Information on EC 5.1.2.3 - 3-hydroxybutyryl-CoA epimerase

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The expected taxonomic range for this enzyme is: Eukaryota, Bacteria

EC NUMBER
COMMENTARY hide
5.1.2.3
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RECOMMENDED NAME
GeneOntology No.
3-hydroxybutyryl-CoA epimerase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
(S)-3-Hydroxybutanoyl-CoA = (R)-3-hydroxybutanoyl-CoA
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
epimerization
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
Butanoate metabolism
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fatty acid beta-oxidation I
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Fatty acid degradation
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unsaturated, even numbered fatty acid beta-oxidation
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lipid metabolism
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SYSTEMATIC NAME
IUBMB Comments
3-hydroxybutanoyl-CoA 3-epimerase
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CAS REGISTRY NUMBER
COMMENTARY hide
9024-21-9
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
Gram-negative bacteria
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Manually annotated by BRENDA team
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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
D-3-Hydroxy-4-trans-decenoyl-CoA
L3-Hydroxy-4-trans-decenoyl-CoA
show the reaction diagram
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D-3-Hydroxydodecanoyl-CoA
L-3-Hydroxydodecanoyl-CoA
show the reaction diagram
D-3-Hydroxyoctanoly-CoA
L-3-Hydroxyoctanoly-CoA
show the reaction diagram
additional information
?
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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
additional information
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
Tris(hydroxymethyl)aminomethane
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remains active in presence of potassium phosphate
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
52.4
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3-hydroxyacyl-CoA epimerase activity of the trifunctional beta-oxidation protein
additional information
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
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exclusively localized in; glycosomal microbodies
Manually annotated by BRENDA team
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exclusively localized in
Manually annotated by BRENDA team
additional information
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no activity in mitochondria
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Manually annotated by BRENDA team
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
73000
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multienzyme complex which exhibits activities of EC 4.2.1.17, EC 2.3.1.16, EC 5.1.2.3, EC 1.1.1.35, and EC 5.3.3.3, 2 * 42000 + 2 * 73000, SDS-PAGE
78000
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multienzyme complex which exhibits activities of EC 4.2.1.17, EC 2.3.1.16, EC 5.1.2.3, and EC 5.3.3.3, 2 * 42000 + 2 * 78000, SDS-PAGE
79047
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multifunctional enzyme which exhibits activities of EC 4.2.1.17, EC 1.1.1.211, EC 5.3.3.8 and EC 5.1.2.3, 1 * 79047, calculation from nucleotide sequence, monomeric protein exhibiting all 4 activities
365000
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trifunctional beta-oxidation protein with activities of EC 1.1.1.35, EC 4.2.1.17 and EC 5.1.2.3, gel filtration
additional information
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
tetramer
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4 * 93000, trifunctional beta-oxidation protein with activities of EC 1.1.1.35, EC 4.2.1.17 and EC 5.1.2.3, SDS-PAGE
additional information
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
lipoprotein
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
multienzyme complex which exhibits activities of EC 4.2.1.17, EC 2.3.1.16, EC 5.1.2.3, and EC 5.3.3.3, is stable for months when stored in 0.2 M potassium phosphate, pH 6.6, containing 25% v/v glycerol and 10 mM mercaptoethanol
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
multienzyme complex which exhibits activities of EC 4.2.1.17, EC 2.3.1.16, EC 5.1.2.3, EC 1.1.1.35, and EC 5.3.3.3
multifunctional enzyme which exhibits activities of EC 4.2.1.17, EC 1.1.1.211, EC 5.3.3.8 and EC 5.1.2.3
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multifunctional enzyme with domain structure. Isolation of fragments containing single enzyme activities provide evidence for hinge regions
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trifunctional beta-oxidation protein with activities of EC 1.1.1.35, EC 4.2.1.17 and EC 5.1.2.3; trifunctional enzyme possessing activities of EC 5.1.2.3, EC 1.1.1.35, and EC 4.2.1.17
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli, multifunctional enzyme which exhibits activities of EC 4.2.1.17, EC 1.1.1.211, EC 5.3.3.8 and EC 5.1.2.3
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
G116F
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both the enoyl-CoA hydratase activity, EC 4.2.1.17 and the 3-hydroxyacyl-CoA epimerase activity, EC 5.1.2.3 are eliminated by the site-directed mutation alpha/Gly116 to Phe. This provides direct evidence that both enzymes are associated with a common active site on the amino-terminal domain of the multifunctional enzyme complex which exhibits the activities of EC 4.2.1.17, EC 2.3.1.16, EC 5.1.2.3, EC 1.1.1.35, and EC 5.3.3.3
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