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

BRENDA support

Literature summary extracted from

  • Lodwig, E.; Kumar, S.; Allaway, D.; Bourdes, A.; Prell, J.; Priefer, U.; Poole, P.
    Regulation of L-alanine dehydrogenase in Rhizobium leguminosarum bv. viciae and its role in pea nodules (2004), J. Bacteriol., 186, 842-849.
    View publication on PubMedView publication on EuropePMC

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.4.1.1 additional information Rhizobium leguminosarum the enzyme is induced by carboxylic acids (succinate, malate and pyruvate), although the best induer is alanine. The role of the enzyme may be to balance the alanine level for optimal functioning of bacteroid metabolism rather than to synthesize alanine as the sole product of N2 reduction ?
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
1.4.1.1 Rhizobium leguminosarum Q9RLB2 bv. viciae
-
1.4.1.1 Rhizobium leguminosarum Q9RLB3 bv. viciae
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.4.1.1 additional information the enzyme is induced by carboxylic acids (succinate, malate and pyruvate), although the best induer is alanine. The role of the enzyme may be to balance the alanine level for optimal functioning of bacteroid metabolism rather than to synthesize alanine as the sole product of N2 reduction Rhizobium leguminosarum ?
-
 ?
1.4.1.1 pyruvate + NH3 + NADH
-
 Rhizobium leguminosarum L-Ala + H2O + NAD+
-
 ?

Synonyms

EC Number Synonyms Comment Organism
1.4.1.1 AldA
-
 Rhizobium leguminosarum

Cofactor

EC Number Cofactor Comment Organism Structure
1.4.1.1 NAD+
-
 Rhizobium leguminosarum