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Literature summary for 1.1.1.36 extracted from

  • Packter, N.M.; Flatman, S.
    Characterization of acetoacetyl-CoA reductase (3-oxoreductase) from Streptomyces coelicolor: Its possible role in polyhydroxybutyrate biosynthesis (1973), Biochem. Soc. Trans., 11, 598-599.
No PubMed abstract available
Search for more literature for 1.1.1.36

Inhibitors

Inhibitors Comment Organism Structure
additional information not inhibited by acetoacetyl-CoA at high concentrations Streptomyces coelicolor

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.008
-
 S-acetoacetyl-N-acetylcysteamine cofactor NADH Streptomyces coelicolor
0.01
-
 acetoacetyl-CoA cofactor NADPH Streptomyces coelicolor
0.018
-
 acetoacetyl-CoA cofactor NADH Streptomyces coelicolor

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
55000
-
 2 * 55000 + 2 * 65000, SDS-PAGE Streptomyces coelicolor
65000
-
 2 * 55000 + 2 * 65000, SDS-PAGE Streptomyces coelicolor
250000
-
 gel filtration Streptomyces coelicolor

Organism

Organism UniProt Comment Textmining
Streptomyces coelicolor
-
-
-

Purification (Commentary)

Purification (Comment) Organism
gel-filtration Sephadex G-200, DEAE-cellulose chromatography, sucrose-gradient centrifugation Streptomyces coelicolor

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
acetoacetyl-CoA + NADPH + H+
-
 Streptomyces coelicolor (3R)-3-hydroxybutyryl-CoA + NADP+
-
 r
additional information not: crotonyl-CoA Streptomyces coelicolor ?
-
 ?
S-acetoacetyl-N-acetylcysteamine + NADPH
-
 Streptomyces coelicolor 3-hydroxybutyryl-N-acetylcysteamine + NADP+
-
 ?

Subunits

Subunits Comment Organism
tetramer 2 * 55000 + 2 * 65000, SDS-PAGE Streptomyces coelicolor

Cofactor

Cofactor Comment Organism Structure
NADH
-
 Streptomyces coelicolor
NADPH
-
 Streptomyces coelicolor