5771-5778. [PMID: 11004176]
Accepted name: ditrans,polycis-polyprenyl diphosphate synthase [(2E,6E)-farnesyl diphosphate specific]
Reaction: (2E,6E)-farnesyl diphosphate + n isopentenyl diphosphate = n diphosphate + ditrans,polycis-polyprenyl diphosphate (n = 10-55)
For diagram of reaction, click here
Other name(s): RER2; Rer2p; Rer2p Z-prenyltransferase; Srt1p; Srt2p Z-prenyltransferase; ACPT; dehydrodolichyl diphosphate synthase 1
Systematic name: (2E,6E)-farnesyl-diphosphate:isopentenyl-diphosphate cistransferase (adding 10-55 isopentenyl units)
Comments: The enzyme is involved in biosynthesis of dolichol (a long-chain polyprenol with a saturated α-isoprene unit, which serves as a glycosyl carrier in protein glycosylation [1]. The yeast Saccharomyces cerevisiae has two different enzymes that catalyse this reaction. Rer2p synthesizes a well-defined family of polyprenols of 13-18 isoprene residues with dominating C80 (16 isoprene residues) extending to C120, while Srt1p synthesizes mainly polyprenol with 22 isoprene subunits. Largest Srt1p products reach C290 [2]. The enzyme from Arabidopsis thaliana catalyses the formation of polyprenyl diphosphates with predominant carbon number C120 [4].
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number:
References:
1. Sato, M., Fujisaki, S., Sato, K., Nishimura, Y. and Nakano, A. Yeast Saccharomyces cerevisiae has two cis-prenyltransferases with different properties and localizations. Implication for their distinct physiological roles in dolichol synthesis. Genes Cells 6 (2001) 495-506. [PMID: 11442630]
2. Poznanski, J. and Szkopinska, A. Precise bacterial polyprenol length control fails in Saccharomyces cerevisiae. Biopolymers 86 (2007) 155-164. [PMID: 17345630]
3. Sato, M., Sato, K., Nishikawa, S., Hirata, A., Kato, J. and Nakano, A. The yeast RER2 gene, identified by endoplasmic reticulum protein localization mutations, encodes cis-prenyltransferase, a key enzyme in dolichol synthesis. Mol. Cell Biol. 19 (1999) 471-483. [PMID: 9858571]
4. Oh, S.K., Han, K.H., Ryu, S.B. and Kang, H. Molecular cloning, expression, and functional analysis of a cis-prenyltransferase from Arabidopsis thaliana. Implications in rubber biosynthesis. J. Biol. Chem. 275 (2000) 18482-18488. [PMID: 10764783]
5. Cunillera, N., Arro, M., Fores, O., Manzano, D. and Ferrer, A. Characterization of dehydrodolichyl diphosphate synthase of Arabidopsis thaliana, a key enzyme in dolichol biosynthesis. FEBS Lett. 477 (2000) 170-174. [PMID: 10908715]
Accepted name: trans,polycis-polyprenyl diphosphate synthase [(2Z,6E)-farnesyl diphosphate specific]
Reaction: (2Z,6E)-farnesyl diphosphate + n isopentenyl diphosphate = n diphosphate + trans,polycis-polyprenyl diphosphate (n = 9-11)
For diagram of reaction, click here
Systematic name: (2Z,6E)-farnesyl-diphosphate:isopentenyl-diphosphate cistransferase (adding 9-11 isopentenyl units)
Comments: Highest activity with (2Z,6E)-farnesyl diphosphate as allylic substrate. Broad product specificity with the major product being dodecaprenyl diphosphate. Synthesizes even C70 prenyl diphosphate as the maximum chain-length product [1].
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number:
References:
1. Ambo, T., Noike, M., Kurokawa, H. and Koyama, T. Cloning and functional analysis of cis-prenyltransferase from Thermobifida fusca. J. Biosci. Bioeng. 107 (2009) 620-622. [PMID: 19447338]
Accepted name: tritrans,polycis-undecaprenyl-diphosphate synthase [geranylgeranyl-diphosphate specific]
Reaction: geranylgeranyl diphosphate + 7 isopentenyl diphosphate = 7 diphosphate + tritrans,heptacis-undecaprenyl diphosphate
Systematic name: geranylgeranyl-diphosphate:isopentenyl-diphosphate cistransferase (adding 7 isopentenyl units)
Comments: This enzyme is involved in the biosynthesis of the glycosyl carrier lipid in some archaebacteria. Unlike EC 2.5.1.31, its counterpart in most bacteria, it prefers geranylgeranyl diphosphate to farnesyl diphosphate as the allylic substrate, resulting in production of a tritrans,polycis variant of undecaprenyl diphosphate [1].
