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Literature summary for 1.4.1.1 extracted from

  • Forde, J.; Oakey, L.; Jennings, L.; Mulcahy, P.
    Fundamental differences in bioaffinity of amino acid dehydrogenases for N6- and S6-linked immobilized cofactors using kinetic-based enzyme-capture strategies (2005), Anal. Biochem., 338, 102-112.
    View publication on PubMed

Inhibitors

Inhibitors Comment Organism Structure
D-Cys
-
Bacillus subtilis

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.63
-
L-Ala at pH 8.6 Bacillus subtilis
1.96
-
L-Ala at pH 7.4 Bacillus subtilis

Organism

Organism UniProt Comment Textmining
Bacillus subtilis
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
L-Ala + H2O + NAD+
-
Bacillus subtilis pyruvate + NH3 + NADH
-
?

Synonyms

Synonyms Comment Organism
ALADH
-
Bacillus subtilis
NAD+-dependent alanine dehydrogenase
-
Bacillus subtilis

Cofactor

Cofactor Comment Organism Structure
NAD+ affinity for NAD+ immobilized through an N6 linkage, as opposed to an N1 linkage, replacement of the nitrogen with sulfur to produce an S6 linkage Bacillus subtilis

Ki Value [mM]

Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
0.71
-
D-Cys at pH 8.6 Bacillus subtilis
1.88
-
D-Cys at pH 7.4 Bacillus subtilis