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Literature summary for 1.3.1.31 extracted from

  • Tischer, W.; Bader, J.; Simon, H.
    Purification and some properties of a hitherto-unknown enzyme reducing the carbon-carbon double bond of alpha, beta-unsaturated carboxylate anions (1979), Eur. J. Biochem., 97, 103-112.
    View publication on PubMed
Search for more literature for 1.3.1.31

Inhibitors

Inhibitors Comment Organism Structure
Mersalyl 1 mM, complete inhibition Clostridium sp.
O2 in the reduced state the enzyme is inactivated in 1-2 min, about 3 h after the removal of oxygen, the activity is partially restored Clostridium sp.
p-hydroxymercuribenzoate 0.1 mM, complete inhibition Clostridium sp.

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
 additional information
-
 Clostridium kluyveri
additional information
-
 additional information Km-value for NADH is lower than 0.02 mM Clostridium sp.
0.02
-
 cinnamate
-
 Clostridium sp.
0.8
-
 (E)-2-butenoate
-
 Clostridium sp.
1.67
-
 (E)-2-methyl-2-butenoate
-
 Clostridium sp.

Metals/Ions

Metals/Ions Comment Organism Structure
Fe iron-sulfur protein, contains 3.5-3.8 atoms of iron and 4.0 atoms of labile sulfur per subunit Clostridium sp.

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
78000
-
 6 * 78000, SDS-PAGE Clostridium sp.
450000
-
 gel filtration Clostridium sp.

Organism

Organism UniProt Comment Textmining
Clostridium kluyveri
-
-
-
Clostridium sp.
-
-
-

Purification (Commentary)

Purification (Comment) Organism
-
 Clostridium sp.

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
6.9
-
-
 Clostridium sp.

Storage Stability

Storage Stability Organism
-20°C, phosphate buffer, pH 7.0, containing (E)-2-methyl-2-butenoate, EDTA, sucrose and 2-mercaptoethanol, repeatedly thawed and frozen, 50% loss of activity Clostridium sp.

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
(E)-2-butenoate + NADH
-
 Clostridium kluyveri butanoate + NAD+
-
 ?
(E)-2-butenoate + NADH
-
 Clostridium sp. butanoate + NAD+
-
 ?
(E)-2-methyl-2-butenoate + NADH
-
 Clostridium kluyveri 2-methylbutanoate + NAD+
-
 ?
(E)-2-methyl-2-butenoate + NADH
-
 Clostridium sp. 2-methylbutanoate + NAD+
-
 ?
(E)-3-methylpentenoate + NADH
-
 Clostridium kluyveri 3-methylpentanoate + NAD+
-
 ?
(E)-3-methylpentenoate + NADH
-
 Clostridium sp. 3-methylpentanoate + NAD+
-
 ?
(E)-cinnamate + NADH
-
 Clostridium kluyveri phenylpropionate + NAD+
-
 ?
(E)-cinnamate + NADH
-
 Clostridium sp. phenylpropionate + NAD+
-
 ?
(Z)-3-methylpentenoate + NADH
-
 Clostridium kluyveri 3-methylpentanoate + NAD+
-
 ?
(Z)-3-methylpentenoate + NADH
-
 Clostridium sp. 3-methylpentanoate + NAD+
-
 ?
butenoate + NADH
-
 Clostridium kluyveri butanoate + NAD+
-
 ?
butenoate + NADH reverse reaction is energetically extremely unfavorable Clostridium sp. butanoate + NAD+
-
 ?
cinnamate + NADH
-
 Clostridium sp. phenylpropionate + NAD+
-
 ?

Subunits

Subunits Comment Organism
hexamer 6 * 78000, SDS-PAGE Clostridium sp.

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
55
-
 20 min, stable Clostridium sp.

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
6
-
-
 Clostridium sp.

Cofactor

Cofactor Comment Organism Structure
FAD enzyme contains 1 mol of FAD per mol of subunit Clostridium sp.
NADH
-
 Clostridium kluyveri
NADH
-
 Clostridium sp.