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6.2.1.46: L-allo-isoleucine-holo-[CmaA peptidyl-carrier protein] ligase

This is an abbreviated version!
For detailed information about L-allo-isoleucine-holo-[CmaA peptidyl-carrier protein] ligase, go to the full flat file.

Reaction

ATP
+
L-allo-isoleucine
+
holo-[CmaA peptidyl-carrier protein]
=
AMP
+
diphosphate
+
L-allo-isoleucyl-[CmaA peptidyl-carrier protein]

Synonyms

CmaA, CmaE, L-allo-isoleucine:holo-[CmaA peptidyl-carrier protein] ligase

ECTree

     6 Ligases
         6.2 Forming carbon-sulfur bonds
             6.2.1 Acid-thiol ligases
                6.2.1.46 L-allo-isoleucine-holo-[CmaA peptidyl-carrier protein] ligase

Reference

Reference on EC 6.2.1.46 - L-allo-isoleucine-holo-[CmaA peptidyl-carrier protein] ligase

Please use the Reference Search for a specific query.
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Strieter, E.R.; Vaillancourt, F.H.; Walsh, C.T.
CmaE: a transferase shuttling aminoacyl groups between carrier protein domains in the coronamic acid biosynthetic pathway
Biochemistry
46
7549-7557
2007
Pseudomonas syringae
Manually annotated by BRENDA team
Couch, R.; O'Connor, S.E.; Seidle, H.; Walsh, C.T.; Parry, R.
Characterization of CmaA, an adenylation-thiolation didomain enzyme involved in the biosynthesis of coronatine
J. Bacteriol.
186
35-42
2004
Pseudomonas syringae (Q6TNA5), Pseudomonas syringae pv. glycinea PG4180 (Q6TNA5)
Manually annotated by BRENDA team
Vaillancourt, F.H.; Yeh, E.; Vosburg, D.A.; O'Connor, S.E.; Walsh, C.T.
Cryptic chlorination by a non-haem iron enzyme during cyclopropyl amino acid biosynthesis
Nature
436
1191-1194
2005
Pseudomonas syringae
Manually annotated by BRENDA team