The absolute configuration of belactin A, a beta-lactone-containing serine carboxypeptidase inhibitor: importance of the beta-lactone structure for serine carboxypeptidase inhibition.
The absolute configuration of belactin A, a beta-lactone-containing serine carboxypeptidase inhibitor was studied by a crystal X-ray diffraction analysis and its absolute structure was determined to be (2R,3S)-2-¿(3S)-3-[(2-amino-5-chlorophenyl)carboxamido]-1,1-dimethyl-2-o xobutyl¿-3-methyl-4-oxooxetane. The importance of the beta-lactone structure for inhibitory activity was found by preparing several derivatives of belactin A.
Murakami
S
S
Institute of Microbial Chemistry, Tokyo, Japan.
Takahashi
Y
Y
Takeuchi
T
T
Kodama
Y
Y
Aoyagi
T
T
D001549:Benzamides / Q000737:chemistry*; D002268:Carboxypeptidases / Q000037:antagonists & inhibitors* / Q000737:chemistry / Q000378:metabolism; D043402:Cathepsin A; D003460:Crystallization; D004791:Enzyme Inhibitors / Q000737:chemistry; D020128:Inhibitory Concentration 50; D007783:Lactones / Q000737:chemistry*; D014961:X-Ray Diffraction
D001549:Benzamides; D004791:Enzyme Inhibitors; D007783:Lactones; C098701:belactin A; D002268:Carboxypeptidases; D043402:Cathepsin A; C022633:serine carboxypeptidase