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Literature summary for 4.2.1.17 extracted from

  • Wu, W.J.; Feng, Y.; He, X.; Hofstein, H.A.; Raleigh, D.P.; Tonge, P.J.
    Stereospecificity of the reaction catalyzed by enoyl-CoA hydratase (2000), J. Am. Chem. Soc., 122, 3987-3994.
No PubMed abstract available

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.05
-
crotonyl-CoA
-
Rattus norvegicus
0.05
-
(Z)-2-butenoyl-CoA pH 7.4, 25°C Rattus norvegicus

Localization

Localization Comment Organism GeneOntology No. Textmining
mitochondrion
-
Rattus norvegicus 5739
-

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
(Z)-2-butenoyl-CoA + H2O Rattus norvegicus kcat is 12fold slower than with the trans-iosmer crotonyl-CoA (3R)-3-hydroxybutanoyl-CoA
-
?
crotonyl-CoA + H2O Rattus norvegicus i.e. (E)-2-butenoyl-CoA. The reaction proceeds via the syn addition of water and thus the pro-2R proton of (3S)-hydroxybutyryl-CoA is derived from solvent. The equilibrium constant for the hydration of trans-2-crotonyl-CoA to (3S)-hydroxybutyryl-CoA is 7.5. The rate of 3(R)-hydroxybutyryl-CoA formation is 400000fold slower than the normal hydration reaction (of crotonyl-CoA to (3S)-3-hydroxybutanoyl-CoA) but at least 1600000fold faster than the non-enzyme-catalyzed reaction. Formation of the incorrect stereoisomer likely occurs via syn addition of water to the incorrect face of the trans-2-crotonyl-CoA double bond. The absolute stereospecificity for the enzyme-catalyzed reaction is 1 in 400000. To account for the exchange of the hydroxybutyryl pro-2S proton, the enzyme must also catalyze the dehydration of 3(R)-hydroxybutyryl-CoA to cis-2-crotonyl-CoA. Thus, the enzyme is capable of catalyzing the epimerization of hydroxybutyryl-CoA (3S)-3-hydroxybutanoyl-CoA
-
r

Organism

Organism UniProt Comment Textmining
Rattus norvegicus
-
recombinant enzyme
-

Purification (Commentary)

Purification (Comment) Organism
recombinant Rattus norvegicus

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
(Z)-2-butenoyl-CoA + H2O kcat is 12fold slower than with the trans-iosmer crotonyl-CoA Rattus norvegicus (3R)-3-hydroxybutanoyl-CoA
-
?
crotonyl-CoA + H2O i.e. (E)-2-butenoyl-CoA. The reaction proceeds via the syn addition of water and thus the pro-2R proton of (3S)-hydroxybutyryl-CoA is derived from solvent. The equilibrium constant for the hydration of trans-2-crotonyl-CoA to (3S)-hydroxybutyryl-CoA is 7.5. The rate of 3(R)-hydroxybutyryl-CoA formation is 400000fold slower than the normal hydration reaction (of crotonyl-CoA to (3S)-3-hydroxybutanoyl-CoA) but at least 1600000fold faster than the non-enzyme-catalyzed reaction. Formation of the incorrect stereoisomer likely occurs via syn addition of water to the incorrect face of the trans-2-crotonyl-CoA double bond. The absolute stereospecificity for the enzyme-catalyzed reaction is 1 in 400000. To account for the exchange of the hydroxybutyryl pro-2S proton, the enzyme must also catalyze the dehydration of 3(R)-hydroxybutyryl-CoA to cis-2-crotonyl-CoA. Thus, the enzyme is capable of catalyzing the epimerization of hydroxybutyryl-CoA Rattus norvegicus (3S)-3-hydroxybutanoyl-CoA
-
r
crotonyl-CoA + H2O i.e. (E)-2-butenoyl-CoA. The reaction proceeds via the syn addition of water and thus the pro-2R proton of (3S)-hydroxybutyryl-CoA is derived from solvent. The equilibrium constant for the hydration of trans-2-crotonyl-CoA to (3S)-hydroxybutyryl-CoA is 7.5. The rate of 3(R)-hydroxybutyryl-CoA formation is 400000fold slower than the normal hydration reaction (of crotonyl-CoA to (3S)-3-hydroxybutanoyl-CoA) but at least 1600000fold faster than the non-enzyme-catalyzed reaction. Formation of the incorrect stereoisomer likely occurs via syn addition of water to the incorrect face of the trans-2-crotonyl-CoA double bond. The absolute stereospecificity for the enzyme-catalyzed reaction is 1 in 400000 Rattus norvegicus (3S)-3-hydroxybutanoyl-CoA
-
r

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
152
-
(Z)-2-butenoyl-CoA pH 7.4, 25°C Rattus norvegicus
1790
-
crotonyl-CoA
-
Rattus norvegicus