KEGG   ENZYME: 2.1.1.303Help
Entry
EC 2.1.1.303                Enzyme                                 

Name
2,7-dihydroxy-5-methyl-1-naphthoate 7-O-methyltransferase;
NcsB1;
neocarzinostatin O-methyltransferase
Class
Transferases;
Transferring one-carbon groups;
Methyltransferases
BRITE hierarchy
Sysname
S-adenosyl-L-methionine:2,7-dihydroxy-5-methyl-1-naphthoate 7-O-methyltransferase
Reaction(IUBMB)
S-adenosyl-L-methionine + 2,7-dihydroxy-5-methyl-1-naphthoate = S-adenosyl-L-homocysteine + 2-hydroxy-7-methoxy-5-methyl-1-naphthoate [RN:R10963]
Reaction(KEGG)
Substrate
S-adenosyl-L-methionine [CPD:C00019];
2,7-dihydroxy-5-methyl-1-naphthoate [CPD:C20857]
Product
S-adenosyl-L-homocysteine [CPD:C00021];
2-hydroxy-7-methoxy-5-methyl-1-naphthoate [CPD:C20841]
Comment
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.
History
EC 2.1.1.303 created 2014
Pathway
Biosynthesis of enediyne antibiotics
Biosynthesis of antibiotics
Orthology
K20421  
2,7-dihydroxy-5-methyl-1-naphthoate 7-O-methyltransferase
Genes
NCY: 
NNO: 
DTM: 
SMA: 
SSX: 
SHY: 
SHO: 
SALU: 
SALL: 
SCW: 
SXI: 
SPRI: 
SLE: 
sle_66100(sle_66100)
NAL: 
B005_2465(dnrK)
SEN: 
AMD: 
AMN: 
AMM: 
AMZ: 
AOI: 
AJA: 
ALU: 
PDX: 
PSEE: 
PECQ: 
PHH: 
AMI: 
SESP: 
KPHY: 
LED: 
AHM: 
ACTI: 
ACAD: 
STP: 
SAQ: 
MAU: 
MIL: 
AMS: 
SUS: 
 » show all
Taxonomy
Reference
1  [PMID:18387946]
  Authors
Luo Y, Lin S, Zhang J, Cooke HA, Bruner SD, Shen B
  Title
Regiospecific O-methylation of naphthoic acids catalyzed by NcsB1, an O-methyltransferase involved in the biosynthesis of the enediyne antitumor antibiotic neocarzinostatin.
  Journal
J. Biol. Chem. 283 (2008) 14694-702.
  Sequence
Reference
2  [PMID:19702337]
  Authors
Cooke HA, Guenther EL, Luo Y, Shen B, Bruner SD
  Title
Molecular basis of substrate promiscuity for the SAM-dependent O-methyltransferase NcsB1, involved in the biosynthesis of the enediyne antitumor antibiotic neocarzinostatin.
  Journal
Biochemistry. 48 (2009) 9590-8.
  Sequence
Other DBs
ExplorEnz - The Enzyme Database: 
IUBMB Enzyme Nomenclature: 
ExPASy - ENZYME nomenclature database: 
BRENDA, the Enzyme Database: 

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