CATH Classification

Domain Context

CATH Clusters

Superfamily Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain
Functional Family Carminomycin 4-O-methyltransferase DnrK

Enzyme Information

2.1.1.303
2,7-dihydroxy-5-methyl-1-naphthoate 7-O-methyltransferase.
based on mapping to UniProt Q84HC8
S-adenosyl-L-methionine + 2,7-dihydroxy-5-methyl-1-naphthoate = S-adenosyl-L-homocysteine + 2-hydroxy-7-methoxy-5-methyl-1-naphthoate.
-!- 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 catalyzes 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 catalyzes their regiospecific O-methylation.

UniProtKB Entries (1)

Q84HC8
NCSB1_STRCZ
Streptomyces carzinostaticus
2,7-dihydroxy-5-methyl-1-naphthoate 7-O-methyltransferase

PDB Structure

PDB 3I58
External Links
Method X-RAY DIFFRACTION
Organism
Primary Citation
Molecular basis of substrate promiscuity for the SAM-dependent O-methyltransferase NcsB1, involved in the biosynthesis of the enediyne antitumor antibiotic neocarzinostatin.
Cooke, H.A., Guenther, E.L., Luo, Y., Shen, B., Bruner, S.D.
Biochemistry