Competitive inhibition of a glutamate carboxypeptidase by phosphonamidothionate derivatives of glutamic acid.
Several N-thiophosphonyl-glutamates were found to be potent competitive inhibitors of a zinc-dependent glutamyl hydrolase, carboxypeptidase G (CPG). Weak inhibition exhibited by an analogous N-phosphonyl-glutamate suggests that the enhanced potency of the phosphonamidothioates is due to the presence of their sulfur ligand and its favorable interactions with active site features, presumably zinc(II).
Rodriguez
C E
CE
Department of Chemistry & Biochemistry, San Francisco State University, CA 94132, USA.
Lu
H
H
Dinh
T T
TT
Mlodnosky
K L
KL
Dastgah
A
A
Lam
V Q
VQ
Nichols
C B
CB
Berkman
C E
CE
D002268:Carboxypeptidases / Q000037:antagonists & inhibitors*; D004791:Enzyme Inhibitors / Q000737:chemistry / Q000494:pharmacology*; D018698:Glutamic Acid / Q000031:analogs & derivatives / Q000494:pharmacology*; D009943:Organophosphorus Compounds / Q000737:chemistry; D013329:Structure-Activity Relationship; D013873:Thionucleotides / Q000737:chemistry
D004791:Enzyme Inhibitors; D009943:Organophosphorus Compounds; D013873:Thionucleotides; D018698:Glutamic Acid; D002268:Carboxypeptidases; C026134:glutamate carboxypeptidase