Information on EC 4.2.1.150 - short-chain-enoyl-CoA hydratase

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

EC NUMBER
COMMENTARY hide
4.2.1.150
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RECOMMENDED NAME
GeneOntology No.
short-chain-enoyl-CoA hydratase
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
a short-chain (3S)-3-hydroxyacyl-CoA = a short-chain trans-2-enoyl-CoA + H2O
show the reaction diagram
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
3-hydroxypropanoate/4-hydroxybutanate cycle
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crotonate fermentation (to acetate and cyclohexane carboxylate)
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gallate degradation III (anaerobic)
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glutaryl-CoA degradation
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L-glutamate degradation V (via hydroxyglutarate)
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pyruvate fermentation to butanoate
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pyruvate fermentation to butanol I
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pyruvate fermentation to butanol II (engineered)
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pyruvate fermentation to hexanol (engineered)
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CO2 fixation in Crenarchaeota
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tryptophan metabolism
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SYSTEMATIC NAME
IUBMB Comments
short-chain-(3S)-3-hydroxyacyl-CoA hydro-lyase
The enzyme from the bacterium Clostridium acetobutylicum is part of the central fermentation pathway and plays a key role in the production of both acids and solvents. It is specific for short, C4-C6, chain length substrates and exhibits an extremely high turnover number for crotonyl-CoA. cf. EC 4.2.1.17, enoyl-CoA hydratase and EC 4.2.1.74, long-chain-enoyl-CoA hydratase.
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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
3-hydroxybutyryl-CoA
crotonyl-CoA + H2O
show the reaction diagram
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?
a short-chain trans-2-enoyl-CoA + H2O
short-chain (3S)-3-hydroxyacyl-CoA
show the reaction diagram
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the enzyme is specific for short chain fatty acyl-CoA substrates and is sensitive to high concentrations of crotonyl-CoA. It requires a complete coenzyme A thioester substrate for efficient catalysis
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?
crotonyl-CoA + H2O
(S)-3-hydroxybutanoyl-CoA
show the reaction diagram
crotonyl-CoA + H2O
3-hydroxybutyryl-CoA
show the reaction diagram
crotonyl-CoA + H2O
?
show the reaction diagram
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?
hexenoyl-CoA + H2O
?
show the reaction diagram
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
3-hydroxybutyryl-CoA
crotonyl-CoA + H2O
show the reaction diagram
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?
crotonyl-CoA + H2O
(S)-3-hydroxybutanoyl-CoA
show the reaction diagram
crotonyl-CoA + H2O
3-hydroxybutyryl-CoA
show the reaction diagram
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?
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
crotonyl-CoA
additional information
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not inhibited by hexenoyl-CoA
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.03 - 0.3
crotonyl-CoA
0.13
hexenoyl-CoA
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
19
crotonyl-CoA
Metallosphaera sedula
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pH 8.0, 70°C
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
260
crotonyl-CoA
Metallosphaera sedula
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pH 8.0, 70°C
406
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
3 - 8
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pH 8.0, 65°C, native enzyme, autotrophically- or heterotrophically-grown cell
6155
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25°C, pH 7.5
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
28200
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x * 28200, calculated from amino acid sequence
29000
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x * 29000, SDS-PAGE
40000
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4 * 40000, SDS-PAGE
43000
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4 * 43000, SDS-PAGE
70000
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x * 70000, SDS-PAGE
158000
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
homotetramer
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4 * 40000, SDS-PAGE
tetramer
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4 * 43000, SDS-PAGE
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
lyophilization results in negligible loss of enzymatic activity
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
4 or -20°C, Tris-HCl, pH 8.0, rapid loss of activity
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
acetone precipitation, Sephadex G-200 gel filtration, and DEAE-Sephadex column chromatography
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli XL1-Blue cells
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expression in Escherichia coli
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recombinantly expressed in Escherichia coli
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