The Enzyme Database

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EC 1.14.11.45     
Accepted name: L-isoleucine 4-hydroxylase
Reaction: L-isoleucine + 2-oxoglutarate + O2 = (4S)-4-hydroxy-L-isoleucine + succinate + CO2
Glossary: (4S)-4-hydroxy-L-isoleucine = (2S,3R,4S)-2-amino-4-hydroxy-3-methylpentanoate
Other name(s): ido (gene name)
Systematic name: L-isoleucine,2-oxoglutarate:oxygen oxidoreductase (4-hydroxylating)
Comments: The enzyme, characterized from the bacterium Bacillus thuringiensis, can also catalyse the hydroxylation of L-leucine, L-norvaline, L-norleucine, and L-allo-isoleucine, as well as the sulfoxidation of L-methionine, L-ethionine, S-methyl-L-cysteine, S-ethyl-L-cysteine, and S-allyl-L-cysteine.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Kodera, T., Smirnov, S.V., Samsonova, N.N., Kozlov, Y.I., Koyama, R., Hibi, M., Ogawa, J., Yokozeki, K. and Shimizu, S. A novel L-isoleucine hydroxylating enzyme, L-isoleucine dioxygenase from Bacillus thuringiensis, produces (2S,3R,4S)-4-hydroxyisoleucine. Biochem. Biophys. Res. Commun. 390 (2009) 506–510. [DOI] [PMID: 19850012]
2.  Hibi, M., Kawashima, T., Kodera, T., Smirnov, S.V., Sokolov, P.M., Sugiyama, M., Shimizu, S., Yokozeki, K. and Ogawa, J. Characterization of Bacillus thuringiensis L-isoleucine dioxygenase for production of useful amino acids. Appl. Environ. Microbiol. 77 (2011) 6926–6930. [DOI] [PMID: 21821743]
3.  Hibi, M., Kawashima, T., Yajima, H., Smirnov, S.V., Kodera, T., Sugiyama, M., Shimizu, S., Yokozeki, K., and Ogawa, J. Enzymatic synthesis of chiral amino acid sulfoxides by Fe(II)/α ketoglutarate-dependent dioxygenase. Tetrahedron Asym. 24 (2013) 990–994.
[EC 1.14.11.45 created 2014]
 
 
EC 2.3.2.28     
Accepted name: L-allo-isoleucyltransferase
Reaction: L-allo-isoleucyl-[CmaA peptidyl-carrier protein] + holo-[CmaD peptidyl-carrier protein] = L-allo-isoleucyl-[CmaD peptidyl-carrier protein] + holo-[CmaA peptidyl-carrier protein]
Glossary: L-allo-isoleucine = (2S,3R)-2-amino-3-methylpentanoic acid
Other name(s): CmaE
Systematic name: L-allo-isoleucyl-[CmaA peptidyl-carrier protein]:holo-[CmaD peptidyl-carrier protein] L-allo-isoleucyltransferase
Comments: The enzyme, characterized from the bacterium Pseudomonas syringae, is involved in the biosynthesis of the toxin coronatine.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Vaillancourt, F.H., Yeh, E., Vosburg, D.A., O'Connor, S.E. and Walsh, C.T. Cryptic chlorination by a non-haem iron enzyme during cyclopropyl amino acid biosynthesis. Nature 436 (2005) 1191–1194. [DOI] [PMID: 16121186]
2.  Strieter, E.R., Vaillancourt, F.H. and Walsh, C.T. CmaE: a transferase shuttling aminoacyl groups between carrier protein domains in the coronamic acid biosynthetic pathway. Biochemistry 46 (2007) 7549–7557. [DOI] [PMID: 17530782]
[EC 2.3.2.28 created 2015]
 
 
EC 6.2.1.46     
Accepted name: L-allo-isoleucine—holo-[CmaA peptidyl-carrier protein] ligase
Reaction: ATP + L-allo-isoleucine + holo-[CmaA peptidyl-carrier protein] = AMP + diphosphate + L-allo-isoleucyl-[CmaA peptidyl-carrier protein]
Other name(s): CmaA
Systematic name: L-allo-isoleucine:holo-[CmaA peptidyl-carrier protein] ligase (AMP-forming)
Comments: This two-domain protein from the bacterium Pseudomonas syringae contains an adenylation domain (A domain) and a thiolation domain (T domain). It catalyses the adenylation of L-allo-isoleucine and its attachment to the T domain. The enzyme is involved in the biosynthesis of the toxin coronatine, which mimics the plant hormone jasmonic acid isoleucine. Coronatine promotes opening of the plant stomata allowing bacterial invasion, which is followed by bacterial growth in the apoplast, systemic susceptibility, and disease.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Couch, R., O'Connor, S.E., Seidle, H., Walsh, C.T. and Parry, R. Characterization of CmaA, an adenylation-thiolation didomain enzyme involved in the biosynthesis of coronatine. J. Bacteriol. 186 (2004) 35–42. [DOI] [PMID: 14679222]
[EC 6.2.1.46 created 2015]
 
 


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