Information on EC 4.2.1.120 - 4-hydroxybutanoyl-CoA dehydratase

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

EC NUMBER
COMMENTARY hide
4.2.1.120
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RECOMMENDED NAME
GeneOntology No.
4-hydroxybutanoyl-CoA dehydratase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
4-hydroxybutanoyl-CoA = (E)-but-2-enoyl-CoA + H2O
show the reaction diagram
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
3-hydroxypropanoate/4-hydroxybutanate cycle
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4-aminobutanoate degradation V
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Butanoate metabolism
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Carbon fixation pathways in prokaryotes
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crotonyl-CoA/ethylmalonyl-CoA/hydroxybutyryl-CoA cycle (engineered)
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Metabolic pathways
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Microbial metabolism in diverse environments
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succinate fermentation to butanoate
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CO2 fixation in Crenarchaeota
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SYSTEMATIC NAME
IUBMB Comments
4-hydroxybutanoyl-CoA hydro-lyase
Contains FAD and a [4Fe-4S] iron-sulfur cluster. The enzyme has been characterized from several microorganisms, including Clostridium kluyveri, where it participates in succinate fermentation [1,2], Clostridium aminobutyricum, where it participates in 4-aminobutyrate degradation [3,4], and Metallosphaera sedula, where it participates in the 3-hydroxypropionate/4-hydroxybutyrate cycle, an autotrophic CO2 fixation pathway found in some thermoacidophilic archaea [5].
CAS REGISTRY NUMBER
COMMENTARY hide
129430-44-0
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
4-hydroxybutanoyl-CoA
(E)-but-2-enoyl-CoA + H2O
show the reaction diagram
4-hydroxybutanoyl-CoA
but-3-enoyl-CoA + H2O
show the reaction diagram
4-hydroxybutanoyl-CoA
crotonyl-CoA + H2O
show the reaction diagram
4-hydroxybutanoyl-CoA
vinylacetyl-CoA + H2O
show the reaction diagram
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-
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r
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
4-hydroxybutanoyl-CoA
(E)-but-2-enoyl-CoA + H2O
show the reaction diagram
4-hydroxybutanoyl-CoA
but-3-enoyl-CoA + H2O
show the reaction diagram
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-
-
-
?
4-hydroxybutanoyl-CoA
crotonyl-CoA + H2O
show the reaction diagram
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
4Fe-4S-center
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
Dithionite
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inactivation, oxidation with potassium hexacyanoferrate(III) results in up to 84% reactivation
additional information
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enzyme is not inactivated by 5 mM 4-nitrophenol, 5 mM chloramphenicol, and 5 mM hydroxylamine
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
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enzyme does not require ATP, MgCl2, and Ti(III)citrate
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.05 - 0.15
4-hydroxybutanoyl-CoA
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2.1
4-hydroxybutanoyl-CoA
Metallosphaera sedula
A4YGC7
pH 8.0, 70°C
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
14
4-hydroxybutanoyl-CoA
Metallosphaera sedula
A4YGC7
pH 8.0, 70°C
8018
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.1
40°C, pH and temperature not specified in the publication
12.5
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pH 9.0, 25°C
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
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enzyme is largely membrane- or particle-bound and may be solubilized by detergent
Manually annotated by BRENDA team
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high enzymic activity in anaerobically grown cell extract grown on succinate plus ethanol
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Manually annotated by BRENDA team
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
56000
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4 * 56000, SDS-PAGE
59000
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4 * 59000, SDS-PAGE
232000
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gel filtration
237000
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gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
tetramer
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
to 1.6 A resolution. A [4Fe-4S]2+ cluster, coordinated by three cysteine and one histidine residues, is located 7 A from the Re-side of a flavin adenine dinucleotide moiety. The substrate can be bound between the [4Fe-4S]2+ cluster and the FAD with both cofactors contributing to its radical activation and catalytic conversio
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
stable under anaerobic conditions
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OXIDATION STABILITY
ORGANISM
UNIPROT
LITERATURE
exposure to air leads to irreversible inactivation
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2965
exposure to air results in initial activation followed by irreversible inactivation
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2966
inactivation by oxygen
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698004
upon exposure to air at 0°C, complete loss of dehydration activity within 40 min
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696186
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
purification under strictly anaerobic conditions
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using anaerobic conditions
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
recombinantly expressed in Escherichia coli
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
approximately 10fold downregulated in presence of acetate, 4-hydroxybutyrate, succinate or pyruvate
Renatured/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
enzyme is inactivated by dithionite, oxidation with potassium hexacyanoferrate(III) results in up to 84% reactivation
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