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

BRENDA support

Literature summary for 5.1.1.3 extracted from

  • Whalen, K.L.; Pankow, K.L.; Blanke, S.R.; Spies, M.A.
    Exploiting enzyme plasticity in virtual screening: high efficiency inhibitors of glutamate racemase (2010), ACS Med. Chem. Lett., 1, 9-13.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 5.1.1.3

Inhibitors

Inhibitors Comment Organism Structure
2-hydroxy-3,4,5-trioxocyclopent-1-en-1-olate
-
 Bacillus subtilis
4-chlorobenzene-1,2,3-triol noncompetitive inhibition Bacillus subtilis
benzene-1,3-disulfonate
-
 Bacillus subtilis

Organism

Organism UniProt Comment Textmining
Bacillus subtilis
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
L-glutamate
-
 Bacillus subtilis D-glutamate
-
 ?

Cofactor

Cofactor Comment Organism Structure
additional information no cofactor required Bacillus subtilis

Ki Value [mM]

Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
0.042
-
 2-hydroxy-3,4,5-trioxocyclopent-1-en-1-olate pH and temperature not specified in the publication Bacillus subtilis
0.059
-
 benzene-1,3-disulfonate pH and temperature not specified in the publication Bacillus subtilis

General Information

General Information Comment Organism
physiological function glutamate racemase catalyzes stereoinversion at the Calpha of glutamate and is a source of D-glutamate in bacteria, an essential component of the peptidoglycan layer of the bacterial cell walls Bacillus subtilis