The Enzyme Database

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EC 5.4.99.5     
Accepted name: chorismate mutase
Reaction: chorismate = prephenate
For diagram of phenylalanine and tyrosine biosynthesis, click here and for mechanism of reaction, click here
Other name(s): hydroxyphenylpyruvate synthase
Systematic name: chorismate pyruvatemutase
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 9068-30-8
References:
1.  Cotton, R.G.H. and Gibson, F. The biosynthesis of phenylalanine and tyrosine; enzymes converting chorismic acid into prephenic acid and their relationships to prephenate dehydratase and prephenate dehydrogenase. Biochim. Biophys. Acta 100 (1965) 76–88. [DOI] [PMID: 14323651]
2.  Lorence, J.H. and Nester, E.W. Multiple molecular forms of chorismate mutase in Bacillus subtillis. Biochemistry 6 (1967) 1541–1543. [PMID: 4962500]
3.  Sprössler, B. and Lingens, F. Chorismat-Mutase aus Claviceps. I. Eigenschaften der Chorismat-Mutase aus verschiedenen Claviceps-Stämmen. Hoppe-Seyler's Z. Physiol. Chem. 351 (1970) 448–458. [PMID: 5443801]
4.  Woodin, T.S. and Nishioka, L. Evidence for three isozymes of chorismate mutase in alfalfa. Biochim. Biophys. Acta 309 (1973) 211–223. [DOI] [PMID: 4708674]
[EC 5.4.99.5 created 1972]
 
 
EC 5.4.99.50     
Accepted name: friedelin synthase
Reaction: (3S)-2,3-epoxy-2,3-dihydrosqualene = friedelin
For diagram of friedelin, glutinol, isomultiflorenol and taraxerol biosynthesis, click here
Systematic name: (3S)-2,3-epoxy-2,3-dihydrosqualene mutase (cyclizing, friedelin-forming)
Comments: The enzyme from Kalanchoe daigremontiana also gives traces of other triterpenoids.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Wang, Z., Yeats, T., Han, H. and Jetter, R. Cloning and characterization of oxidosqualene cyclases from Kalanchoe daigremontiana: enzymes catalyzing up to 10 rearrangement steps yielding friedelin and other triterpenoids. J. Biol. Chem. 285 (2010) 29703–29712. [DOI] [PMID: 20610397]
[EC 5.4.99.50 created 2011]
 
 
EC 5.4.99.51     
Accepted name: baccharis oxide synthase
Reaction: (3S)-2,3-epoxy-2,3-dihydrosqualene = baccharis oxide
For diagram of baccharis oxide, baruol and shionone biosynthesis, click here
Systematic name: (3S)-2,3-epoxy-2,3-dihydrosqualene mutase (cyclizing, baccharis-oxide-forming)
Comments: The enzyme from Stevia rebaudiana also gives traces of other triterpenoids.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Shibuya, M., Sagara, A., Saitoh, A., Kushiro, T. and Ebizuka, Y. Biosynthesis of baccharis oxide, a triterpene with a 3,10-oxide bridge in the A-ring. Org. Lett. 10 (2008) 5071–5074. [DOI] [PMID: 18850716]
[EC 5.4.99.51 created 2011]
 
 
EC 5.4.99.52     
Accepted name: α-seco-amyrin synthase
Reaction: (3S)-2,3-epoxy-2,3-dihydrosqualene = α-seco-amyrin
For diagram of α-amyrin, α-seco-amyrin and germanicol biosynthesis, click here
Glossary: α-seco-amyrin = 8,14-secoursa-7,13-diene-3β-ol
Systematic name: (3S)-2,3-epoxy-2,3-dihydrosqualene mutase (cyclizing, α-seco-amyrin-forming)
Comments: The enzyme from Arabidopsis thaliana is multifunctional and produces about equal amounts of α- and β-seco-amyrin. See EC 5.4.99.54, β-seco-amyrin synthase.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Shibuya, M., Xiang, T., Katsube, Y., Otsuka, M., Zhang, H. and Ebizuka, Y. Origin of structural diversity in natural triterpenes: direct synthesis of seco-triterpene skeletons by oxidosqualene cyclase. J. Am. Chem. Soc. 129 (2007) 1450–1455. [DOI] [PMID: 17263431]
[EC 5.4.99.52 created 2011]
 
