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Literature summary extracted from

  • Madan, V.K.; Hillmer, P.; Gottschalk, G.
    Purification and properties of NADP-dependent L(+)-3-hydroxybutyryl-CoA dehydrogenase from Clostridium kluyveri (1973), Eur. J. Biochem., 32, 51-56.
    View publication on PubMed

Inhibitors

EC Number Inhibitors Comment Organism Structure
1.1.1.157 5,5'-dithiobis(2-nitrobenzoic acid) 0.05 mM, 80% inhibition Clostridium kluyveri
1.1.1.157 iodoacetamide 1 mM, slight inhibition Clostridium kluyveri
1.1.1.157 N-ethylmaleimide 1 mM, slight inhibition Clostridium kluyveri
1.1.1.157 p-chloromercuribenzoate 1 mM, complete inhibition Clostridium kluyveri

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.1.1.157 0.05
-
 3-acetoacetyl-CoA pH 6.5, 25°C Clostridium kluyveri
1.1.1.157 0.07
-
 NADPH pH 6.5, 25°C Clostridium kluyveri

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
1.1.1.157 26000
-
 8 * 26000, SDS-PAGE Clostridium kluyveri
1.1.1.157 215000
-
 gel filtration Clostridium kluyveri
1.1.1.157 220000
-
 equilibrium sedimentation Clostridium kluyveri

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.1.1.157 3-acetoacetyl-CoA + NADPH + H+ Clostridium kluyveri synthesis of butyrate (S)-3-hydroxybutanoyl-CoA + NADP+
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
1.1.1.157 Clostridium kluyveri
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
1.1.1.157
-
 Clostridium kluyveri

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
1.1.1.157 445
-
 reduction of 3-acetoacetyl-CoA, pH 6.5, 25°C Clostridium kluyveri

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.1.1.157 3-acetoacetyl-CoA + NADPH + H+ synthesis of butyrate Clostridium kluyveri (S)-3-hydroxybutanoyl-CoA + NADP+
-
 ?
1.1.1.157 3-acetoacetyl-CoA + NADPH + H+ the oxidation of (S)-3-hydroxybutanoyl-CoA at pH 9.5 proceeds with 7% of the rate of the 3-acetoacetyl-CoA reduction. At pH 6.5, the reduction of 3-acetoacetyl-CoA is 14times faster than the oxidation of (S)-3-hydroxybutanoyl-CoA.The enzyme does not oxidize 3-hydroxyvaleryl-CoA or 3-hydroxycaproyl-CoA Clostridium kluyveri (S)-3-hydroxybutanoyl-CoA + NADP+
-
 r

Subunits

EC Number Subunits Comment Organism
1.1.1.157 octamer 8 * 26000, SDS-PAGE Clostridium kluyveri

Synonyms

EC Number Synonyms Comment Organism
1.1.1.157 L(+)-3-hydroxybutyryl-CoA dehydrogenase
-
 Clostridium kluyveri

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
1.1.1.157 25
-
 assay at Clostridium kluyveri

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
1.1.1.157 6.5
-
 at the pH optimum 6.5 the reduction of 3-acetoacetyl-CoA is 14times faster than the oxidation of (S)-3-hydroxybutanoyl-CoA at its pH optimum 9.5 Clostridium kluyveri
1.1.1.157 9.5
-
 at the pH optimum 6.5 the reduction of 3-acetoacetyl-CoA is 14times faster than the oxidation of (S)-3-hydroxybutanoyl-CoA at its pH optimum 9.5 Clostridium kluyveri

pH Range

EC Number pH Minimum pH Maximum Comment Organism
1.1.1.157 5 7.5 pH 5: about 35% of maximal activity, pH 7.5: about 55% of maximal activity, reduction of 3-acetoacetyl-CoA Clostridium kluyveri

Cofactor

EC Number Cofactor Comment Organism Structure
1.1.1.157 NADP+
-
 Clostridium kluyveri
1.1.1.157 NADPH the rate with NADH is below 0.25% of that with NADPH Clostridium kluyveri