4.2.1.150: short-chain-enoyl-CoA hydratase
This is an abbreviated version!
For detailed information about short-chain-enoyl-CoA hydratase, go to the full flat file.
Reaction
Synonyms
3-hydroxyacyl-CoA dehydratase, 3-hydroxybutyryl-CoA dehydratase, CaCRT, CDYL, chromodomain Y-like protein, crotonase, crotonyl-CoA hydratase, crt, L-3-hydroxyacyl-CoA hydro-lyase, More, Mr-Crt, Mrub_2284, Msed_0399
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Substrates Products
Substrates Products on EC 4.2.1.150 - short-chain-enoyl-CoA hydratase
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REACTION DIAGRAM
a short-chain trans-2-enoyl-CoA + H2O
short-chain (3S)-3-hydroxyacyl-CoA
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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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3-hydroxybutyryl-CoA
crotonyl-CoA + H2O
Clostridium acetobutylicum ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787
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r
crotonyl-CoA + H2O
(S)-3-hydroxybutanoyl-CoA
the enzyme is involved in autotrophic carbon fixation
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crotonyl-CoA + H2O
(S)-3-hydroxybutanoyl-CoA
the enzyme is involved in the 3-hydroxypropionate/4-hydroxybutyrate carbon fixation pathway
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crotonyl-CoA + H2O
(S)-3-hydroxybutanoyl-CoA
bifunctional crotonyl-CoA hydratase/(S)-3-hydroxybutanoyl-CoA dehydrogenase (EC 4.2.1.150/EC 1.1.1.35)
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crotonyl-CoA + H2O
(S)-3-hydroxybutanoyl-CoA
the enzyme is involved in the 3-hydroxypropionate/4-hydroxybutyrate carbon fixation pathway
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crotonyl-CoA + H2O
(S)-3-hydroxybutanoyl-CoA
the enzyme is involved in autotrophic carbon fixation
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?
crotonyl-CoA + H2O
(S)-3-hydroxybutanoyl-CoA
bifunctional crotonyl-CoA hydratase/(S)-3-hydroxybutanoyl-CoA dehydrogenase (EC 4.2.1.150/EC 1.1.1.35)
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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 tight 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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Clostridium acetobutylicum ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787
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 tight 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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