Journal article
Competitive inhibition of a glutamate carboxypeptidase by phosphonamidothionate derivatives of glutamic acid
Bioorganic & medicinal chemistry letters, Vol.9(10), pp.1415-1418
1999
Handle:
https://hdl.handle.net/2376/109358
PMID: 10360747
Abstract
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).
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).
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Details
- Title
- Competitive inhibition of a glutamate carboxypeptidase by phosphonamidothionate derivatives of glutamic acid
- Creators
- Chester E RodriguezHaiyan LuTrang T DingKaryn L MlodnoskyAzar DastgahVinh Q LamC.Blake NicholsClifford E Berkman
- Publication Details
- Bioorganic & medicinal chemistry letters, Vol.9(10), pp.1415-1418
- Academic Unit
- Chemistry, Department of
- Publisher
- Elsevier Ltd
- Identifiers
- 99900547169901842
- Language
- English
- Resource Type
- Journal article