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:
References:
1. Hemmi, H., Yamashita, S., Shimoyama, T., Nakayama, T. and Nishino, T. Cloning, expression, and characterization of cis-polyprenyl diphosphate synthase from the thermoacidophilic archaeon Sulfolobus acidocaldarius. J. Bacteriol. 183 (2001) 401-404. [PMID: 11114943]
Accepted name: all-trans-octaprenyl-diphosphate synthase
Reaction: (2E,6E)-farnesyl diphosphate + 5 isopentenyl diphosphate = 5 diphosphate + all-trans-octaprenyl diphosphate
For diagram of reaction, click here.
Glossary: all-trans-octaprenyl diphosphate = OPP
Other name(s): octaprenyl-diphosphate synthase; octaprenyl pyrophosphate synthetase; polyprenylpyrophosphate synthetase; terpenoidallyltransferase; terpenyl pyrophosphate synthetase; trans-heptaprenyltranstransferase; trans-prenyltransferase
Systematic name: (2E,6E)-farnesyl-diphosphate:isopentenyl-diphosphate farnesyltranstransferase (adding 5 isopentenyl units)
Comments: This enzyme catalyses the condensation reactions resulting in the formation of all-trans-octaprenyl diphosphate, the isoprenoid side chain of ubiquinone-8 and menaquinone-8. The enzyme adds five isopentenyl diphosphate molecules sequentially to farnesyl diphosphate with trans stereochemistry
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number:
References:
1. Fujisaki, S., Nishino, T. and Katsuki, H. Isoprenoid synthesis in Escherichia coli. Separation and partial purification of four enzymes involved in the synthesis. J. Biochem. 99 (1986) 1327-1337. [PMID: 3519603]
2. Asai, K., Fujisaki, S., Nishimura, Y., Nishino, T., Okada, K., Nakagawa, T., Kawamukai, M. and Matsuda, H. The identification of Escherichia coli ispB (cel) gene encoding the octaprenyl diphosphate synthase. Biochem. Biophys. Res. Commun. 202 (1994) 340-345. [PMID: 8037730]
Accepted name: all-trans-decaprenyl-diphosphate synthase
Reaction: (2E,6E)-farnesyl diphosphate + 7 isopentenyl diphosphate = 7 diphosphate + all-trans-decaprenyl diphosphate
For diagram of reaction, click here.
Other name(s): decaprenyl-diphosphate synthase; decaprenyl pyrophosphate synthetase; polyprenylpyrophosphate synthetase; terpenoidallyltransferase; terpenyl pyrophosphate synthetase; trans-prenyltransferase
Systematic name: (2E,6E)-farnesyl-diphosphate:isopentenyl-diphosphate farnesyltranstransferase (adding 7 isopentenyl units)
Comments: This enzyme catalyses the condensation reactions resulting in the formation of all-trans-decaprenyl diphosphate, the isoprenoid side chain of ubiquinone-10 and menaquinone-10. The enzyme adds seven isopentenyl diphosphate molecules sequentially to farnesyl diphosphate with trans stereochemistry.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:
References:
1. Saiki, R., Nagata, A., Kainou, T., Matsuda, H. and Kawamukai, M. Characterization of solanesyl and decaprenyl diphosphate synthases in mice and humans. FEBS J. 272 (2005) 5606-5622. [PMID: 16262699]
Accepted name: (2Z,6Z)-farnesyl diphosphate synthase
Reaction: dimethylallyl diphosphate + 2 isopentenyl diphosphate = 2 diphosphate + (2Z,6Z)-farnesyl diphosphate
Other name(s): cis,cis-farnesyl diphosphate synthase; Z,Z-FPP synthase; zFPS; Z,Z-farnesyl pyrophosphate synthase
Systematic name: dimethylallyl-diphosphate:isopentenyl-diphosphate cistransferase (adding 2 isopentenyl units)
Comments: This enzyme, originally characterized from wild tomato, specifically forms (2Z,6Z)-farnesyl diphosphate via neryl diphosphate and isopentenyl diphosphate. In wild tomato it is involved in the biosynthesis of several sesquiterpenes. See also EC 2.5.1.68 [(2Z,6E)-farnesyl diphosphate synthase] and EC 2.5.1.10 [(2E,6E)-farnesyl diphosphate synthase].
