Title of article :
The inhibition of glutamate racemase by
Author/Authors :
Suzana Glavas، نويسنده , , Martin E. Tanner، نويسنده ,
Issue Information :
روزنامه با شماره پیاپی سال 1997
Abstract :
We report that is a competitive inhibitor of glutamate racemase (KI = 56 μM). The compound acts as an alternate substrate and is converted into α-ketoglutarate and ammonia (KM = 57 μM, kcat/KM = 3.2 × 103M−1sec−1). An imine intermediate is likely the species causing the inhibition. is a weak inhibitor and is slowly converted to α-ketoglutarate (kcat/KM = 30 M−1sec−1).
Journal title :
Bioorganic & Medicinal Chemistry Letters
Journal title :
Bioorganic & Medicinal Chemistry Letters