We're sorry, but BRENDA doesn't work properly without JavaScript. Please make sure you have JavaScript enabled in your browser settings.
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
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.
Synonyms
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
S-adenosyl-L-methionine + 2,7-dihydroxy-5-methyl-1-naphthoate = S-adenosyl-L-homocysteine + 2-hydroxy-7-methoxy-5-methyl-1-naphthoate
-
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
S-adenosyl-L-methionine + 1,4-dihydroxy-2-naphthoic acid
S-adenosyl-L-homocysteine + 1-hydroxy-4-methoxy-2-naphthoate
Substrates: 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
S-adenosyl-L-methionine + 3,5-dihydroxy-2-naphthoate
S-adenosyl-L-homocysteine + 3-hydroxy-5-methoxy-2-naphthoate
Substrates: 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
Substrates: kcat/KM is 14% compared to the wild-type value
?
additional information
?
-
Substrates: 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
?
S-adenosyl-L-methionine + 2,7-dihydroxy-5-methyl-1-naphthoate
S-adenosyl-L-homocysteine + 2-hydroxy-7-methoxy-5-methyl-1-naphthoate
Substrates: the enzyme is involved in the biosynthesis of the enediyne antitumor antibiotic neocarzinostatin
?
S-adenosyl-L-methionine + 2,7-dihydroxy-5-methyl-1-naphthoate
S-adenosyl-L-homocysteine + 2-hydroxy-7-methoxy-5-methyl-1-naphthoate
Substrates: -
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
S-adenosyl-L-methionine + 2,7-dihydroxy-5-methyl-1-naphthoate
S-adenosyl-L-homocysteine + 2-hydroxy-7-methoxy-5-methyl-1-naphthoate
Substrates: the enzyme is involved in the biosynthesis of the enediyne antitumor antibiotic neocarzinostatin
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Cu2+
complete loss of activity
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
0.206
2,7-dihydroxy-5-methyl-1-naphthoate
pH 7.5, 25°C, wild-type enzyme
0.206
2,7-dihydroxy-5-methyl-1-naphthoate
pH 6.0, 25°C
0.319
2,7-dihydroxy-5-methyl-1-naphthoate
pH 7.5, 25°C, mutant enzyme R11K
0.4
2,7-dihydroxy-5-methyl-1-naphthoate
pH 7.5, 25°C, mutant enzyme R11W
0.419
2,7-dihydroxy-5-methyl-1-naphthoate
pH 7.5, 25°C, mutant enzyme R11A
0.649
2,7-dihydroxy-5-methyl-1-naphthoate
pH 7.5, 25°C, mutant enzyme Y293I
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
0.01
2,7-dihydroxy-5-methyl-1-naphthoate
pH 7.5, 25°C, mutant enzyme R11W
0.0115
2,7-dihydroxy-5-methyl-1-naphthoate
pH 7.5, 25°C, wild-type enzyme
0.0115
2,7-dihydroxy-5-methyl-1-naphthoate
pH 6.0, 25°C
0.013
2,7-dihydroxy-5-methyl-1-naphthoate
pH 7.5, 25°C, mutant enzyme Y293I
0.02
2,7-dihydroxy-5-methyl-1-naphthoate
pH 7.5, 25°C, mutant enzyme R11A
0.02
2,7-dihydroxy-5-methyl-1-naphthoate
pH 7.5, 25°C, mutant enzyme R11K
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
0.02
2,7-dihydroxy-5-methyl-1-naphthoate
pH 7.5, 25°C, mutant enzyme Y293I
0.025
2,7-dihydroxy-5-methyl-1-naphthoate
pH 7.5, 25°C, mutant enzyme R11W
0.048
2,7-dihydroxy-5-methyl-1-naphthoate
pH 7.5, 25°C, mutant enzyme R11A
0.06
2,7-dihydroxy-5-methyl-1-naphthoate
pH 7.5, 25°C, wild-type enzyme
0.06
2,7-dihydroxy-5-methyl-1-naphthoate
pH 6.0, 25°C
0.063
2,7-dihydroxy-5-methyl-1-naphthoate
pH 7.5, 25°C, mutant enzyme TR11K
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
6 - 8
pH 6.0: optimum, pH 8.0: about 50% of maximal activity, no activity below pH 5.5
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
-
UniProt
brenda
Highest Expressing Human Cell Lines
Filter by:
Cell Line Links
Gene Links
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
physiological function
the enzyme is involved in the biosynthesis of the enediyne antitumor antibiotic neocarzinostatin
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
NCSB1_STRCZ
332
0
34592
Swiss-Prot
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
39500
x * 39500, SDS-PAGE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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)
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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)
brenda
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)
brenda
html completed
show
top