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number:
References:
1. Sallaud, C., Rontein, D., Onillon, S., Jabes, F., Duffe, P., Giacalone, C., Thoraval, S., Escoffier, C., Herbette, G., Leonhardt, N., Causse, M. and Tissier, A. A novel pathway for sesquiterpene biosynthesis from Z,Z-farnesyl pyrophosphate in the wild tomato Solanum habrochaites. Plant Cell 21 (2009) 301-317. [PMID: 19155349]
Accepted name: 4-hydroxybenzoate geranyltransferase
Reaction: geranyl diphosphate + 4-hydroxybenzoate = 3-geranyl-4-hydroxybenzoate + diphosphate
Other name(s): PGT1; PGT2; 4HB geranyltransferase; 4HB:geranyltransferase; p-hydroxybenzoate geranyltransferase; PHB geranyltransferase; geranyl diphosphate:4-hydroxybenzoate geranyltransferase; p-hydroxybenzoate geranyltransferase
Systematic name: geranyl-diphosphate:4-hydroxybenzoate 3-geranyltransferase
Comments: The enzyme is involved in shikonin biosynthesis. It has a strict substrate specificity for geranyl diphosphate and an absolute requirement for Mg2+ [2].
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:
References:
1. Ohara, K., Muroya, A., Fukushima, N. and Yazaki, K. Functional characterization of LePGT1, a membrane-bound prenyltransferase involved in the geranylation of p-hydroxybenzoic acid. Biochem. J. 421 (2009) 231-241. [PMID: 19392660]
2. Muhlenweg, A., Melzer, M., Li, S.M. and Heide, L. 4-Hydroxybenzoate 3-geranyltransferase from Lithospermum erythrorhizon: purification of a plant membrane-bound prenyltransferase. Planta 205 (1998) 407-413. [PMID: 9640665]
3. Yazaki, K., Kunihisa, M., Fujisaki, T. and Sato, F. Geranyl diphosphate:4-hydroxybenzoate geranyltransferase from Lithospermum erythrorhizon. Cloning and characterization of a key enzyme in shikonin biosynthesis. J. Biol. Chem. 277 (2002) 6240-6246. [PMID: 11744717]
Accepted name: adenosyl-chloride synthase
Reaction: S-adenosyl-L-methionine + chloride = 5-deoxy-5-chloroadenosine + L-methionine
Glossary: 5-deoxy-5-chloroadenosine = 5'-chloro-5'-deoxyadenosine
Other name(s): chlorinase; 5'-chloro-5'-deoxyadenosine synthase
Systematic name: S-adenosyl-L-methionine:chloride adenosyltransferase
Comments: This enzyme, isolated from the marine bacterium Salinispora tropica, catalyses an early step in the pathway leading to biosynthesis of the proteosome inhibitor salinosporamide A. The enzyme is very similar to EC 2.5.1.63, adenosyl-fluoride synthase, but does not accept fluoride.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number:
References:
1. Eustaquio, A.S., Pojer, F., Noel, J.P. and Moore, B.S. Discovery and characterization of a marine bacterial SAM-dependent chlorinase. Nat. Chem. Biol. 4 (2008) 69-74. [PMID: 18059261]
Accepted name: xanthan ketal pyruvate transferase
Reaction: phosphoenolpyruvate + D-Man-β-(1→4)-D-GlcA-β-(1→2)-D-Man-α-(1→3)-D-Glc-β-(1→4)-D-Glc-α-1-diphospho-ditrans,octacis-undecaprenol = 4,6-CH3(COO–)C-D-Man-β-(1→4)-D-GlcA-β-(1→2)-D-Man-α-(1→3)-D-Glc-β-(1→4)-D-Glc-α-1-diphospho-ditrans,octacis-undecaprenol + phosphate
