Information on EC 1.3.99.B12 - menaquinone-7 reductase (acceptor)

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The expected taxonomic range for this enzyme is: Archaeoglobus fulgidus

EC NUMBER
COMMENTARY hide
1.3.99.B12
preliminary BRENDA-supplied EC number
RECOMMENDED NAME
GeneOntology No.
menaquinone-7 reductase (acceptor)
-
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
menaquinone-7 with partially saturated prenyl side chain + acceptor = menaquinone-7 + reduced acceptor
show the reaction diagram
-
-
-
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
SwissProt
Manually annotated by BRENDA team
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
menaquinone-7 + reduced acceptor
?
show the reaction diagram
the enzyme is involved in the biosynthesis of menaquinone-7(14H) i.e. menaquinone with a fully saturated heptaprenyl side chain
-
-
?
menaquinone-7 + reduced dithionite
menaquinone-7 with partially saturated prenyl side chain + dithionite
show the reaction diagram
menaquinone-7 i.e. menaquinone with a fully saturated heptaprenyl side chain. The enzyme specifically reduces the prenyl side chain of menaquinone, whereas the prenyl moieties of ubiquinone-8 and geranygeranyl diphosphates are relatively resistant to reduction. The enzyme is not able to utilize NAD(P)H as the electron donor
-
-
?
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
menaquinone-7 + reduced acceptor
?
show the reaction diagram
O29609
the enzyme is involved in the biosynthesis of menaquinone-7(14H) i.e. menaquinone with a fully saturated heptaprenyl side chain
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
FAD
noncovalently bound to the enzyme
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli