Detection of an anhydride intermediate in the carboxypeptidase a catalyzed hydrolysis of a peptide substrate by solid state NMR spectroscopy and its mechanistic implication
SCIE
SCOPUS
- Title
- Detection of an anhydride intermediate in the carboxypeptidase a catalyzed hydrolysis of a peptide substrate by solid state NMR spectroscopy and its mechanistic implication
- Authors
- Lee, HC; Ko, YH; Bin Baek, S; Kim, DH
- Date Issued
- 1998-12-01
- Publisher
- PERGAMON-ELSEVIER SCIENCE LTD
- Abstract
- 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 by the N-terminal amino group of Gly-Tyr, the carboxylate of Glu-270 becomes to attack the amide bond to generate the anhydride intermediate. (C) 1998 Elsevier Science Ltd. All rights reserved.
- Keywords
- ESTER HYDROLYSIS; METAL-ION; ACID; BINDING; COMPLEX; MODEL
- URI
- https://oasis.postech.ac.kr/handle/2014.oak/20571
- DOI
- 10.1016/S0960-894X(98)00624-6
- ISSN
- 0960-894X
- Article Type
- Article
- Citation
- BIOORGANIC & MEDICINAL CHEMISTRY LETTERS, vol. 8, no. 23, page. 3379 - 3384, 1998-12-01
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- There are no files associated with this item.
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