For diagram of reaction click here
Other name(s): KPT
Systematic name: phosphoenolpyruvate:D-Man-β-(1→4)-GlcA-β-(1→2)-D-Man-α-(1→3)-D-Glc-β-(1→4)-D-Glc-α-1-diphospho-ditrans,octacis-undecaprenol 4,6-O-(1-carboxyethan-1,1-diyl)transferase
Comments: Involved in the biosynthesis of the polysaccharide xanthan. 30-40% of the terminal mannose residues of xanthan have a 4,6-O-(1-carboxyethan-1,1-diyl) ketal group. It also acts on the 6-O-acetyl derivative of the inner mannose unit.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:
References:
1. Marzocca, M.P., Harding, N.E., Petroni, E.A., Cleary, J.M. and Ielpi, L. Location and cloning of the ketal pyruvate transferase gene of Xanthomonas campestris. J. Bacteriol. 173 (1991) 7519-7524. [PMID: 1657892]
Accepted name: 4,4'-diapophytoene synthase
Reaction: 2 (2E,6E)-farnesyl diphosphate = 15-cis-4,4'-diapophytoene + 2 diphosphate (overall reaction)
(1a) 2 (2E,6E)-farnesyl diphosphate = diphosphate + presqualene diphosphate
(1b) presqualene diphosphate = 15-cis-4,4'-diapophytoene + diphosphate
For diagram of reaction, click here
Other name(s): dehydrosqualene synthase; DAP synthase; C30 carotene synthase; CrtM
Systematic name: farnesyl-diphosphate:farnesyl-diphosphate farnesyltransferase (15-cis-4,4'-diapophytoene forming)
Comments: Requires Mn2+. Typical of Staphylococcus aureus and some other bacteria such as Heliobacillus sp.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number:
References:
1. Umeno, D., Tobias, A.V. and Arnold, F.H. Evolution of the C30 carotenoid synthase CrtM for function in a C40 pathway. J. Bacteriol. 184 (2002) 6690-6699. [PMID: 12426357]
2. Pelz, A., Wieland, K.P., Putzbach, K., Hentschel, P., Albert, K. and Gotz, F. Structure and biosynthesis of staphyloxanthin from Staphylococcus aureus. J. Biol. Chem. 280 (2005) 32493-32498. [PMID: 16020541]
3. Ku, B., Jeong, J.C., Mijts, B.N., Schmidt-Dannert, C. and Dordick, J.S. Preparation, characterization, and optimization of an in vitro C30 carotenoid pathway. Appl. Environ. Microbiol. 71 (2005) 6578-6583. [PMID: 16269684]
4. Liu, C.I., Liu, G.Y., Song, Y., Yin, F., Hensler, M.E., Jeng, W.Y., Nizet, V., Wang, A.H. and Oldfield, E. A cholesterol biosynthesis inhibitor blocks Staphylococcus aureus virulence. Science 319 (2008) 1391-1394. [PMID: 18276850]
Accepted name: pseudaminic acid synthase
Reaction: phosphoenolpyruvate + 2,4-bis(acetylamino)-2,4,6-trideoxy-β-L-altropyranose + H2O = 5,7-bis(acetylamino)-3,5,7,9-tetradeoxy-L-glycero-α-L-manno-2-nonulopyranosonic acid + phosphate
Glossary: pseudaminic acid = 5,7-bis(acetylamino)-3,5,7,9-tetradeoxy-L-glycero-α-L-manno-2-nonulopyranosonic acid
Other name(s): PseI; NeuB3
Systematic name: phosphoenolpyruvate:2,4-bis(acetylamino)-2,4,6-trideoxy-β-L-altropyranose transferase (phosphate-hydrolysing, 2,7-acetylamino-transfering, 2-carboxy-2-oxoethyl-forming)
Comments: The enzyme requires a divalent metal ion, the highest activity values are observed in the presence of Mn2+ and Co2+ (10 mM).
