Structural principles of the broad substrate specificity of Thermoactinomyces vulgaris carboxypeptidase T--role of amino acid residues at positions 260 and 262-Reference-Cited by-同舟云学术

Structural principles of the broad substrate specificity of Thermoactinomyces vulgaris carboxypeptidase T--role of amino acid residues at positions 260 and 262

Published:2008-05-23 Issue:9 Volume:21 Page:545-551
ISSN:1741-0126
Container-title:Protein Engineering Design and Selection
language:en
Short-container-title:Protein Engineering Design and Selection

Author:

Grishin A.M.,Akparov V.K.,Chestukhina G.G.

Publisher

Oxford University Press (OUP)

Subject

Molecular Biology,Biochemistry,Bioengineering,Biotechnology

Link

http://academic.oup.com/peds/article-pdf/21/9/545/4273218/gzn031.pdf

Reference41 articles.

1. Crystal Structures of Potent Thiol-Based Inhibitors Bound to Carboxypeptidase B,

2. Structural principles of the wide substrate specificity of Thermoactinomyces vulgaris carboxypeptidase T. reconstruction of the carboxypeptidase B primary specificity pocket

3. Metallocarboxypeptidases: Emerging Drug Targets in Biomedicine

4. Designing Subtilisin BPN' To Cleave Substrates Containing Dibasic Residues

5. Procarboxypeptidase A from the insect pestHelicoverpa armigeraand its derived enzyme

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