CATH Classification
| Level | CATH Code | Description |
|---|---|---|
|
3 | Alpha Beta |
|
3.40 | 3-Layer(aba) Sandwich |
|
3.40.50 | Rossmann fold |
|
3.40.50.150 | Vaccinia Virus protein VP39 |
Domain Context
CATH Clusters
| Superfamily | Vaccinia Virus protein VP39 |
| Functional Family |
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.
Biochemistry
|