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:
References:
1. Chou, W.K., Dick, S., Wakarchuk, W.W. and Tanner, M.E. Identification and characterization of NeuB3 from Campylobacter jejuni as a pseudaminic acid synthase. J. Biol. Chem. 280 (2005) 35922-35928. [PMID: 16120604]
Accepted name: Rhizobium leguminosarum exopolysaccharide glucosyl ketal-pyruvate-transferase
Reaction: phosphoenolpyruvate + [β-D-GlcA-(1→4)-2-O-Ac-β-D-GlcA-(1→4)-β-D-Glc-(1→4)-[3-O-(CH3CH(OH)CH2C(O))-4,6-CH3(COO–)C-β-D-Gal-(1→4)-β-D-Glc-(1→4)-β-D-Glc-(1→4)-β-D-Glc-(1→6)]-2(or 3)-O-Ac-α-D-Glc-(1→6)]n = [β-D-GlcA-(1→4)-2-O-Ac-β-D-GlcA-(1→4)-β-D-Glc-(1→4)-[3-O-(CH3CH(OH)CH2C(O))-4,6-CH3(COO–)C-β-D-Gal-(1→3)-4,6-CH3(COO–)C-β-D-Glc-(1→4)-β-D-Glc-(1→4)-β-D-Glc-(1→6)]-2(or 3)-O-Ac-α-D-Glc-(1→6)]n + phosphate
Other name(s): PssM; phosphoenolpyruvate:[D-GlcA-β-(1→4)-2-O-Ac-D-GlcA-β-(1→4)-D-Glc-β-(1→4)-[3-O-CH3-CH2CH(OH)C(O)-D-Gal-β-(1→4)-D-Glc-β-(1→4)-D-Glc-β-(1→4)-D-Glc-β-(1→6)]-2(or 3)-O-Ac-D-Glc-α-(1→6)]n 4,6-O-(1-carboxyethan-1,1-diyl)transferase
Systematic name: phosphoenolpyruvate:[β-D-GlcA-(1→4)-2-O-Ac-β-D-GlcA-(1→4)-β-D-Glc-(1→4)-[3-O-CH3-CH2CH(OH)C(O)-4,6-CH3(COO–)C-β-D-Gal-(1→4)-β-D-Glc-(1→4)-β-D-Glc-(1→4)-β-D-Glc-(1→6)]-2(or 3)-O-Ac-α-D-Glc-(1→6)]n 4,6-O-(1-carboxyethan-1,1-diyl)transferase
Comments: The enzyme is responsible for pyruvylation of the subterminal glucose in the acidic octasaccharide repeating unit of the exopolysaccharide of Rhizobium leguminosarum (bv. viciae strain VF39) which is necessary to establish nitrogen-fixing symbiosis with Pisum sativum, Vicia faba, and Vicia sativa.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number:
References:
1. Ivashina, T.V., Fedorova, E.E., Ashina, N.P., Kalinchuk, N.A., Druzhinina, T.N., Shashkov, A.S., Shibaev, V.N. and Ksenzenko, V.N. Mutation in the pssM gene encoding ketal pyruvate transferase leads to disruption of Rhizobium leguminosarum bv. viciae—Pisum sativum symbiosis. J. Appl. Microbiol. 109 (2010) 731-742. [PMID: 20233262]
[EC 2.5.1.99 Deleted entry: all-trans-phytoene synthase. The activity was an artifact caused by photoisomerization of the product of EC 2.5.1.32, 15-cis-phytoene synthase. (EC 2.5.1.99 created 2012, deleted 2018)]
Accepted name: fumigaclavine A dimethylallyltransferase
Reaction: fumigaclavine A + dimethylallyl diphosphate = fumigaclavine C + diphosphate
For diagram of reaction click here.
Glossary: fumigaclavine A = 6,8β-dimethylergolin-9β-yl acetate
fumigaclavine C = 2-(2-methylbut-3-en-2-yl)-6,8β-dimethylergolin-9β-yl acetate
Other name(s): FgaPT1
Systematic name: dimethylallyl-diphosphate:fumigaclavine A dimethylallyltransferase
Comments: Fumigaclavine C is an ergot alkaloid produced by some fungi of the Trichocomaceae family. Activity does not require any metal ions.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:
References:
1. Unsöld, I.A. and Li, S.M. Reverse prenyltransferase in the biosynthesis of fumigaclavine C in Aspergillus fumigatus: gene expression, purification, and characterization of fumigaclavine C synthase FGAPT1. ChemBioChem. 7 (2006) 158-164. [PMID: 16397874]