Information on EC 1.14.99.40 - 5,6-dimethylbenzimidazole synthase

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
1.14.99.40
transferred to EC 1.13.11.79
RECOMMENDED NAME
GeneOntology No.
5,6-dimethylbenzimidazole synthase
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
FMNH2 + NADH + H+ + O2 = 5,6-dimethylbenzimidazole + D-erythrose 4-phosphate + NAD+ + other product
show the reaction diagram
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
gene bluB
UniProt
Manually annotated by BRENDA team
gene bluB
UniProt
Manually annotated by BRENDA team
gene bluB
UniProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
FMNH2 + NADH + H+ + O2
5,6-dimethylbenzimidazole + D-erythrose 4-phosphate + NAD+ + other product
show the reaction diagram
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
FMNH2 + NADH + H+ + O2
5,6-dimethylbenzimidazole + D-erythrose 4-phosphate + NAD+ + other product
show the reaction diagram
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
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 hide
LITERATURE
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
gene bluB, expression in Escherichia coli strain BL21star(DE3)pLysS
gene bluB, genotyping
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
A156V
site-directed mutagenesis, inactive mutant
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
E78K
site-directed mutagenesis, the mutant is not soluble
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
G193D
site-directed mutagenesis, inactive mutant
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
P65L
site-directed mutagenesis, inactive mutant
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