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Information on EC 1.1.1.36 - acetoacetyl-CoA reductase and Organism(s) Homo sapiens and UniProt Accession C9JRZ8

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Homo sapiens
UNIPROT: C9JRZ8 not found.
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The taxonomic range for the selected organisms is: Homo sapiens
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Synonyms
acetoacetyl-coa reductase, mfe-2, akr1b15, nadph-dependent acetoacetyl-coa reductase, ketoacyl reductase, d-3-hydroxyacyl-coa dehydrogenase, (3r)-hydroxyacyl-coa dehydrogenase, acetoacetyl coa reductase, nadh-preferring acetoacetyl-coa reductase, nadph-linked acetoacetyl-coa reductase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
aldo-keto reductase 1B15
-
(3R)-hydroxyacyl-CoA dehydrogenase
(R)-3-hydroxyacyl-CoA dehydrogenase
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-
-
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acetoacetyl coenzyme A reductase
-
-
-
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beta-ketoacyl-CoA reductase
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-
-
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D(-)-beta-hydroxybutyryl CoA-NADP oxidoreductase
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-
-
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D-3-hydroxyacyl-CoA reductase
-
-
-
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hydroxyacyl coenzyme-A dehydrogenase
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-
-
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NADP-linked acetoacetyl CoA reductase
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-
-
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NADPH:acetoacetyl-CoA reductase
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-
-
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short chain beta-ketoacetyl(acetoacetyl)-CoA reductase
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-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
redox reaction
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-
-
-
SYSTEMATIC NAME
IUBMB Comments
(R)-3-hydroxyacyl-CoA:NADP+ oxidoreductase
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CAS REGISTRY NUMBER
COMMENTARY hide
9028-41-5
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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
acetoacetyl-CoA + NADPH + H+
3-hydroxybutyryl-CoA + NADP+
show the reaction diagram
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-
-
r
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
acetoacetyl-CoA + NADPH + H+
3-hydroxybutyryl-CoA + NADP+
show the reaction diagram
-
-
-
r
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0634
acetoacetyl-CoA
pH 7.4, 37°C recombinant His-tagged enzyme
additional information
additional information
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.5
acetoacetyl-CoA
pH 7.4, 37°C recombinant His-tagged enzyme
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
10
acetoacetyl-CoA
pH 7.4, 37°C recombinant His-tagged enzyme
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.023
0.039
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strain HsMFE-2(E408A), (3R)-hydroxyacyl-CoA dehydrogenase
0.041
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strain HsMFE-2(D490A), (3R)-hydroxyacyl-CoA dehydrogenase
0.046
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strain HsMFE-2(H406A), (3R)-hydroxyacyl-CoA dehydrogenase
0.047
-
strain HsMFE-2(D370A), (3R)-hydroxyacyl-CoA dehydrogenase
0.048
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strain HsMFE-2(D517A), (3R)-hydroxyacyl-CoA dehydrogenase
0.051
-
strain HsMFE-2(D510A), (3R)-hydroxyacyl-CoA dehydrogenase
0.056
-
strain HsMFE-2(E366A), (3R)-hydroxyacyl-CoA dehydrogenase
0.066
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strain HsMFE-2(H532A), (3R)-hydroxyacyl-CoA dehydrogenase
0.08
-
(3R)-hydroxyacyl-CoA dehydrogenase, Hs MFE-2
0.082
-
strain HsMFE-2, (3R)-hydroxyacyl-CoA dehydrogenase
0.091
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strain UTL-7A, (3R)-hydroxyacyl-CoA dehydrogenase
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.4
assay at
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
37
assay at
