Information on EC 5.3.3.3 - vinylacetyl-CoA DELTA-isomerase

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

EC NUMBER
COMMENTARY
5.3.3.3
-
RECOMMENDED NAME
GeneOntology No.
vinylacetyl-CoA DELTA-isomerase
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
vinylacetyl-CoA = (E)-but-2-enoyl-CoA
show the reaction diagram
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-
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vinylacetyl-CoA = (E)-but-2-enoyl-CoA
show the reaction diagram
mechanism
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REACTION TYPE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
intramolecular oxidoreduction
-
-
-
-
isomerization
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-
-
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PATHWAY
KEGG Link
MetaCyc Link
Butanoate metabolism
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Carbon fixation pathways in prokaryotes
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Metabolic pathways
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Microbial metabolism in diverse environments
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SYSTEMATIC NAME
IUBMB Comments
vinylacetyl-CoA Delta3-Delta2-isomerase
Also acts on 3-methyl-vinylacetyl-CoA.
SYNONYMS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
cis-3,trans-2-Enoyl-CoA-isomerase
-
-
-
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DELTA3-cis-DELTA2-trans-enoyl-CoA isomerase
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-
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Isomerase, vinylacetyl coenzyme ADELTA-
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Vinylacetyl coenzyme A isomerase
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-
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CAS REGISTRY NUMBER
COMMENTARY
9023-73-8
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ORGANISM
COMMENTARY
LITERATURE
SEQUENCE CODE
SEQUENCE DB
SOURCE
i.e. Cavia porcellus, component of the beta-oxidation enzyme complex
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-
Manually annotated by BRENDA team
strain B; strain fad B64
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-
Manually annotated by BRENDA team
strain B; strain K-12
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Manually annotated by BRENDA team
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
2-butenoyl N-acetylcysteamine
?
show the reaction diagram
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-
-
-
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3-Hexenoyl-CoA
?
show the reaction diagram
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-
-
-
-
Beta-Methylvinylacetyl-CoA
Beta-Methylvinylacetyl-CoA
show the reaction diagram
-
ir
-
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cis-3-Octenoyl-CoA
?
show the reaction diagram
-
-
-
-
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vinylacetyl N-acetylcysteamine
?
show the reaction diagram
-
-
-
-
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Vinylacetyl pantetheine
?
show the reaction diagram
-
-
-
-
-
cis-3-Octenoyl-CoA
?
show the reaction diagram
-
-
-
-
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additional information
?
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not 4-pentenoyl-CoA, beta-methylvinylacetate, beta-vinylacetyl ethyl ester, 5-androstan-3,17-dione, 5-cholestenone, 5-pregnene-3,20-dione
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COFACTOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
FAD
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2 mol per mol of enzyme, bifunctional enzyme possessing 4-hydroxybutyryl-CoA dehydratase and vinylacetyl DELTA-isomerase activity
FAD
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2 mol per mol of enzyme, bifunctional enzyme possessing 4-hydroxybutyryl-CoA dehydratase and vinylacetyl DELTA-isomerase activity
additional information
-
no cofactor
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METALS and IONS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
Fe-S
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0.8 mol Fe and 10.8 mol S per mol of enzyme, iron-sulfur protein, bifunctional enzyme possessing 4-hydroxybutyryl-CoA dehydratase and vinylacetyl DELTA-isomerase activity
Fe-S
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16 mol Fe and 14 mol S per mol of enzyme, iron-sulfur protein, bifunctional enzyme possessing 4-hydroxybutyryl-CoA dehydratase and vinylacetyl DELTA-isomerase activity
additional information
-
not influenced by Na+ or K+
additional information
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no activation by Fe2+, Mn2+, Co2+, Ni2+, Ca2+, Mg2+, Zn2+
INHIBITORS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
3-butynoyl N-acetylcysteamine
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beta-methylcrotonyl-CoA
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N-ethylmaleimide
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p-chloromercuribenzoate
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-
additional information
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not inhibited by iodoacetate
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additional information
-
not inhibited by Fe2+, Mn2+, Co2+, Ni2+, Ca2+, Mg2+, Zn2+
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KM VALUE [mM]
KM VALUE [mM] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.05
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vinylacetyl-CoA
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beta-methylvinylacetyl-CoA
SPECIFIC ACTIVITY [µmol/min/mg]
SPECIFIC ACTIVITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
2.6
-
-
strain K-12YMel, substrate cis-3-octenoyl-CoA
7.5
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strain fad B64, substrate cis-3-octenoyl-CoA
9.8
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substrate cis-3-octenoyl-CoA
32
-
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substrate beta-vinylacetyl-CoA
pH OPTIMUM
pH MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
8
9
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-
SOURCE TISSUE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
MOLECULAR WEIGHT
MOLECULAR WEIGHT MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
232000
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bifunctional enzyme possessing 4-hydroxybutyryl-CoA dehydratase and vinylacetyl DELTA-isomerase activity, gel filtration
237000
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bifunctional enzyme possessing 4-hydroxybutyryl-CoA dehydratase and vinylacetyl DELTA-isomerase activity, gel filtration
240000
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fatty acid oxidation complex consisting of EC 4.2.1.17, EC 1.1.1.35, EC 2.3.1.16, EC 5.1.2.3, EC 5.3.3.3, gel filtration
SUBUNITS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
oligomer
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fatty acid oxidation complex consisting of EC 4.2.1.17, EC 1.1.1.35, EC 2.3.1.16, EC 5.1.2.3, EC 5.3.3.3, SDS-PAGE
tetramer
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4 * 59000, bifunctional enzyme possessing 4-hydroxybutyryl-CoA dehydratase and vinylacetyl DELTA-isomerase activity, SDS-PAGE
tetramer
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4 * 56000, bifunctional enzyme possessing 4-hydroxybutyryl-CoA dehydratase and vinylacetyl DELTA-isomerase activity, SDS-PAGE
OXIDATION STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
oxygen irreversibly inactivates
-
2966
oxygen irreversibly inactivates
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2965
STORAGE STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
frozen or at 5°C, stable for months
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Purification/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
bifunctional enzyme possessing 4-hydroxybutyryl-CoA dehydratase and vinylacetyl DELTA-isomerase activity
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bifunctional enzyme possessing 4-hydroxybutyryl-CoA dehydratase and vinylacetyl DELTA-isomerase activity
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fatty acid oxidation complex consisting of EC 4.2.1.17, EC 1.1.1.35, EC 2.3.1.16, EC 5.1.2.3, EC 5.3.3.3
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fatty acid oxidation complex consisting of EC 4.2.1.17, EC 1.1.1.35, EC 2.3.1.16, EC 5.1.2.3, EC 5.3.3.3
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