4.2.1.55: 3-hydroxybutyryl-CoA dehydratase
This is an abbreviated version!
For detailed information about 3-hydroxybutyryl-CoA dehydratase, go to the full flat file.
Word Map on EC 4.2.1.55
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4.2.1.55
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thiolase
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crotonyl-coa
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r-specific
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beta-hydroxybutyryl-coa
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carboxymethylproline
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trans-2-enoyl-coas
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enoyl-coenzyme
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beta-diketones
- 4.2.1.55
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thiolase
- crotonyl-coa
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r-specific
- beta-hydroxybutyryl-coa
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carboxymethylproline
- trans-2-enoyl-coas
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enoyl-coenzyme
- beta-diketones
Reaction
Synonyms
(R)-specific enoyl-CoA hydratase, CaCRT, CP 24, crotonase, D-3-Hydroxybutyryl coenzyme A dehydratase, D-3-Hydroxybutyryl-CoA dehydratase, Dehydratase, D-3-hydroxybutyryl coenzyme A, ECH 2, Enoyl coenzyme A hydrase (D), enoyl coenzyme A hydratase, enoyl-CoA hydratase 2, Ferp_1035, phaJ
ECTree
4.2.1.55 3-hydroxybutyryl-CoA dehydrataseAdvanced search results
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results (Substrates Products
Substrates Products on EC 4.2.1.55 - 3-hydroxybutyryl-CoA dehydratase
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SUBSTRATE 
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
crotonyl-CoA
?
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enzyme is involved in synthesis of poly-beta-hydroxybutyrate, lipid reserve of bacteria
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?
Crotonyl-[acyl-carrier protein] + H2O
?
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about 50% of the activity with crotonyl-CoA
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-
?
Crotonylpantetheine
?
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about 55% of the activity with crotonyl-CoA
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-
?
trans-2-Hexenoyl-CoA + H2O
?
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about 35% of the activity with crotonyl-CoA
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-
?
crotonoyl-CoA + H2O
(3R)-3-hydroxybutanoyl-CoA
the enzyme is involved in benzoyl-coenzyme A degradation
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-
?
crotonoyl-CoA + H2O
(3R)-3-hydroxybutanoyl-CoA
the enzyme is involved in benzoyl-coenzyme A degradation
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-
?
additional information
?
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enzyme residues Ser69 and Ala24 are signature residues of CaCRT, resulting in a distinct ADP binding mode wherein the ADP moiety of acetoacetyl-CoA is bound at a different position compared with other crotonases. The substrate specificity of crotonase enzymes is determined by both the structural feature of the a3 helix region and the residues contributing the enoyl-CoA binding pocket. A tightly formed a3 helix and two phenylalanine residues, Phe143 and Phe233, aid CaCRT to accommodate crotonyl-CoA as the substrate. Phe143 and Phe233 are key residues for the constitution of the crotonyl binding pocket to accommodate the four-carbon crotonyl-CoA as a substrate
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-
?
additional information
?
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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
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-
?
additional information
?
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no activity with crotonylglutathione, acrylyl-CoA
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-
?
