| EC |
2.1.1.303 |
| Accepted name: |
2,7-dihydroxy-5-methyl-1-naphthoate 7-O-methyltransferase |
| Reaction: |
S-adenosyl-L-methionine + 2,7-dihydroxy-5-methyl-1-naphthoate = S-adenosyl-L-homocysteine + 2-hydroxy-7-methoxy-5-methyl-1-naphthoate
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For diagram of neocarzinostatin biosynthesis, click here |
| Other name(s): |
NcsB1; neocarzinostatin O-methyltransferase |
| Systematic name: |
S-adenosyl-L-methionine:2,7-dihydroxy-5-methyl-1-naphthoate 7-O-methyltransferase |
| Comments: |
The enzyme from the bacterium Streptomyces carzinostaticus is involved in the biosynthesis of 2-hydroxy-7-methoxy-5-methyl-1-naphthoate. This compound is part of the enediyne chromophore of the antitumor antibiotic neocarzinostatin. In vivo the enzyme catalyses the regiospecific methylation at the 7-hydroxy group of its native substrate 2,7-dihydroxy-5-methyl-1-naphthoate. In vitro it also recognizes other dihydroxynaphthoic acids and catalyses their regiospecific O-methylation. |
| Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB |
| References: |
| 1. |
Luo, Y., Lin, S., Zhang, J., Cooke, H.A., Bruner, S.D. and Shen, B. Regiospecific O-methylation of naphthoic acids catalyzed by NcsB1, an O-methyltransferase involved in the biosynthesis of the enediyne antitumor antibiotic neocarzinostatin. J. Biol. Chem. 283 (2008) 14694–14702. [DOI] [PMID: 18387946] |
| 2. |
Cooke, H.A., Guenther, E.L., Luo, Y., Shen, B. and Bruner, S.D. Molecular basis of substrate promiscuity for the SAM-dependent O-methyltransferase NcsB1, involved in the biosynthesis of the enediyne antitumor antibiotic neocarzinostatin. Biochemistry 48 (2009) 9590–9598. [DOI] [PMID: 19702337] |
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| [EC 2.1.1.303 created 2014] |
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