KEGG   ENZYME: 6.2.1.43Help
Entry
EC 6.2.1.43                 Enzyme                                 

Name
2-hydroxy-7-methoxy-5-methyl-1-naphthoate---CoA ligase;
NcsB2
Class
Ligases;
Forming carbon-sulfur bonds;
Acid-thiol ligases
BRITE hierarchy
Sysname
2-hydroxy-7-methoxy-5-methyl-1-naphthoate:CoA ligase
Reaction(IUBMB)
ATP + 2-hydroxy-7-methoxy-5-methyl-1-naphthoate + CoA = AMP + diphosphate + 2-hydroxy-7-methoxy-5-methyl-1-naphthoyl-CoA [RN:R10771]
Reaction(KEGG)
Substrate
ATP [CPD:C00002];
2-hydroxy-7-methoxy-5-methyl-1-naphthoate [CPD:C20841];
CoA [CPD:C00010]
Product
AMP [CPD:C00020];
diphosphate [CPD:C00013];
2-hydroxy-7-methoxy-5-methyl-1-naphthoyl-CoA [CPD:C20842]
Comment
The enzyme from the bacterium Streptomyces carzinostaticus is involved in the attachment of the 2-hydroxy-7-methoxy-5-methyl-1-naphthoate moiety of the antibiotic neocarzinostatin. In vitro the enzyme also catalyses the activation of other 1-naphthoic acid analogues, e.g. 2-hydroxy-5-methyl-1-naphthoate or 2,7-dihydroxy-5-methyl-1-naphthoate.
History
EC 6.2.1.43 created 2014
Pathway
ec01059  Biosynthesis of enediyne antibiotics
ec01130  Biosynthesis of antibiotics
Orthology
K20423  2-hydroxy-7-methoxy-5-methyl-1-naphthoate---CoA ligase
Genes
MTS: MTES_3604
APN: Asphe3_39850
PSUL: AU252_00410
AOI: AORI_6598(dhbE)
AMQ: AMETH_3626(dhbE)
PDX: Psed_5064
SAQ: Sare_4933
ACTN: L083_3190
Taxonomy
Reference
1  [PMID:17539640]
  Authors
Cooke HA, Zhang J, Griffin MA, Nonaka K, Van Lanen SG, Shen B, Bruner SD
  Title
Characterization of NcsB2 as a promiscuous naphthoic acid/coenzyme A ligase integral to the biosynthesis of the enediyne antitumor antibiotic neocarzinostatin.
  Journal
J Am Chem Soc 129:7728-9 (2007)
DOI:10.1021/ja071886a
  Sequence
Other DBs
ExplorEnz - The Enzyme Database: 6.2.1.43
IUBMB Enzyme Nomenclature: 6.2.1.43
ExPASy - ENZYME nomenclature database: 6.2.1.43
BRENDA, the Enzyme Database: 6.2.1.43

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