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Literature summary for 1.1.1.157 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

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

KM Value [mM]

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

Molecular Weight [Da]

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

Natural Substrates/ Products (Substrates)

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

Organism

Organism UniProt Comment Textmining
Clostridium kluyveri
-
-
-

Purification (Commentary)

Purification (Comment) Organism
-
Clostridium kluyveri

Specific Activity [micromol/min/mg]

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

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3-acetoacetyl-CoA + NADPH + H+ synthesis of butyrate Clostridium kluyveri (S)-3-hydroxybutanoyl-CoA + NADP+
-
?
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

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

Synonyms

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

Temperature Optimum [°C]

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

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
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
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

pH Minimum pH Maximum Comment Organism
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

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