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Information on EC 6.2.1.43 - 2-hydroxy-7-methoxy-5-methyl-1-naphthoate-CoA ligase
for references in articles please use BRENDA:EC6.2.1.43
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EC Tree 6 Ligases
6.2 Forming carbon-sulfur bonds
6.2.1 Acid-thiol ligases
6.2.1.43 2-hydroxy-7-methoxy-5-methyl-1-naphthoate-CoA ligase
IUBMB Comments
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.
The expected taxonomic range for this enzyme is: Streptomyces carzinostaticus
Reaction Schemes
showSynonyms
ncsb2, more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
naphthoic acid/coenzyme A ligase
naphthoyl CoA ligase
NcsB2
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
ATP + 2-hydroxy-7-methoxy-5-methyl-1-naphthoate + CoA = AMP + diphosphate + 2-hydroxy-7-methoxy-5-methyl-1-naphthoyl-CoA
-
-
-
-
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PATHWAY SOURCE
PATHWAYS
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SYSTEMATIC NAME
IUBMB Comments
2-hydroxy-7-methoxy-5-methyl-1-naphthoate:CoA ligase
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.
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
ATP + 1-naphthoate + CoA
AMP + diphosphate + 1-naphthoyl-CoA
-
Substrates: kcat/Km is 0.6% compared to the wild-type value
Products: -
Products: -
?
ATP + 2,7-dihydroxy-5-methyl-1-naphthoate + CoA
AMP + diphosphate + 2,7-dihydroxy-5-methyl-1-naphthoyl-CoA
ATP + 2,7-dihydroxy-5-methylnaphthalene-1-carboxylic acid + CoA
AMP + diphosphate + ?
-
Substrates: 47% activity compared to 2-hydroxy-7-methoxy-5-methyl-1-naphthoate
Products: -
Products: -
?
ATP + 2-hydroxy-1-naphthoate + CoA
AMP + diphosphate + 2-hydroxy-1-naphthoyl-CoA
-
Substrates: kcat/Km is 1.3% compared to the wild-type value
Products: -
Products: -
?
ATP + 2-hydroxy-5,7-dimethoxy-1-naphthoate + CoA
AMP + diphosphate + 2-hydroxy-5,7-dimethoxy-1-naphthoyl-CoA
-
Substrates: kcat/Km is 35% compared to the wild-type value
Products: -
Products: -
?
ATP + 2-hydroxy-5,7-dimethoxynaphthalene-1-carboxylic acid + CoA
AMP + diphosphate + ?
-
Substrates: 35% activity compared to 2-hydroxy-7-methoxy-5-methyl-1-naphthoate
Products: -
Products: -
?
ATP + 2-hydroxy-5-methyl-1-naphthoate + CoA
AMP + diphosphate + 2-hydroxy-5-methyl-1-naphthoyl-CoA
ATP + 2-hydroxy-5-methylnaphthalene-1-carboxylic acid + CoA
AMP + diphosphate + ?
-
Substrates: 50% activity compared to 2-hydroxy-7-methoxy-5-methyl-1-naphthoate
Products: -
Products: -
?
ATP + 2-hydroxy-7-methoxy-1-naphthoate + CoA
AMP + diphosphate + 2-hydroxy-7-methoxy-1-naphthoyl-CoA
ATP + 2-hydroxy-7-methoxy-5-methyl-1-naphthoate + CoA
AMP + diphosphate + 2-hydroxy-7-methoxy-5-methyl-1-naphthoyl-CoA
ATP + 2-hydroxy-7-methoxynaphthalene-1-carboxylic acid + CoA
AMP + diphosphate + ?
-
Substrates: 4.8% activity compared to 2-hydroxy-7-methoxy-5-methyl-1-naphthoate
Products: -
Products: -
?
ATP + 2-hydroxynaphthalene-1-carboxylic acid + CoA
AMP + diphosphate + ?
-
Substrates: 1.3% activity compared to 2-hydroxy-7-methoxy-5-methyl-1-naphthoate
Products: -
Products: -
?
ATP + naphthalene-1-carboxylic acid + CoA
AMP + diphosphate + ?
-
Substrates: 0.58% activity compared to 2-hydroxy-7-methoxy-5-methyl-1-naphthoate
Products: -
Products: -
?
ATP + 2,7-dihydroxy-5-methyl-1-naphthoate + CoA
AMP + diphosphate + 2,7-dihydroxy-5-methyl-1-naphthoyl-CoA
-
Substrates: kcat/Km is 47% compared to the wild-type value
Products: -
Products: -
?
ATP + 2,7-dihydroxy-5-methyl-1-naphthoate + CoA
AMP + diphosphate + 2,7-dihydroxy-5-methyl-1-naphthoyl-CoA
-
Substrates: kcat/Km is 47% compared to the wild-type value
Products: -
Products: -
?
ATP + 2-hydroxy-5-methyl-1-naphthoate + CoA
AMP + diphosphate + 2-hydroxy-5-methyl-1-naphthoyl-CoA
-
Substrates: kcat/Km is 50% compared to the wild-type value
Products: -
Products: -
?
ATP + 2-hydroxy-5-methyl-1-naphthoate + CoA
AMP + diphosphate + 2-hydroxy-5-methyl-1-naphthoyl-CoA
-
Substrates: kcat/Km is 50% compared to the wild-type value
Products: -
Products: -
?
ATP + 2-hydroxy-7-methoxy-1-naphthoate + CoA
AMP + diphosphate + 2-hydroxy-7-methoxy-1-naphthoyl-CoA
-
Substrates: kcat/Km is 5% compared to the wild-type value
Products: -
Products: -
?
