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Literature summary for 5.1.1.1 extracted from

  • Henderson, L.L.; Johnson, R.B.
    Inhibition studies of the enantiomers of beta-chloroalanine on purified alanine racemase from Bacillus subtilis (1976), Biochem. Biophys. Res. Commun., 68, 793-798.
    View publication on PubMed

Inhibitors

Inhibitors Comment Organism Structure
D-Chloroalanine Ki: 0.005 mM, competitive Bacillus subtilis
L-chloroalanine Ki: 1.71 mM, noncompetitive Bacillus subtilis

Organism

Organism UniProt Comment Textmining
Bacillus subtilis
-
-
-

Reaction

Reaction Comment Organism Reaction ID
L-alanine = D-alanine the active site of the alanine racemase reacts asymmetrically with the enantiomers of the substrate and has a conformation which greatly favors the D-enantiomer Bacillus subtilis

Substrates and Products (Substrate)

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