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Literature summary for 1.3.1.10 extracted from

  • Weeks, G.; Wakil, S.J.
    Studies on the mechanism of fatty acid synthesis. 18. Preparation and general properties of the enoyl acyl carrier protein reductases from Escherichia coli (1968), J. Biol. Chem., 243, 1180-1189.
    View publication on PubMed
Search for more literature for 1.3.1.10

Inhibitors

Inhibitors Comment Organism Structure
N-ethylmaleimide
-
 Escherichia coli
p-hydroxymercuribenzoate
-
 Escherichia coli

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
additional information Escherichia coli part of fatty acid synthesis reducing double bonds of a great varity of acyl thioesters ?
-
 ?

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
-
-

Purification (Commentary)

Purification (Comment) Organism
no separation from NADH specific enzyme Escherichia coli

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2-hexenoyl-[acyl-carrier protein] + NADPH
-
 Escherichia coli hexanoyl-[acyl-carrier protein] + NADP+
-
 ?
crotonyl-[acyl-carrier protein] + NADPH
-
 Escherichia coli butyryl-[acyl-carrier protein] + NADP+
-
 ?
additional information active on substrates with acyl chain length C4-C16 Escherichia coli ?
-
 ?
additional information inactive with enoyl-CoA substrates Escherichia coli ?
-
 ?
additional information part of fatty acid synthesis reducing double bonds of a great varity of acyl thioesters Escherichia coli ?
-
 ?

pH Optimum

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

pH Range

pH Minimum pH Maximum Comment Organism
6
-
-
 Escherichia coli

pH Stability

pH Stability pH Stability Maximum Comment Organism
7.6
-
 unstable at Escherichia coli

Cofactor

Cofactor Comment Organism Structure
NADPH
-
 Escherichia coli