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Literature summary for 1.3.1.31 extracted from

  • Verhaert, R.M.D.; Tyrakowska, B.; Hilhorst, R.; Schaafsma, T.J.; Veeger, C.
    Enzyme kinetics in reversed micelles. 2. Behaviour of enoate reductase (1990), Eur. J. Biochem., 187, 73-79.
    View publication on PubMed
Search for more literature for 1.3.1.31

Inhibitors

Inhibitors Comment Organism Structure
2-methylbutenoate in all reversed micellar solutions inhibition by the enoate is observed at an overall concentration of 0.5-5 mM, implying that a concentration of substrate equal to the Km value in aqueous solution may already cause inhibition in reversed micelles Clostridium sp.

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.02
-
 NADH in 50 mM HEPES, pH 7.0, ionic strength 0.05 M Clostridium sp.
6
-
 2-methylbutenoate in 50 mM HEPES, pH 7.0, ionic strength 0.05 M Clostridium sp.

Organism

Organism UniProt Comment Textmining
Clostridium sp.
-
-
-

Reaction

Reaction Comment Organism Reaction ID
butanoate + NAD+ = but-2-enoate + NADH + H+ ping-pong mechanism in aqueous solution Clostridium sp.
a
butanoate + NAD+ = but-2-enoate + NADH + H+ enzyme kinetics in reversed micelles Clostridium sp.
a

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2-methylbutenoate + NADH
-
 Clostridium sp. 2-methylbutanoate + NAD+
-
 ?
butenoate + NADH
-
 Clostridium sp. butanoate + NAD+
-
 ?

Cofactor

Cofactor Comment Organism Structure
NADH
-
 Clostridium sp.