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
-
-
-
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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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-
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DELTA3-cis-DELTA2-trans-enoyl-CoA isomerase
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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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-
-
-
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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
-
-
-
-
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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
-
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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-
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
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2966
oxygen irreversibly inactivates
-
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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