KEGG   ENZYME: 6.2.1.46Help
Entry
EC 6.2.1.46                 Enzyme                                 

Name
L-allo-isoleucine:holo-[CmaA peptidyl-carrier protein] ligase;
CmaA
Class
Ligases;
Forming carbon-sulfur bonds;
Acid-thiol ligases
BRITE hierarchy
Sysname
L-allo-isoleucine:holo-[CmaA peptidyl-carrier protein] ligase (AMP-forming)
Reaction(IUBMB)
ATP + L-allo-isoleucine + holo-[CmaA peptidyl-carrier protein] = AMP + diphosphate + L-allo-isoleucyl-S-[CmaA peptidyl-carrier protein] [RN:R11084]
Reaction(KEGG)
Substrate
ATP [CPD:C00002];
L-allo-isoleucine [CPD:C21096];
holo-[CmaA peptidyl-carrier protein]
Product
AMP [CPD:C00020];
diphosphate [CPD:C00013];
L-allo-isoleucyl-S-[CmaA peptidyl-carrier protein]
Comment
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.
History
EC 6.2.1.46 created 2015
Orthology
K15646  
coronamic acid synthetase CmaA, adenylation and thiolation didomain protein
Genes
PST: 
AZL: 
Taxonomy
Reference
1  [PMID:14679222]
  Authors
Couch R, O'Connor SE, Seidle H, Walsh CT, Parry R
  Title
Characterization of CmaA, an adenylation-thiolation didomain enzyme involved in the biosynthesis of coronatine.
  Journal
J. Bacteriol. 186 (2004) 35-42.
  Sequence
Other DBs
ExplorEnz - The Enzyme Database: 
IUBMB Enzyme Nomenclature: 
ExPASy - ENZYME nomenclature database: 
BRENDA, the Enzyme Database: 

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