BRENDA - Enzyme Database
show all sequences of 5.3.3.3

Purification and properties of an iron-sulfur and FAD-containing 4-hydroxybutyryl-CoA dehydratase/vinylacetyl-CoA DELTA3-DELTA2-isomerase from Clostridium aminobutyricum

Scherf, U.; Buckel, W.; Eur. J. Biochem. 215, 421-429 (1993)

Data extracted from this reference:

Inhibitors
Inhibitors
Commentary
Organism
Structure
Cu2+
-
Clostridium aminobutyricum
additional information
not inhibited by Fe2+, Mn2+, Co2+, Ni2+, Ca2+, Mg2+, Zn2+
Clostridium aminobutyricum
Metals/Ions
Metals/Ions
Commentary
Organism
Structure
Fe-S
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
Clostridium aminobutyricum
additional information
no activation by Fe2+, Mn2+, Co2+, Ni2+, Ca2+, Mg2+, Zn2+
Clostridium aminobutyricum
Molecular Weight [Da]
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
56000
-
4 * 56000, bifunctional enzyme possessing 4-hydroxybutyryl-CoA dehydratase and vinylacetyl DELTA-isomerase activity, SDS-PAGE
Clostridium aminobutyricum
232000
-
bifunctional enzyme possessing 4-hydroxybutyryl-CoA dehydratase and vinylacetyl DELTA-isomerase activity, gel filtration
Clostridium aminobutyricum
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Clostridium aminobutyricum
Q03161
-
-
Oxidation Stability
Oxidation Stability
Organism
oxygen irreversibly inactivates
Clostridium aminobutyricum
Purification (Commentary)
Commentary
Organism
bifunctional enzyme possessing 4-hydroxybutyryl-CoA dehydratase and vinylacetyl DELTA-isomerase activity
Clostridium aminobutyricum
Subunits
Subunits
Commentary
Organism
tetramer
4 * 56000, bifunctional enzyme possessing 4-hydroxybutyryl-CoA dehydratase and vinylacetyl DELTA-isomerase activity, SDS-PAGE
Clostridium aminobutyricum
Cofactor
Cofactor
Commentary
Organism
Structure
FAD
2 mol per mol of enzyme, bifunctional enzyme possessing 4-hydroxybutyryl-CoA dehydratase and vinylacetyl DELTA-isomerase activity
Clostridium aminobutyricum
Cofactor (protein specific)
Cofactor
Commentary
Organism
Structure
FAD
2 mol per mol of enzyme, bifunctional enzyme possessing 4-hydroxybutyryl-CoA dehydratase and vinylacetyl DELTA-isomerase activity
Clostridium aminobutyricum
Inhibitors (protein specific)
Inhibitors
Commentary
Organism
Structure
Cu2+
-
Clostridium aminobutyricum
additional information
not inhibited by Fe2+, Mn2+, Co2+, Ni2+, Ca2+, Mg2+, Zn2+
Clostridium aminobutyricum
Metals/Ions (protein specific)
Metals/Ions
Commentary
Organism
Structure
Fe-S
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
Clostridium aminobutyricum
additional information
no activation by Fe2+, Mn2+, Co2+, Ni2+, Ca2+, Mg2+, Zn2+
Clostridium aminobutyricum
Molecular Weight [Da] (protein specific)
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
56000
-
4 * 56000, bifunctional enzyme possessing 4-hydroxybutyryl-CoA dehydratase and vinylacetyl DELTA-isomerase activity, SDS-PAGE
Clostridium aminobutyricum
232000
-
bifunctional enzyme possessing 4-hydroxybutyryl-CoA dehydratase and vinylacetyl DELTA-isomerase activity, gel filtration
Clostridium aminobutyricum
Oxidation Stability (protein specific)
Oxidation Stability
Organism
oxygen irreversibly inactivates
Clostridium aminobutyricum
Purification (Commentary) (protein specific)
Commentary
Organism
bifunctional enzyme possessing 4-hydroxybutyryl-CoA dehydratase and vinylacetyl DELTA-isomerase activity
Clostridium aminobutyricum
Subunits (protein specific)
Subunits
Commentary
Organism
tetramer
4 * 56000, bifunctional enzyme possessing 4-hydroxybutyryl-CoA dehydratase and vinylacetyl DELTA-isomerase activity, SDS-PAGE
Clostridium aminobutyricum
Other publictions for EC 5.3.3.3
No.
1st author
Pub Med
title
organims
journal
volume
pages
year
Activating Compound
Application
Cloned(Commentary)
Crystallization (Commentary)
Engineering
