| 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]
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| 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] |
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| [EC 2.3.2.28 created 2015] |
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