 
EC 5.4.99.53     
Accepted name: marneral synthase
Reaction: (3S)-2,3-epoxy-2,3-dihydrosqualene = marneral
For diagram of arabidiol, camellidiol and thalianol biosynthesis, click here
Systematic name: (3S)-2,3-epoxy-2,3-dihydrosqualene mutase (cyclizing, marneral-forming)
Comments: Marneral is a triterpenoid formed by Grob fragmentation of the A ring of 2,3-epoxy-2,3-dihydrosqualene during cyclization.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Xiong, Q., Wilson, W.K. and Matsuda, S.P.T. An Arabidopsis oxidosqualene cyclase catalyzes iridal skeleton formation by Grob fragmentation. Angew. Chem. Int. Ed. Engl. 45 (2006) 1285–1288. [DOI] [PMID: 16425307]
[EC 5.4.99.53 created 2011]
 
 
EC 5.4.99.54     
Accepted name: β-seco-amyrin synthase
Reaction: (3S)-2,3-epoxy-2,3-dihydrosqualene = β-seco-amyrin
For diagram of beta-amyrin and soysapogenol biosynthesis, click here
Glossary: β-seco-amyrin = 8,14-secooleana-7,13-diene-3β-ol
Systematic name: (3S)-2,3-epoxy-2,3-dihydrosqualene mutase (cyclizing, β-seco-amyrin-forming)
Comments: The enzyme from Arabidopsis thaliana is multifunctional and produces about equal amounts of α- and β-seco-amyrin. See EC 5.4.99.52, α-seco-amyrin synthase.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Shibuya, M., Xiang, T., Katsube, Y., Otsuka, M., Zhang, H. and Ebizuka, Y. Origin of structural diversity in natural triterpenes: direct synthesis of seco-triterpene skeletons by oxidosqualene cyclase. J. Am. Chem. Soc. 129 (2007) 1450–1455. [DOI] [PMID: 17263431]
[EC 5.4.99.54 created 2011]
 
 
EC 5.4.99.55     
Accepted name: δ-amyrin synthase
Reaction: (3S)-2,3-epoxy-2,3-dihydrosqualene = δ-amyrin
For diagram of α-amyrin, α-seco-amyrin and germanicol biosynthesis, click here
Other name(s): SlTTS2 (gene name)
Systematic name: (3S)-2,3-epoxy-2,3-dihydrosqualene mutase (cyclizing, δ-amyrin-forming)
Comments: The enzyme from tomato (Solanum lycopersicum) gives 48% δ-amyrin, 18% α-amyrin, 13% β-amyrin and traces of three or four other triterpenoid alcohols [1]. See also EC 5.4.99.40, α-amyrin synthase and EC 5.4.99.39, β-amyrin synthase.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Wang, Z., Guhling, O., Yao, R., Li, F., Yeats, T.H., Rose, J.K. and Jetter, R. Two oxidosqualene cyclases responsible for biosynthesis of tomato fruit cuticular triterpenoids. Plant Physiol. 155 (2011) 540–552. [DOI] [PMID: 21059824]
[EC 5.4.99.55 created 2011]
 
