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Enzyme Nomenclature
Information on EC 1.14.99.40 - 5,6-dimethylbenzimidazole synthase
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The enzyme appears in viruses and cellular organisms
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EC NUMBER 
COMMENTARY 
1.14.99.40
transferred to EC 1.13.11.79
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RECOMMENDED NAME
GeneOntology No.
5,6-dimethylbenzimidazole synthase
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
FMNH2 + NADH + H+ + O2 = 5,6-dimethylbenzimidazole + D-erythrose 4-phosphate + NAD+ + other product
FMNH2 + NADH + H+ + O2 = 5,6-dimethylbenzimidazole + D-erythrose 4-phosphate + NAD+ + other product
first step in the proposed mechanism is the activation of molecular oxygen forming a 4a-peroxyflavin intermediate, the 4a-peroxyflavin is generated rapidly and is followed by a much slower decay phase, mechanism overview
FMNH2 + NADH + H+ + O2 = 5,6-dimethylbenzimidazole + D-erythrose 4-phosphate + NAD+ + other product
first step in the proposed mechanism is the activation of molecular oxygen forming a 4a-peroxyflavin intermediate, the 4a-peroxyflavin is generated rapidly and is followed by a much slower decay phase, mechanism overview
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FMNH2 + NADH + H+ + O2 = 5,6-dimethylbenzimidazole + D-erythrose 4-phosphate + NAD+ + other product
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
CbiY from Bacillus megaterium is not a BluB protein
additional information
identification of catalytic residues involved in the reaction, mutational analysis, overview. The enzyme shows interactions with the phosphate group and ribityl tail of FMN
additional information
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CbiY from Bacillus megaterium is not a BluB protein
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
FMNH2 + NADH + H+ + O2
5,6-dimethylbenzimidazole + D-erythrose 4-phosphate + NAD+ + other product
FMNH2 + NADH + H+ + O2
5,6-dimethylbenzimidazole + D-erythrose 4-phosphate + NAD+ + other product
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-
-
?
FMNH2 + NADH + H+ + O2
5,6-dimethylbenzimidazole + D-erythrose 4-phosphate + NAD+ + other product
NADH is required to reduce FMN to FMNH2 which is the substrate for the BluB reaction. BluB forms a peroxyflavin intermediate
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-
?
FMNH2 + NADH + H+ + O2
5,6-dimethylbenzimidazole + D-erythrose 4-phosphate + NAD+ + other product
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-
?
FMNH2 + NADH + H+ + O2
5,6-dimethylbenzimidazole + D-erythrose 4-phosphate + NAD+ + other product
NADH is required to reduce FMN to FMNH2 which is the substrate for the BluB reaction. BluB forms a peroxyflavin intermediate
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-
?
FMNH2 + NADH + H+ + O2
5,6-dimethylbenzimidazole + D-erythrose 4-phosphate + NAD+ + other product
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5,6-dimethylbenzimidazole is the lower axial ligand of vitamin B12, i.e. cobalamin
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?
FMNH2 + NADH + H+ + O2
5,6-dimethylbenzimidazole + D-erythrose 4-phosphate + NAD+ + other product
BluB fragments a flavin isoalloxazine ring
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?
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NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
FMNH2 + NADH + H+ + O2
5,6-dimethylbenzimidazole + D-erythrose 4-phosphate + NAD+ + other product
FMNH2 + NADH + H+ + O2
5,6-dimethylbenzimidazole + D-erythrose 4-phosphate + NAD+ + other product
D5DCL0
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-
-
?
FMNH2 + NADH + H+ + O2
5,6-dimethylbenzimidazole + D-erythrose 4-phosphate + NAD+ + other product
D5DCL0
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-
-
?
FMNH2 + NADH + H+ + O2
5,6-dimethylbenzimidazole + D-erythrose 4-phosphate + NAD+ + other product
Q92PC8
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5,6-dimethylbenzimidazole is the lower axial ligand of vitamin B12, i.e. cobalamin
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?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
NADH
NADH is required to reduce FMN to FMNH2 which is the substrate for the BluB reaction
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
FMN/FMNH2 dissociation constants and free energy of binding of wild-type and mutant enzymes, overview
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
gene bluB, expression in Escherichia coli strain BL21star(DE3)pLysS
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
D32N
site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme
D32N/S167G
site-directed mutagenesis, the mutant shows no activity
G110S
site-directed mutagenesis, the mutant shows no 5,6-dimethylbenzimidazole forming activity
G133S
site-directed mutagenesis, the mutant shows no 5,6-dimethylbenzimidazole forming activity
G61D
site-directed mutagenesis, the mutant shows no 5,6-dimethylbenzimidazole forming activity
M140I
site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme
M94I
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
P202L
site-directed mutagenesis, the mutant shows no 5,6-dimethylbenzimidazole forming activity
R30C
site-directed mutagenesis, the mutant shows no 5,6-dimethylbenzimidazole forming activity
R30H
site-directed mutagenesis, the mutant shows no 5,6-dimethylbenzimidazole forming activity
S167G
site-directed mutagenesis, the mutant shows higly reduced activity compared to the wild-type enzyme
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LINKS TO OTHER DATABASES (specific for EC-Number 1.14.99.40)
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