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Literature summary for 1.1.1.100 extracted from

  • Toomey, R.E.; Wakil, S.J.
    Studies on the mechanism of fatty acid synthesis. XV. Preparation and general properties of beta-ketoacyl acyl carrier protein reductase from Escherichia coli (1966), Biochim. Biophys. Acta, 116, 189-197.
    View publication on PubMed

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
-
-

Purification (Commentary)

Purification (Comment) Organism
-
Escherichia coli

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
4930
-
purified enzyme Escherichia coli

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3-oxoacyl-[acyl-carrier protein] + NADPH pH 6.0-7.0, equilibrium almost completely favors formation of the beta-hydroxyacyl ACP derivatives Escherichia coli (3R)-3-hydroxyacyl-[acyl-carrier protein] + NADP+ product is the D-(-)-stereoisomer ?
acetoacetyl-CoA + NADPH + H+
-
Escherichia coli D-beta-hydroxybutyryl-CoA + NADP+
-
r
acetoacetyl-[acyl-carrier protein] + NADPH
-
Escherichia coli D-beta-hydroxybutyryl-[acyl-carrier protein] + NADP+
-
r
additional information broad specificity for chain length of substrates Escherichia coli ?
-
?

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
6 7
-
Escherichia coli

Cofactor

Cofactor Comment Organism Structure
NADPH absolute specificity for NADPH Escherichia coli