Literature summary for 2.6.1.21 extracted from

Soper, T.S.; Jones, W.M.; Lerner, B.; Trop, M.; Manning, J.M.
Inactivation of bacterial D-amino acid transaminase by beta-chloro-D-alanine (1977), J. Biol. Chem., 252, 3170-3175.

Search for more literature for 2.6.1.21

Inhibitors

Inhibitors	Comment	Organism	Structure
beta-Chloro-D-alanine	catalyzes alpha,beta elimination to yield pyruvate, chloride and ammonia, loss of activity during beta-elimination in presence of D-alanine and 2-oxoglutarate, a potent competitive inhibitor vs. D-alanine	Lysinibacillus sphaericus

KM Value [mM]

KM Value [mM]	KM Value Maximum [mM]	Substrate	Comment	Organism	Structure
4.2	-	D-alanine	-	Lysinibacillus sphaericus

Molecular Weight [Da]

Molecular Weight [Da]	Molecular Weight Maximum [Da]	Comment	Organism
30000	-	2 * 30000, SDS-PAGE	Lysinibacillus sphaericus

Organism

Organism	UniProt	Comment	Textmining
Lysinibacillus sphaericus	-	-	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
beta-chloro-D-alanine	loss in enzyme activity during beta-elimination	Lysinibacillus sphaericus	pyruvate + ammonia + Cl-	-	?

Subunits

Subunits	Comment	Organism
dimer	2 * 30000, SDS-PAGE	Lysinibacillus sphaericus

Temperature Optimum [°C]

Temperature Optimum [°C]	Temperature Optimum Maximum [°C]	Comment	Organism
37	-	assay at	Lysinibacillus sphaericus

Ki Value [mM]

Ki Value [mM]	Ki Value maximum [mM]	Inhibitor	Comment	Organism	Structure
0.01	-	beta-Chloro-D-alanine	-	Lysinibacillus sphaericus

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)