Zobrazeno 1 - 6
of 6
pro vyhledávání: '"Dong H"'
Publikováno v:
Bioorganic & Medicinal Chemistry. 11:4377-4381
All four possible stereomers of 2-benzyl-3-methanesulfinylpropanoic acid were synthesized and evaluated as inhibitors for carboxypeptidase A to find that the isomer having the (2S,4S)-configuration is most potent followed by isomers of (2R,4S)- and (
Publikováno v:
Bioorganic & Medicinal Chemistry. 11:2421-2426
Optically active N -formyl- N -hydroxy-α-phenylalanine methylamide ( 1 ) and N -formyl- N -hydroxy-β-phenylalanine methylamide ( 2 ) were evaluated as inhibitors for thermolysin (TLN) to find that while the d -form is more potent than its enantiome
Publikováno v:
Bioorganic & Medicinal Chemistry. 10:2015-2022
Both d - and l -isomers of N -(hydroxyaminocarbonyl)phenylalanine ( 1 ) were shown to have strong binding affinity towards carboxypeptidase A (CPA) with d - 1 being more potent than its enantiomer by 3-fold (Chung, S. J.; Kim, D. H. Bioorg. Med. Chem
Autor:
Sang J. Chung, Dong H. Kim
Publikováno v:
Bioorganic & Medicinal Chemistry. 9:185-189
N-(Hydroxyaminocarbonyl)phenylalanine (1) was designed rationally as a new type of inhibitor for carboxypeptidase A (CPA). The designed inhibitor was readily prepared from phenylalnine benzyl ester in two steps and evaluated to find that rac-1 inhibi
Autor:
Kyung-Joo Lee, Dong H. Kim
Publikováno v:
Bioorganic & Medicinal Chemistry. 6:1613-1622
The X-ray crystal structure of the complex of carboxypeptidase A (CPA) and Gly-Tyr, has been documented. The crystal structure reveals that both the amide carbonyl oxygen and the terminal amino nitrogen of Gly-Tyr coordinate to the active site zinc i
Publikováno v:
Bioorganic & Medicinal Chemistry. 5:2103-2108
Papain, a prototypic cysteine protease was inactivated by methyl and benzyl esters of (2S,3S)-2-benzyl-3,4-epoxybutanoic acid. On the other hand, methyl ester of (2S,3R)-2-benzyl-3,4-epoxybutanoic acid was shown to be a competitive inhibitor for the