Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary 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

Activating Compound

EC Number Activating Compound Comment Organism Structure
1.3.1.9 N-ethylmaleimide stimulation Escherichia coli

Inhibitors

EC Number Inhibitors Comment Organism Structure
1.3.1.9 4-hydroxymercuribenzoate
-
Escherichia coli
1.3.1.9 iodoacetate
-
Escherichia coli
1.3.1.10 N-ethylmaleimide
-
Escherichia coli
1.3.1.10 p-hydroxymercuribenzoate
-
Escherichia coli

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.3.1.9 0.02
-
crotonyl-[acyl-carrier protein]
-
Escherichia coli
1.3.1.9 2.5
-
crotonyl-CoA
-
Escherichia coli

Natural Substrates/ Products (Substrates)

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

Organism

EC Number Organism UniProt Comment Textmining
1.3.1.9 Escherichia coli
-
-
-
1.3.1.10 Escherichia coli
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
1.3.1.9 no separation from NADPH-specific enzyme Escherichia coli
1.3.1.10 no separation from NADH specific enzyme Escherichia coli

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
1.3.1.9 additional information
-
-
Escherichia coli

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.3.1.9 2-hexenoyl-[acyl-carrier protein] + NADH
-
Escherichia coli hexanoyl-[acyl-carrier protein] + NAD+
-
?
1.3.1.9 2-octenoyl-[acyl-carrier protein] + NADH
-
Escherichia coli octanoyl-[acyl-carrier protein] + NAD+
-
?
1.3.1.9 crotonyl-[acyl-carrier protein] + NADH
-
Escherichia coli butyryl-[acyl-carrier protein] + NAD+
-
ir
1.3.1.9 additional information also active on enoyl-CoA substrates Escherichia coli ?
-
?
1.3.1.9 additional information substrate specificity: acyl chain length C4-C16 Escherichia coli ?
-
?
1.3.1.10 2-hexenoyl-[acyl-carrier protein] + NADPH
-
Escherichia coli hexanoyl-[acyl-carrier protein] + NADP+
-
?
1.3.1.10 crotonyl-[acyl-carrier protein] + NADPH
-
Escherichia coli butyryl-[acyl-carrier protein] + NADP+
-
?
1.3.1.10 additional information active on substrates with acyl chain length C4-C16 Escherichia coli ?
-
?
1.3.1.10 additional information inactive with enoyl-CoA substrates Escherichia coli ?
-
?
1.3.1.10 additional information part of fatty acid synthesis reducing double bonds of a great varity of acyl thioesters Escherichia coli ?
-
?

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
1.3.1.9 55
-
5 min stable Escherichia coli
1.3.1.9 60
-
5 min, inactivation Escherichia coli

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
1.3.1.9 7 8
-
Escherichia coli
1.3.1.10 6
-
-
Escherichia coli

pH Range

EC Number pH Minimum pH Maximum Comment Organism
1.3.1.9 6 9
-
Escherichia coli
1.3.1.10 6
-
-
Escherichia coli

pH Stability

EC Number pH Stability pH Stability Maximum Comment Organism
1.3.1.9 7.5
-
relatively stable above Escherichia coli
1.3.1.10 7.6
-
unstable at Escherichia coli

Cofactor

EC Number Cofactor Comment Organism Structure
1.3.1.9 NADH absolute specificity Escherichia coli
1.3.1.10 NADPH
-
Escherichia coli