 
EC 5.4.99.56     
Accepted name: tirucalladienol synthase
Reaction: (3S)-2,3-epoxy-2,3-dihydrosqualene = tirucalla-7,24-dien-3β-ol
For diagram of dammarenediol II and tirucalla-7,24-dien-3β-ol biosynthesis, click here
Other name(s): PEN3
Systematic name: (3S)-2,3-epoxy-2,3-dihydrosqualene mutase (cyclizing, tirucalla-7,24-dien-3β-ol-forming)
Comments: The product from Arabidopsis thaliana is 85% tirucalla-7,24-dien-3β-ol with trace amounts of other triterpenoids.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Morlacchi, P., Wilson, W.K., Xiong, Q., Bhaduri, A., Sttivend, D., Kolesnikova, M.D. and Matsuda, S.P. Product profile of PEN3: the last unexamined oxidosqualene cyclase in Arabidopsis thaliana. Org. Lett. 11 (2009) 2627–2630. [DOI] [PMID: 19445469]
[EC 5.4.99.56 created 2011]
 
 
EC 5.4.99.57     
Accepted name: baruol synthase
Reaction: (3S)-2,3-epoxy-2,3-dihydrosqualene = baruol
For diagram of baccharis oxide, baruol and shionone biosynthesis, click here
Other name(s): BARS1
Systematic name: (3S)-2,3-epoxy-2,3-dihydrosqualene mutase (cyclizing, baruol-forming)
Comments: The enzyme from Arabidopsis thaliana also produces traces of 22 other triterpenoids.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Lodeiro, S., Xiong, Q., Wilson, W.K., Kolesnikova, M.D., Onak, C.S. and Matsuda, S.P. An oxidosqualene cyclase makes numerous products by diverse mechanisms: a challenge to prevailing concepts of triterpene biosynthesis. J. Am. Chem. Soc. 129 (2007) 11213–11222. [DOI] [PMID: 17705488]
[EC 5.4.99.57 created 2012]
 
 
EC 5.4.99.58     
Accepted name: methylornithine synthase
Reaction: L-lysine = (3R)-3-methyl-D-ornithine
Glossary: (3R)-3-methyl-D-ornithine = (2R,3R)-2,5-diamino-3-methylpentanoate
Other name(s): PylB
Systematic name: L-lysine carboxy-aminomethylmutase
Comments: The enzyme is a member of the superfamily of S-adenosyl-L-methionine-dependent radical (radical AdoMet) enzymes. Binds a [4Fe-4S] cluster that is coordinated by 3 cysteines and an exchangeable S-adenosyl-L-methionine molecule. The reaction is part of the biosynthesis pathway of pyrrolysine, a naturally occurring amino acid found in some archaeal methyltransferases.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Gaston, M.A., Zhang, L., Green-Church, K.B. and Krzycki, J.A. The complete biosynthesis of the genetically encoded amino acid pyrrolysine from lysine. Nature 471 (2011) 647–650. [DOI] [PMID: 21455182]
2.  Quitterer, F., List, A., Eisenreich, W., Bacher, A. and Groll, M. Crystal structure of methylornithine synthase (PylB): insights into the pyrrolysine biosynthesis. Angew. Chem. Int. Ed. Engl. 51 (2012) 1339–1342. [DOI] [PMID: 22095926]
[EC 5.4.99.58 created 2012]
 
 
EC 5.4.99.59     
Accepted name: dTDP-fucopyranose mutase
Reaction: dTDP-α-D-fucopyranose = dTDP-α-D-fucofuranose
For diagram of dTDP-6-deoxyhexose biosynthesis, click here
Other name(s): Fcf2
Systematic name: dTDP-α-D-fucopyranose furanomutase
Comments: The enzyme is involved in the biosynthesis of the Escherichia coli O52 O antigen.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Wang, Q., Ding, P., Perepelov, A.V., Xu, Y., Wang, Y., Knirel, Y.A., Wang, L. and Feng, L. Characterization of the dTDP-D-fucofuranose biosynthetic pathway in Escherichia coli O52. Mol. Microbiol. 70 (2008) 1358–1367. [DOI] [PMID: 19019146]
[EC 5.4.99.59 created 2013]
 
 


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