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

Cited 32 time in scopus
Metadata Downloads
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
Author(s)
Seong Eon Ryu; Hee-Jeong Choi; D H Kim
Bibliographic Citation
Journal of American Chemical Society, vol. 119, no. 1, pp. 38-41
Publication Year
1997
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
Publisher
Amer Chem Soc
DOI
http://dx.doi.org/10.1021/ja9622463
Type
Article
Appears in Collections:
1. Journal Articles > Journal Articles
Files in This Item:
  • There are no files associated with this item.


Items in OpenAccess@KRIBB are protected by copyright, with all rights reserved, unless otherwise indicated.