ATP + 2-hydroxy-7-methoxy-1-naphthoate + CoA
AMP + diphosphate + 2-hydroxy-7-methoxy-1-naphthoyl-CoA
-
Substrates: kcat/Km is 5% compared to the wild-type value
Products: -
Products: -
?
ATP + 2-hydroxy-7-methoxy-5-methyl-1-naphthoate + CoA
AMP + diphosphate + 2-hydroxy-7-methoxy-5-methyl-1-naphthoyl-CoA
-
Substrates: the enzyme is involved in the biosynthesis of the enediyne antitumor antibiotic neocarzinostatin
Products: -
Products: -
?
ATP + 2-hydroxy-7-methoxy-5-methyl-1-naphthoate + CoA
AMP + diphosphate + 2-hydroxy-7-methoxy-5-methyl-1-naphthoyl-CoA
-
Substrates: -
Products: -
Products: -
?
ATP + 2-hydroxy-7-methoxy-5-methyl-1-naphthoate + CoA
AMP + diphosphate + 2-hydroxy-7-methoxy-5-methyl-1-naphthoyl-CoA
-
Substrates: 100% activity
Products: -
Products: -
?
ATP + 2-hydroxy-7-methoxy-5-methyl-1-naphthoate + CoA
AMP + diphosphate + 2-hydroxy-7-methoxy-5-methyl-1-naphthoyl-CoA
-
Substrates: the enzyme is involved in the biosynthesis of the enediyne antitumor antibiotic neocarzinostatin
Products: -
Products: -
?
ATP + 2-hydroxy-7-methoxy-5-methyl-1-naphthoate + CoA
AMP + diphosphate + 2-hydroxy-7-methoxy-5-methyl-1-naphthoyl-CoA
-
Substrates: -
Products: -
Products: -
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
ATP + 2-hydroxy-7-methoxy-5-methyl-1-naphthoate + CoA
AMP + diphosphate + 2-hydroxy-7-methoxy-5-methyl-1-naphthoyl-CoA
ATP + 2-hydroxy-7-methoxy-5-methyl-1-naphthoate + CoA
AMP + diphosphate + 2-hydroxy-7-methoxy-5-methyl-1-naphthoyl-CoA
-
Substrates: the enzyme is involved in the biosynthesis of the enediyne antitumor antibiotic neocarzinostatin
Products: -
Products: -
?
ATP + 2-hydroxy-7-methoxy-5-methyl-1-naphthoate + CoA
AMP + diphosphate + 2-hydroxy-7-methoxy-5-methyl-1-naphthoyl-CoA
-
Substrates: 100% activity
Products: -
Products: -
?
ATP + 2-hydroxy-7-methoxy-5-methyl-1-naphthoate + CoA
AMP + diphosphate + 2-hydroxy-7-methoxy-5-methyl-1-naphthoyl-CoA
-
Substrates: the enzyme is involved in the biosynthesis of the enediyne antitumor antibiotic neocarzinostatin
Products: -
Products: -
?
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0031
2,7-dihydroxy-5-methylnaphthalene-1-carboxylic acid
-
pH and temperature not specified in the publication
0.0011
2-hydroxy-5,7-dimethoxynaphthalene-1-carboxylic acid
-
pH and temperature not specified in the publication
0.00025
2-hydroxy-5-methylnaphthalene-1-carboxylic acid
-
pH and temperature not specified in the publication
0.0023
2-hydroxy-7-methoxynaphthalene-1-carboxylic acid
-
pH and temperature not specified in the publication
0.0034
2-hydroxynaphthalene-1-carboxylic acid
-
pH and temperature not specified in the publication
0.018
Naphthalene-1-carboxylic acid
-
pH and temperature not specified in the publication
0.00059
2-hydroxy-7-methoxy-5-methyl-1-naphthoate
-
pH 8.0, 24°C
0.00059
2-hydroxy-7-methoxy-5-methyl-1-naphthoate
-
pH and temperature not specified in the publication
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
1.55
2,7-dihydroxy-5-methylnaphthalene-1-carboxylic acid
-
pH and temperature not specified in the publication
0.42
2-hydroxy-5,7-dimethoxynaphthalene-1-carboxylic acid
-
pH and temperature not specified in the publication
0.135
2-hydroxy-5-methylnaphthalene-1-carboxylic acid
-
pH and temperature not specified in the publication
0.12
2-hydroxy-7-methoxynaphthalene-1-carboxylic acid
-
pH and temperature not specified in the publication
0.05
2-hydroxynaphthalene-1-carboxylic acid
-
pH and temperature not specified in the publication
0.11
Naphthalene-1-carboxylic acid
-
pH and temperature not specified in the publication
0.63
2-hydroxy-7-methoxy-5-methyl-1-naphthoate
-
pH and temperature not specified in the publication
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
Highest Expressing Human Cell Lines
Cell Line LinksPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
physiological function
physiological function
-
the enzyme is involved in the biosynthesis of the enediyne antitumor antibiotic neocarzinostatin
physiological function
-
the enzyme is involved in the biosynthesis of the enediyne antitumor antibiotic neocarzinostatin
-
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UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Cooke, H.A.; Zhang, J.; Griffin, M.A.; Nonaka, K.; van Lanen, S.G.; Shen, B.; Bruner, S.D.
Characterization of NcsB2 as a promiscuous naphthoic acid/coenzyme A ligase integral to the biosynthesis of the enediyne antitumor antibiotic neocarzinostatin
J. Am. Chem. Soc.
129
7728-7729
2007
Streptomyces carzinostaticus, Streptomyces carzinostaticus ATCC 15944
brenda
EXTERNAL LINKS (specific for EC-Number 6.2.1.43)
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Release 2026.1 (March 2026)
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