Information on EC 4.2.1.55 - 3-Hydroxybutyryl-CoA dehydratase

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

EC NUMBER
COMMENTARY
4.2.1.55
-
RECOMMENDED NAME
GeneOntology No.
3-Hydroxybutyryl-CoA dehydratase
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
(3R)-3-hydroxybutanoyl-CoA = crotonoyl-CoA + H2O
show the reaction diagram
-
-
-
-
(3R)-3-hydroxybutanoyl-CoA = crotonoyl-CoA + H2O
show the reaction diagram
stereochemistry
-
REACTION TYPE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
addition
-
-
-
-
elimination
-
-
-
-
PATHWAY
KEGG Link
MetaCyc Link
acetyl-CoA fermentation to butyrate II
-
Butanoate metabolism
-
Carbon fixation pathways in prokaryotes
-
ethylmalonyl pathway
-
Glyoxylate and dicarboxylate metabolism
-
Microbial metabolism in diverse environments
-
SYSTEMATIC NAME
IUBMB Comments
(3R)-3-hydroxybutanoyl-CoA hydro-lyase (crotonoyl-CoA-forming)
Also acts on crotonoyl thioesters of pantetheine and acyl-carrier protein.
SYNONYMS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
CP 24
-
-
-
-
crotonase
-
-
-
-
D-3-Hydroxybutyryl coenzyme A dehydratase
-
-
-
-
D-3-Hydroxybutyryl-CoA dehydratase
-
-
-
-
Dehydratase, D-3-hydroxybutyryl coenzyme A
-
-
-
-
Enoyl coenzyme A hydrase (D)
-
-
-
-
enoyl-CoA hydratase 2
-
-
CAS REGISTRY NUMBER
COMMENTARY
37290-82-7
-
ORGANISM
COMMENTARY
LITERATURE
SEQUENCE CODE
SEQUENCE DB
SOURCE
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
(3R)-3-Hydroxybutanoyl-CoA
Crotonyl-CoA + H2O
show the reaction diagram
-
-
-
-
crotonyl-CoA
?
show the reaction diagram
-
enzyme is involved in synthesis of poly-beta-hydroxybutyrate, lipid reserve of bacteria
-
-
-
Crotonyl-CoA + H2O
(3R)-3-Hydroxybutanoyl-CoA
show the reaction diagram
-
-
-
-
Crotonyl-[acyl-carrier protein] + H2O
?
show the reaction diagram
-
about 50% of the activity with crotonyl-CoA
-
-
-
trans-2-Hexenoyl-CoA + H2O
?
show the reaction diagram
-
about 35% of the activity with crotonyl-CoA
-
-
-
Crotonylpantetheine
?
show the reaction diagram
-
about 55% of the activity with crotonyl-CoA
-
-
-
additional information
?
-
-
no activity with crotonylglutathione, acrylyl-CoA
-
-
-
additional information
?
-
-
2-enoyl-CoA hydratase 2 is the middle part of the mammalian multifunctional protein-2, MFP-2, which catalyzes the (R)-specific hydration of 2-enoyl-CoA thioesters
-
-
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
crotonyl-CoA
?
show the reaction diagram
-
enzyme is involved in synthesis of poly-beta-hydroxybutyrate, lipid reserve of bacteria
-
-
-
additional information
?
-
-
2-enoyl-CoA hydratase 2 is the middle part of the mammalian multifunctional protein-2, MFP-2, which catalyzes the (R)-specific hydration of 2-enoyl-CoA thioesters
-
-
-
INHIBITORS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
iodoacetamide
-
0.01 M, 30% inhibition
iodoacetic acid
-
0.01 M, 12% inhibition
N-ethylmaleimide
-
0.01 M, 23% inhibition
oct-2-yn-4-enoyl-CoA
-
a multifunctional irreversible enzyme inhibitor in fatty acid oxidation mainly targeting mitochondrial trifunctional protein beta-subunit, alsoirreversibly inactivates enoyl-CoA hydratase 2, mechanism for inactivation, overview
p-Substituted mercuribenzoate
-
3 mM, 65% inhibition
KM VALUE [mM]
KM VALUE [mM] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.00926
-
crotonyl-CoA
-
-
0.08
-
crotonyl-[acyl-carrier protein]
-
-
0.118
-
Crotonylpantetheine
-
-
0.0263
-
trans-2-Hexenoyl-CoA
-
-
Ki VALUE [mM]
Ki VALUE [mM] Maximum
INHIBITOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.025
-
oct-2-yn-4-enoyl-CoA
-
ECH 2
SPECIFIC ACTIVITY [µmol/min/mg]
SPECIFIC ACTIVITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
additional information
-
-
-
pH OPTIMUM
pH MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
PDB
SCOP
CATH
ORGANISM
Rhodopseudomonas palustris (strain ATCC BAA-98 / CGA009)
SUBUNITS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
hexamer
-
2-enoyl-CoA hydratase 2 is the middle part of the MFP-2, the enzyme is a homodimer, unlike the mitochondrial 2-enoyl-CoA hydratase 1 that is a hexamer
homodimer
-
2-enoyl-CoA hydratase 2 is the middle part of the MFP-2, the enzyme is a homodimer, unlike the mitochondrial 2-enoyl-CoA hydratase 1 that is a hexamer
Purification/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE