Information on EC 1.10.2.1 - L-ascorbate-cytochrome-b5 reductase

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
1.10.2.1
-
RECOMMENDED NAME
GeneOntology No.
L-ascorbate-cytochrome-b5 reductase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
L-ascorbate + ferricytochrome b5 = monodehydroascorbate + ferrocytochrome b5 + H+
show the reaction diagram
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-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
oxidation
-
-
-
-
redox reaction
-
-
-
-
reduction
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
L-ascorbate:ferricytochrome-b5 oxidoreductase
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CAS REGISTRY NUMBER
COMMENTARY hide
37237-57-3
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
-
-
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
L-(+)-ascorbate + ferricytochrome b5
monodehydro-L(+)-ascorbate + ferrocytochrome b5
show the reaction diagram
L-ascorbate + ferricytochrome b5
monodehydro-L-ascorbate + ferrocytochrome b5
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
L-(+)-ascorbate + ferricytochrome b5
monodehydro-L(+)-ascorbate + ferrocytochrome b5
show the reaction diagram
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
asolectin
-
lipid micelles increases activity about 2fold
-
lecithin
-
lipid micelles increases activity about 2fold
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.001 - 0.009
cytochrome b5
-
12
L-ascorbate
-
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.0163
-
microsomes after ultracentrifugation
6.5
-
microsomes after CM-cellulose-chromatography, ultrafiltration and dialysis P2
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.4 - 6.7
-
-
6.8
-
Sepharose-bound cytochrome b5 as substrate
6.9
-
enriched enzyme
7.2 - 7.4
-
in microsomes
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
-
duodenal brush border membrane
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
45
-
denaturation above
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
enzymes loses its activity during isoelectric focusing
-
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
0°C, enzymatic activity tolerates ampholine over a 24 h period
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
gene appears to encode the corresponding reductase cloned from mouse
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