EC |
6.2.1.43 |
Accepted name: |
2-hydroxy-7-methoxy-5-methyl-1-naphthoate—CoA ligase |
Reaction: |
ATP + 2-hydroxy-7-methoxy-5-methyl-1-naphthoate + CoA = AMP + diphosphate + 2-hydroxy-7-methoxy-5-methyl-1-naphthoyl-CoA |
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For diagram of neocarzinostatin biosynthesis, click here |
Other name(s): |
NcsB2 |
Systematic name: |
2-hydroxy-7-methoxy-5-methyl-1-naphthoate:CoA ligase |
Comments: |
The enzyme from the bacterium Streptomyces carzinostaticus is involved in the attachment of the 2-hydroxy-7-methoxy-5-methyl-1-naphthoate moiety of the antibiotic neocarzinostatin. In vitro the enzyme also catalyses the activation of other 1-naphthoic acid analogues, e.g. 2-hydroxy-5-methyl-1-naphthoate or 2,7-dihydroxy-5-methyl-1-naphthoate. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc |
References: |
1. |
Cooke, H.A., Zhang, J., Griffin, M.A., Nonaka, K., Van Lanen, S.G., Shen, B. and Bruner, S.D. Characterization of NcsB2 as a promiscuous naphthoic acid/coenzyme A ligase integral to the biosynthesis of the enediyne antitumor antibiotic neocarzinostatin. J. Am. Chem. Soc. 129 (2007) 7728–7729. [DOI] [PMID: 17539640] |
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[EC 6.2.1.43 created 2014] |
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