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Information on EC 2.1.1.303 - 2,7-dihydroxy-5-methyl-1-naphthoate 7-O-methyltransferase and Organism(s) Streptomyces carzinostaticus and UniProt Accession Q84HC8

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IUBMB Comments
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.
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Streptomyces carzinostaticus
UNIPROT: Q84HC8
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The taxonomic range for the selected organisms is: Streptomyces carzinostaticus
The enzyme appears in selected viruses and cellular organisms
Synonyms
ncsb1, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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.
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
kcat/KM is 10% compared to the wild-type value
-
-
?
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
kcat/KM is 23% compared to the wild-type value
-
-
?
S-adenosyl-L-methionine + 3,7-dihydroxy-2-naphthoate
S-adenosyl-L-homocysteine + 3-hydroxy-7-methoxy-2-naphthoate
show the reaction diagram
kcat/KM is 14% compared to the wild-type value
-
-
?
additional information
?
-
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
-
-
?
NATURAL SUBSTRATE
NATURAL 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 + 2,7-dihydroxy-5-methyl-1-naphthoate
S-adenosyl-L-homocysteine + 2-hydroxy-7-methoxy-5-methyl-1-naphthoate
show the reaction diagram
the enzyme is involved in the biosynthesis of the enediyne antitumor antibiotic neocarzinostatin
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Ca2+
increases activity
Mn2+
increases activity
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
Cu2+
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
pH 6.0, 25°C
0.206 - 0.649
2,7-dihydroxy-5-methyl-1-naphthoate
0.352
3,5-dihydroxy-2-naphthoate
pH 6.0, 25°C
0.066
3,7-dihydroxy-2-naphthoate
pH 6.0, 25°C
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.000133
1,4-dihydroxy-2-naphthoic acid
pH 6.0, 25°C
0.01 - 0.02
2,7-dihydroxy-5-methyl-1-naphthoate
0.0045
3,5-dihydroxy-2-naphthoate
pH 6.0, 25°C
0.0004
3,7-dihydroxy-2-naphthoate
pH 6.0, 25°C
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0055
1,4-dihydroxy-2-naphthoic acid
pH 6.0, 25°C
0.02 - 0.063
2,7-dihydroxy-5-methyl-1-naphthoate
0.013
3,5-dihydroxy-2-naphthoate
pH 6.0, 25°C
0.0061
3,7-dihydroxy-2-naphthoate
pH 6.0, 25°C
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6 - 8
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
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
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
NCSB1_STRCZ
332
0
34592
Swiss-Prot
-
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
39500
x * 39500, SDS-PAGE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
R11A
kcat/Km is 88% of the wild-type value
R11K
kcat/Km is 110% of the wild-type value
R11W
kcat/Km is 45% of the wild-type value
Y293I
kcat/Km is 35% of the wild-type value
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)
the enzyme is overproduced as an N-terminal His6-tagged fusion protein using expression plasmid pBS5039 in Escherichia coli BL21(DE3)
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Cooke, H.A.; Guenther, E.L.; Luo, Y.; Shen, B.; Bruner, S.D.
Molecular basis of substrate promiscuity for the SAM-dependent O-methyltransferase NcsB1, involved in the biosynthesis of the enediyne antitumor antibiotic neocarzinostatin
Biochemistry
48
9590-9598
2009
Streptomyces carzinostaticus (Q84HC8)
Manually annotated by BRENDA team
Luo, Y.; Lin, S.; Zhang, J.; Cooke, H.A.; Bruner. S.D.; Shen, B.
Regiospecific O-methylation of naphthoic acids catalyzed by NcsB1, an O-methyltransferase involved in the biosynthesis of the enediyne antitumor antibiotic neocarzinostatin
J. Biol. Chem.
283
14694-14702
2008
Streptomyces carzinostaticus (Q84HC8)
Manually annotated by BRENDA team