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Information on EC 1.3.1.3 - DELTA4-3-oxosteroid 5beta-reductase and Organism(s) Arabidopsis thaliana and UniProt Accession Q9STX2

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IUBMB Comments
The enzyme from human efficiently catalyses the reduction of progesterone, androstenedione, 17alpha-hydroxyprogesterone and testosterone to 5beta-reduced metabolites; it can also act on aldosterone, corticosterone and cortisol, but to a lesser extent . The bile acid intermediates 7alpha,12alpha-dihydroxy-4-cholesten-3-one and 7alpha-hydroxy-4-cholesten-3-one can also act as substrates .
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Select one or more organisms in this record:
This record set is specific for:
Arabidopsis thaliana
UNIPROT: Q9STX2
Word Map
The taxonomic range for the selected organisms is: Arabidopsis thaliana
The enzyme appears in selected viruses and cellular organisms
Synonyms
3-oxo-DELTA4-steroid 5beta-reductase, 4,5beta-dihydrocortisone:NADP+ DELTA4-oxidoreductase, 5-beta-reductase, 5beta-POR, 5beta-red, AKR1D1, aldo-keto reductase, aldo-keto reductase 1D1, aldo–keto reductase 1D1, androstenedione 5beta-reductase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4,5beta-dihydrocortisone:NADP+ DELTA4-oxidoreductase
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-
-
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5-beta-reductase
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-
-
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androstenedione 5beta-reductase
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-
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cortisone 5beta-reductase
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cortisone beta-reductase
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-
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DELTA 4-5beta-reductase
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-
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DELTA4-3-ketosteroid 5beta-reductase
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DELTA4-hydrogenase
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P5betaR
299676
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progesterone 5beta-reductase
299676
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reductase, cholestenone 5beta.-
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reductase, cortisone DELTA4-5beta-
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steroid 5beta.-reductase
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testosterone 5-beta-reductase
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testosterone 5beta-reductase
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-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
oxidation
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redox reaction
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reduction
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SYSTEMATIC NAME
IUBMB Comments
5beta-cholestan-3-one:NADP+ 4,5-oxidoreductase
The enzyme from human efficiently catalyses the reduction of progesterone, androstenedione, 17alpha-hydroxyprogesterone and testosterone to 5beta-reduced metabolites; it can also act on aldosterone, corticosterone and cortisol, but to a lesser extent [8]. The bile acid intermediates 7alpha,12alpha-dihydroxy-4-cholesten-3-one and 7alpha-hydroxy-4-cholesten-3-one can also act as substrates [9].
CAS REGISTRY NUMBER
COMMENTARY hide
37255-35-9
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9029-08-7
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SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
2-cyclohexen-1-one + NADPH + H+
cyclohexanone + NADP+
show the reaction diagram
-
-
-
?
progesterone + NADPH + H+
5beta-pregnane-3,20-dione + NADP+
show the reaction diagram
-
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
2-cyclohexen-1-one + NADPH + H+
cyclohexanone + NADP+
show the reaction diagram
Q9STX2
-
-
-
?
progesterone + NADPH + H+
5beta-pregnane-3,20-dione + NADP+
show the reaction diagram
Q9STX2
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-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.116
2-cyclohexen-1-one
pH 8.0, 40°C, recombinant wild-type enzyme
0.268
progesterone
pH 8.0, 40°C, recombinant wild-type enzyme
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1.11
2-cyclohexen-1-one
pH 8.0, 40°C, recombinant wild-type enzyme
0.17
progesterone
pH 8.0, 40°C, recombinant wild-type enzyme
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
9.607
2-cyclohexen-1-one
pH 8.0, 40°C, recombinant wild-type enzyme
0.628
progesterone
pH 8.0, 40°C, recombinant wild-type enzyme
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
evolution
the enzyme belongs to the aldo–keto reductase (AKR) family, sequence comparisons, overview
additional information
the enzyme shows high catalytic efficiency
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
Sequence
VEP1_ARATH
388
0
44230
Swiss-Prot
PURIFICATION/commentary
ORGANISM
UNIPROT
LITERATURE
recombinant wild-type and mutant enzymes from Escherichia coli strain M15 by nickel affinity chromatography
CLONED/commentary
ORGANISM
UNIPROT
LITERATURE
DNA and amino acid sequence determination and analysis, sequence comparisons, expression of wild-type and mutant enzymes in Escherichia coli strain M15
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Bauer, P.; Rudolph, K.; Mueller-Uri, F.; Kreis, W.
Vein patterning 1-encoded progesterone 5beta-reductase: activity-guided improvement of catalytic efficiency
Phytochemistry
77
53-59
2012
Arabidopsis thaliana (Q9STX2), Digitalis lanata
Manually annotated by BRENDA team
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