ID: | 2.1.1.303 |
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Description: | 2,7-dihydroxy-5-methyl-1-naphthoate 7-O-methyltransferase. |
Alternative Name: |
Neocarzinostatin O-methyltransferase. |
Cath: | 1.10.10.10; 1.10.287.1350; 3.40.50.150; |
Click one PDB to see exact 3D structure provided by NGL.
Note: Use your mouse to drag, rotate, and zoom in and out of the structure. Mouse-over to identify atoms and bonds. Mouse controls documentation.UniProtKB Enzyme Link: | UniProtKB 2.1.1.303 |
BRENDA Enzyme Link: | BRENDA 2.1.1.303 |
KEGG Enzyme Link: | KEGG2.1.1.303 |
BioCyc Enzyme Link: | BioCyc 2.1.1.303 |
ExPASy Enzyme Link: | ExPASy2.1.1.303 |
EC2PDB Enzyme Link: | EC2PDB 2.1.1.303 |
ExplorEnz Enzyme Link: | ExplorEnz 2.1.1.303 |
PRIAM enzyme-specific profiles Link: | PRIAM 2.1.1.303 |
IntEnz Enzyme Link: | IntEnz 2.1.1.303 |
MEDLINE Enzyme Link: | MEDLINE 2.1.1.303 |
MSA: | |
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Phylogenetic Tree: | |
Uniprot: | |
M-CSA: |
RHEA:41536 | 2,7-dihydroxy-5-methyl-1-naphthoate + S-adenosyl-L-methionine = 2-hydroxy-7-methoxy-5-methyl-1-naphthoate + H(+) + S-adenosyl-L-homocysteine |
RULE(radius=1) | [*:1]-[OH;+0:2].[*:3]-[S+;H0:4](-[*:5])-[CH3;+0:6]>>[*:1]-[O;H0;+0:2]-[CH3;+0:6].[*:3]-[S;H0;+0:4]-[*:5] |
Reaction | ![]() |
Core-to-Core | No scaffolds atoms were exchanged as a result of the reaction |
Title | Authors | Date | PubMed ID |
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Molecular basis of substrate promiscuity for the SAM-dependent O-methyltransferase NcsB1, involved in the biosynthesis of the enediyne antitumor antibiotic neocarzinostatin. | Cooke HA, Guenther EL, Luo Y, Shen B, Bruner SD | 2009 Oct 13 | 19702337 |
Regiospecific O-methylation of naphthoic acids catalyzed by NcsB1, an O-methyltransferase involved in the biosynthesis of the enediyne antitumor antibiotic neocarzinostatin. | Luo Y, Lin S, Zhang J, Cooke HA, Bruner SD, Shen B | 2008 May 23 | 18387946 |