Information on EC 1.1.4.B1 - prostamide synthase

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
1.1.4.B1
preliminary BRENDA-supplied EC number
RECOMMENDED NAME
GeneOntology No.
prostamide synthase
-
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
prostamide F2alpha + oxidized thioredoxin = prostamide H2 + reduced thioredoxin
show the reaction diagram
SYSTEMATIC NAME
IUBMB Comments
prostamide F2alpha:oxidized thioredoxin oxidoreductase
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
SwissProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
-
prostaglandin ethanolamide, i.e. prostamide, F2alpha is a COX-2-catalyzed metabolite of arachidonoyl ethanolamide (anandamide) that induces pharmacological actions in ocular tissues. Prostamide/PGF synthase catalyzes the reductions of prostamide H2 to prostamide F2alpha and PGH2 to PGF2alpha, chiefly in the central nervous system
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
cumene hydroperoxide + reduced thioredoxin
? + oxidized thioredoxin
show the reaction diagram
hydrogen peroxide + reduced thioredoxin
? + oxidized thioredoxin
show the reaction diagram
prostaglandin H2 + NADPH + H+
(5Z,13E)-(15S)-9alpha,11alpha,15-trihydroxyprosta-5,13-dienoate + NADP+
show the reaction diagram
prostaglandin H2 + reduced thioredoxin
(5Z,13E)-(15S)-9alpha,11alpha,15-trihydroxyprosta-5,13-dienoate + oxidized thioredoxin
show the reaction diagram
prostamide H2 + NADPH + H+
prostamide F2alpha + NADP+
show the reaction diagram
prostamide H2 + reduced thioredoxin
prostamide F2alpha + oxidized thioredoxin
show the reaction diagram
tert-butyl hydroperoxide + reduced thioredoxin
? + oxidized thioredoxin
show the reaction diagram
additional information
?
-
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
glutathione
NADPH
thioredoxin
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
ammonium sulfate
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.026
cumene hydroperoxide
-
pH 7.0, 24°C
1.6
hydrogen peroxide
-
pH 7.0, 24°C
0.0069
prostaglandin H2
-
pH 7.0, 24°C
0.0076
prostamide H2
0.001
reduced thioredoxin
-
pH 7.0, 24°C
0.4
tert-butyl peroxide
-
pH 7.0, 24°C
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.12
cumene hydroperoxide
0.12
hydrogen peroxide
0.247
prostaglandin H2
0.09
prostamide H2
0.09
reduced thioredoxin
0.09
tert-butyl peroxide
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.053
substrate prostamide H2, pH 7.0, 24°C
0.062
substrate prostaglandin H2, pH 7.0, 24°C
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
-
enzyme distribution in the tissue, expression analysis, overview. The enzyme is expressed preferentially in the white matter bundles of the entire CNS of adult mice with less marked expression in neuronal cell bodies. The enzyme is colocalized with myelin basic protein in myelin sheaths but not in axons. At the ultrastructural level, the enzyme is localized to myelin sheaths
Manually annotated by BRENDA team
-
activity in decreasing order: ovary, uterus, testis, and vesicular gland
Manually annotated by BRENDA team
-
activity in decreasing order: ovary, uterus, testis, and vesicular gland
Manually annotated by BRENDA team
-
activity in decreasing order: ovary, uterus, testis, and vesicular gland
Manually annotated by BRENDA team
-
activity in decreasing order: ovary, uterus, testis, and vesicular gland
Manually annotated by BRENDA team
additional information
-
expression of the enzyme increases between P9 and P14 during the postnatal development, presumably in accordance with myelinogenesis
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
about 70% of activity in the cytosolic fraction
-
Manually annotated by BRENDA team
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
20000
x * 20000, SDS-PAGE
21669
-
x * 21669, calculated, x * 23000, SDS-PAGE
23000
-
x * 21669, calculated, x * 23000, SDS-PAGE
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
-
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
C44S
-
less than 1% of wild-type activity
C44S/C47S
-
less than 1% of wild-type activity
C47S
-
about 63% of wild-type activity