CATH Classification
| Level | CATH Code | Description |
|---|---|---|
|
1 | Mainly Alpha |
|
1.10 | Orthogonal Bundle |
|
1.10.10 | Arc Repressor Mutant, subunit A |
|
1.10.10.10 | Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain |
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 | 3I53 |
| 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
|
