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Title 

Stereochemistry in inactivation of carboxypeptidase A. : structural analysis of the inactivated carboxypeptidase A by an enantiomeric pair of 2-benzyl-3,4-epoxybutanoic acids

Authors 

Seong Eon RyuHee-Jeong ChoiD H Kim

Publisher 

American Chemical Society

Issue Date 

1997

Citation 

Journal of American Chemical Society, vol. 119, no. 1, pp. 38-41

Keywords 

2 benzyl 3,4 epoxybutyric acidcarboxypeptidase aunclassified drugarticleenantiomerenzyme active siteenzyme modificationX ray analysis

Abstract 

The X-ray crystal structure of inactivated carboxypeptidase A by (2R,3S)-2-benzyl-3,4-epoxybutanoic acid, a pseudomechanism-based inactivator, was determined to show that the carboxylate of Glu-270 at the active site of the enzyme is covalently modified: the inhibitor is tethered to the carboxylate forming an ester linkage which is brought about by the attack of the carboxylate on the oxirane ring of the inhibitor. Examination of the crystal structure in comparison with that inactivated by its enantiomer, (2S,3R)-2-benzyl-3,4-epoxybutanoic acid, shows that the two inhibitors are bound covalently to the enzyme in a symmetrical fashion. An explanation for the lack of inactivating activity found previously with (2R,3R)- as well as (2S,3S)-2-benzyl-3,4-epoxybutanoic acids was offered.

ISSN 

0002-7863

Appears in Collections

1. Journal Articles > Journal Articles

Registered Date

2017-04-19


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