General Stability
Inhibitors
KM Value [mM]
Localization
Metals/Ions
Molecular Weight [Da]
Natural Substrates/ Products (Substrates)
Organic Solvent Stability
Organism
Oxidation Stability
Posttranslational Modification
Purification (Commentary)
Reaction
Renatured (Commentary)
Source Tissue
Specific Activity [micromol/min/mg]
Storage Stability
Substrates and Products (Substrate)
Subunits
Temperature Optimum [C]
Temperature Range [C]
Temperature Stability [C]
Turnover Number [1/s]
pH Optimum
pH Range
pH Stability
Cofactor
Ki Value [mM]
pI Value
IC50 Value
Activating Compound (protein specific)
Application (protein specific)
Cloned(Commentary) (protein specific)
Cofactor (protein specific)
Crystallization (Commentary) (protein specific)
Engineering (protein specific)
General Stability (protein specific)
IC50 Value (protein specific)
Inhibitors (protein specific)
Ki Value [mM] (protein specific)
KM Value [mM] (protein specific)
Localization (protein specific)
Metals/Ions (protein specific)
Molecular Weight [Da] (protein specific)
Natural Substrates/ Products (Substrates) (protein specific)
Organic Solvent Stability (protein specific)
Oxidation Stability (protein specific)
Posttranslational Modification (protein specific)
Purification (Commentary) (protein specific)
Renatured (Commentary) (protein specific)
Source Tissue (protein specific)
Specific Activity [micromol/min/mg] (protein specific)
Storage Stability (protein specific)
Substrates and Products (Substrate) (protein specific)
Subunits (protein specific)
Temperature Optimum [C] (protein specific)
Temperature Range [C] (protein specific)
Temperature Stability [C] (protein specific)
Turnover Number [1/s] (protein specific)
pH Optimum (protein specific)
pH Range (protein specific)
pH Stability (protein specific)
pI Value (protein specific)
Expression
General Information
General Information (protein specific)
Expression (protein specific)
KCat/KM [mM/s]
KCat/KM [mM/s] (protein specific)
2964
Puoilly
The enzymes of beta-oxidation ...
Rhodococcus ruber
Biochem. Soc. Trans.
22
223S
1994
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2965
Scherf
Succinate-ethanol fermentation ...
Clostridium kluyveri
Arch. Microbiol.
161
239-245
1994
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2966
Scherf
Purification and properties of ...
Clostridium aminobutyricum
Eur. J. Biochem.
215
421-429
1993
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2967
Yamamoto
Investigation of peroxisomal l ...
Cavia porcellus
J. Histochem. Cytochem.
40
1909-1918
1992
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2213
Imamura
Purification of the multienzym ...
Pseudomonas fragi
J. Biochem.
107
184-189
1990
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2209
Pramanik
Multienzyme complexes of fatty ...
Escherichia coli, Escherichia coli B / ATCC 11303
Biochim. Biophys. Acta
750
41-46
1983
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177
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2962
Binstock
Fatty acid oxidation complex f ...
Escherichia coli, Escherichia coli B / ATCC 11303
Methods Enzymol.
71
403-411
1981
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177
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2961
Schleicher
On the mechanism and some prop ...
Clostridium kluyveri
Hoppe-Seyler's Z. Physiol. Chem.
357
535-541
1976
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2960
Rilling
The enzymatic isomerization of ...
Bos taurus, Gallus gallus, Pseudomonas sp., Sus scrofa
J. Biol. Chem.
235
3087-3092
1960
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4
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4
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4
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4
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