Literature summary for 1.4.1.1 extracted from

Delforge, D.; Devreese, B.; Dieu, M.; Delaive, E.; Van Beeumen, J.; Remacle, J.
Identification of lysine 74 in the pyruvate binding site of alanine dehydrogenase from Bacillus subtilis. Chemical modification with 2,4,6-trinitrobenzenesulfonic acid, n-succinimidyl 3-(2-pyridyldithio)propionate, and 5'-(p-(fluorosulfonyl)benzoyl)adenosine (1997), J. Biol. Chem., 272, 2276-2284.

Search for more literature for 1.4.1.1

Inhibitors

Inhibitors	Comment	Organism	Structure
2,4,6-Trinitrobenzenesulfonic acid	inactivation follows pseudo first-order kinetics with a 1:1 stoichiometric ratio between the reagent and the enzyme subunit. Partial protection by each of the substrates, NADH or pyruvate. Complete protection only in presence of the ternary complex enzyme-NADH-pyruvate	Bacillus subtilis
3-(2-pyridyldithio)propionate	inactivation follows pseudo first-order kinetics with a 1:1 stoichiometric ratio between the reagent and the enzyme subunit. Partial protection by each of the substrates, NADH or pyruvate. Complete protection only in presence of the ternary complex enzyme-NADH-pyruvate	Bacillus subtilis
5'-(p-(fluorosulfonyl)-benzoyl)adenosine	inactivation follows pseudo-first-order kinetics, complete inactivation of the enzyme can not be obtained even at high reagent concentration	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	-	r

Cofactor

Cofactor	Comment	Organism	Structure
NAD+	-	Bacillus subtilis
NADH	-	Bacillus subtilis

Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.

Release 2023.1 (January 2023)