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Literature summary for 1.3.1.102 extracted from

  • Dick, R.A.; Kensler, T.W.
    The catalytic and kinetic mechanisms of NADPH-dependent alkenal/one oxidoreductase (2004), J. Biol. Chem., 279, 17269-17277.
    View publication on PubMed

Inhibitors

Inhibitors Comment Organism Structure
2-nonanone competitive inhibition versus 3-nonen-2-one and noncompetitive inhibition versus NADPH Rattus norvegicus
NADP+ competitive inhibition versus NADPH and noncompetitive inhibition versus 3-nonen-2-one Rattus norvegicus
NADPH uncompetitive inhibition Rattus norvegicus
Zn2+ the addition of 0.25 mM Zn2+ inhibits enzyme activity more than 2fold Rattus norvegicus

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.004
-
NADPH with trans-2-nonenal as cosubstrate, in 100 mM Tris (pH 7.2), at 25°C Rattus norvegicus
0.0282
-
trans-3-nonen-2-one with trans-3-nonen-2-one as cosubstrate, in 100 mM Tris (pH 7.2), at 25°C Rattus norvegicus
0.032
-
NADPH with trans-3-nonen-2-one as cosubstrate, in 100 mM Tris (pH 7.2), at 25°C Rattus norvegicus
0.0776
-
trans-2-nonenal with trans-3-nonen-2-one as cosubstrate, in 100 mM Tris (pH 7.2), at 25°C Rattus norvegicus

Organism

Organism UniProt Comment Textmining
Rattus norvegicus
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
trans-2-nonenal + NADPH + H+
-
Rattus norvegicus nonanal + NADP+
-
?
trans-3-nonen-2-one + NADPH + H+
-
Rattus norvegicus nonan-2-one + NADP+
-
?

Synonyms

Synonyms Comment Organism
AOR
-
Rattus norvegicus
NADPH-dependent alkenal/one oxidoreductase
-
Rattus norvegicus

Cofactor

Cofactor Comment Organism Structure
NADPH nearly 20fold preference for NADPH over NADH Rattus norvegicus