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
UniProt
Manually annotated by BRENDA team
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
isozymes AKR1B15.1 and AKR1B15.2
Manually annotated by BRENDA team
fetal, very low expression of isozyme AKR1B15.2
Manually annotated by BRENDA team
very low expression of isozymes AKR1B15.1 and AKR1B15.2
Manually annotated by BRENDA team
isozymes AKR1B15.1 and AKR1B15.2
Manually annotated by BRENDA team
low expression of isozymes AKR1B15.1 and AKR1B15.2
Manually annotated by BRENDA team
isozymes AKR1B15.1 and AKR1B15.2
Manually annotated by BRENDA team
isozyme AKR1B15.1
Manually annotated by BRENDA team
isozymes AKR1B15.1 and AKR1B15.2
Manually annotated by BRENDA team
isozyme AKR1B15.1, very low expression of isozyme AKR1B15.2
Manually annotated by BRENDA team
isozymes AKR1B15.1 and AKR1B15.2
Manually annotated by BRENDA team
isozyme AKR1B15.2
Manually annotated by BRENDA team
very low expression of isozymes AKR1B15.1 and AKR1B15.2
Manually annotated by BRENDA team
additional information
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
isozyme AKR1B15.2
Manually annotated by BRENDA team
isozyme AKR1B15.1
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
metabolism
AKR1B15.1 is a mitochondrial carbonyl reductase. Two alternatively spliced protein isoforms encoded by the human AKRgene AKR1B15 exist, the AKR1B15.1 isoform catalyzes reduction of steroids and 3-keto-acyl-CoA conjugates
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
AK1BF_HUMAN
316
0
36537
Swiss-Prot
-
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
D370A
-
site-directed mutagenesis
D490A
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site-directed mutagenesis
D510A
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site-directed mutagenesis, inactive
D517A
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site-directed mutagenesis
E366A
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site-directed mutagenesis, kcat/Km 100times lower than that of the wild type
E408A
-
site-directed mutagenesis
G16S
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site-directed mutagenesis
H406A
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site-directed mutagenesis
H515A
-
site-directed mutagenesis
H532A
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site-directed mutagenesis
Y347A
-
site-directed mutagenesis
Y410A
-
site-directed mutagenesis
Y505A
-
site-directed mutagenesis
additional information
-
constructs are tested for complementation in Saccharomyces cerevisiae
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant His-tagged isozymes AKR1B15.1 and AKR1B15.2 isozymes from Escherichia coli strain BL21(DE3) by nickel affinity chromatography
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
gene AKR1B15 located on chromosome 7, cloning of two isoforms: AKR1B15.1 and AKR1B15.2, DNA and amino acid sequence determination and analysis, recombinant expression of N-terminally His-tagged isozymes in Escherichia coli strain BL21(DE3), recombinant expression of C- or N-terminally c-Myctagged isozymes in HEK-293 cells
wild type (HsMFE-2) and its variants are expressed in Saccharomyces cerevisiae
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Qin, Y.M.; Haapalainen, A.M.; Kilpelainen, S.H.; Marttila, M.S.; Koski, M.K.; Glumoff, T.; Novikov, D.K.; Hiltunen, J.K.
Human peroxisomal multifunctional enzyme type 2: site-directed mutagenesis studies show the importance of two protic residues for 2-enoyl-CoA hydratase 2 activity
J. Biol. Chem.
275
4965-4972
2000
Homo sapiens
Manually annotated by BRENDA team
Qin, Y.M.; Marttila, M.S.; Haapalainen, A.M.; Siivari, K.M.; Glumoff, T.; Hiltunen, J.K.
Yeast peroxisomal multifunctional enzyme: (3R)-hydroxyacyl-CoA dehydrogenase domains A and B are required for optimal growth on oleic acid
J. Biol. Chem.
274
28619-28625
1999
Candida tropicalis, Homo sapiens, Saccharomyces cerevisiae
Manually annotated by BRENDA team
Weber, S.; Salabei, J.K.; Moeller, G.; Kremmer, E.; Bhatnagar, A.; Adamski, J.; Barski, O.A.
Aldo-keto Reductase 1B15 (AKR1B15): a mitochondrial human aldo-keto reductase with activity toward steroids and 3-keto-acyl-CoA conjugates
J. Biol. Chem.
290
6531-6545
2015
Homo sapiens (C9JRZ8), Homo sapiens
Manually annotated by BRENDA team