Information on EC 2.1.1.303 - 2,7-dihydroxy-5-methyl-1-naphthoate 7-O-methyltransferase

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The expected taxonomic range for this enzyme is: Streptomyces carzinostaticus

EC NUMBER
COMMENTARY hide
2.1.1.303
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RECOMMENDED NAME
GeneOntology No.
2,7-dihydroxy-5-methyl-1-naphthoate 7-O-methyltransferase
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
S-adenosyl-L-methionine + 2,7-dihydroxy-5-methyl-1-naphthoate = S-adenosyl-L-homocysteine + 2-hydroxy-7-methoxy-5-methyl-1-naphthoate
show the reaction diagram
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
Biosynthesis of antibiotics
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Biosynthesis of enediyne antibiotics
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SYSTEMATIC NAME
IUBMB Comments
S-adenosyl-L-methionine:2,7-dihydroxy-5-methyl-1-naphthoate 7-O-methyltransferase
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.
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
the enzyme is involved in the biosynthesis of the enediyne antitumor antibiotic neocarzinostatin
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
S-adenosyl-L-methionine + 1,4-dihydroxy-2-naphthoic acid
S-adenosyl-L-homocysteine + 1-hydroxy-4-methoxy-2-naphthoate
show the reaction diagram
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kcat/KM is 10% compared to the wild-type value
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-
?
S-adenosyl-L-methionine + 2,7-dihydroxy-5-methyl-1-naphthoate
S-adenosyl-L-homocysteine + 2-hydroxy-7-methoxy-5-methyl-1-naphthoate
show the reaction diagram
S-adenosyl-L-methionine + 3,5-dihydroxy-2-naphthoate
S-adenosyl-L-homocysteine + 3-hydroxy-5-methoxy-2-naphthoate
show the reaction diagram
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kcat/KM is 23% compared to the wild-type value
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-
?
S-adenosyl-L-methionine + 3,7-dihydroxy-2-naphthoate
S-adenosyl-L-homocysteine + 3-hydroxy-7-methoxy-2-naphthoate
show the reaction diagram
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kcat/KM is 14% compared to the wild-type value
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?
additional information
?
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NcsB1 also recognizes other dihydroxynaphthoic acids as substrates and catalyzes regiospecific O-methylation. The carboxylate and its ortho-hydroxy groups of the substrate appear to be crucial for NcsB1 substrate recognition and binding, and O-methylation takes place only at the free hydroxy group of these dihydroxynaphthoic acids
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NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
S-adenosyl-L-methionine + 2,7-dihydroxy-5-methyl-1-naphthoate
S-adenosyl-L-homocysteine + 2-hydroxy-7-methoxy-5-methyl-1-naphthoate
show the reaction diagram
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Ca2+
-
increases activity
Mn2+
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increases activity
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
Cu2+
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complete loss of activity
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.024
1,4-dihydroxy-2-naphthoic acid
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pH 6.0, 25C
0.206 - 0.649
2,7-dihydroxy-5-methyl-1-naphthoate
0.352
3,5-dihydroxy-2-naphthoate
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pH 6.0, 25C
0.066
3,7-dihydroxy-2-naphthoate
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pH 6.0, 25C
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.000133
1,4-dihydroxy-2-naphthoic acid
Streptomyces carzinostaticus
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pH 6.0, 25C
0.01 - 0.02
2,7-dihydroxy-5-methyl-1-naphthoate
0.0045
3,5-dihydroxy-2-naphthoate
Streptomyces carzinostaticus
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pH 6.0, 25C
0.0004
3,7-dihydroxy-2-naphthoate
Streptomyces carzinostaticus
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pH 6.0, 25C
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0055
1,4-dihydroxy-2-naphthoic acid
Streptomyces carzinostaticus
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pH 6.0, 25C
21233
0.02 - 0.063
2,7-dihydroxy-5-methyl-1-naphthoate
4455
0.013
3,5-dihydroxy-2-naphthoate
Streptomyces carzinostaticus
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pH 6.0, 25C
42635
0.0061
3,7-dihydroxy-2-naphthoate
Streptomyces carzinostaticus
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pH 6.0, 25C
42636
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6 - 8
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pH 6.0: optimum, pH 8.0: about 50% of maximal activity, no activity below pH 5.5
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
39500
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x * 39500, SDS-PAGE
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
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x * 39500, SDS-PAGE
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
the enzyme is crystallized with a substituted naphthoic acid and/or S-adenosyl-L-methionine/S-adenosyl-L-homocysteine by the hanging drop vapor diffusion method
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
NcsB1 is overproduced as an N-terminal His6-tagged fusion protein in Escherichia coli BL21(DE3)
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the enzyme is overproduced as an N-terminal His6-tagged fusion protein using expression plasmid pBS5039 in Escherichia coli BL21(DE3)
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
R11A
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kcat/Km is 88% of the wild-type value
R11K
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kcat/Km is 110% of the wild-type value
R11W
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kcat/Km is 45% of the wild-type value
Y293I
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kcat/Km is 35% of the wild-type value