Zobrazeno 1 - 10
of 53
pro vyhledávání: '"Dong H"'
Autor:
Kim, Dong H., Jin, Yonghao
Publikováno v:
In Bioorganic & Medicinal Chemistry Letters 1999 9(5):691-696
Autor:
Dong H. Kim, Yonghao Jin
Publikováno v:
Bioorganic & Medicinal Chemistry Letters. 9:691-696
A series of N-acyl-N-hydroxy-beta-Phe were designed, synthesized, and shown to have potent inhibitory activity for carboxypeptidase A (CPA). They are the first examples of CPA inhibitors having a hydroxamate functionality.
Publikováno v:
Bioorganic & Medicinal Chemistry Letters. 8:3379-3384
We have detected an anhydride intermediate in the CPA catalyzed proteolytic reaction of Gly-Tyr. It appears that since the zinc-bound water molecule which is believed to attack the scissile amide carbonyl carbon in the hydrolysis reaction is excluded
Autor:
Kyung-Joo Lee, Dong H. Kim
Publikováno v:
Bioorganic & Medicinal Chemistry Letters. 8:323-326
Nitrones are utilized as the active site zinc coordinating functionality in the design of inhibitors for thermolysin. This new type of thermolysin inhibitors are as potent as the existing inhibitors bearing a carboxylate or hydroxamate zinc ligating
Autor:
Kyung-Joo Lee, Dong H. Kim
Publikováno v:
Bioorganic & Medicinal Chemistry Letters. 7:2607-2612
O- (Hydroxyacetyl)- l -β-phenyllactic acid that was conceived as a mechanism-based inactivator for carboxypeptidase A from the X-ray crystal structure of the enzyme complexed with slowly hydrolyzed substrate, Gly-Tyr and a proposed mechanism for the
Autor:
Dong H. Kim, Jeong il Park
Publikováno v:
Bioorganic & Medicinal Chemistry Letters. 6:2967-2970
Replacement of the α-proton of 2-benzyl-3-hydoroxypropanoic acid, a competitive inhibitor of carboxypeptidase A with a fluoro group brought about a 2-fold increase in K i value (0.61 mM → 1.19 mM), while p K a value decreased by 1.4 units (4.36
Publikováno v:
Bioorganic & Medicinal Chemistry Letters. 6:2837-2840
The replacement of the ester group in (2S,3R)-2-benzyl-3,4-epoxybutanoic acid methyl ester (1) with a N-benzoyl-2-pyrrolidylcarboxamide moiety changes the mode of inhibition for α-chymotrypsin from an active site directed inactivator to a reversible
Autor:
Kyung-Joo Lee, Dong H. Kim
Publikováno v:
Bioorganic & Medicinal Chemistry Letters. 6:2431-2436
(S)-2-Benzyl-2-(3-oxo-2-isoxazolidinyl)acetic acid was designed, synthesized, and kinetically proven to be a mechanism-based inactivator for carboxypeptidase A, a representative zinc-containing protease.
Publikováno v:
Bioorganic & Medicinal Chemistry Letters. 6:1449-1452
Using the electrospray ionization mass spectrometric method, we have shown that (2S,3R)-2-benzyl-3,4-epoxybutanoic acid methyl ester (BEBAME) inactivates α-chymotrypsin most probably by modifying covalently the hydroxyl of Ser-195.
Publikováno v:
Bioorganic & Medicinal Chemistry Letters. 5:1953-1956
The title compound which shows a potent in vitro cytotoxic activity has been synthesized employing the tandem double ring closure reaction of N -acyl- N -(2′-hydroxyphenyl) anthranilic acid with acetic anhydride as a key step.