Glu88 in the non-catalytic domain of acylpeptide hydrolase plays dual roles: Charge neutralization for enzymatic activity and formation of salt bridge for thermodynamic stability-Reference-Cited by-同舟云学术

Glu88 in the non-catalytic domain of acylpeptide hydrolase plays dual roles: Charge neutralization for enzymatic activity and formation of salt bridge for thermodynamic stability

Published:2009-01 Issue:1 Volume:1794 Page:94-102
ISSN:1570-9639
Container-title:Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics
language:en
Short-container-title:Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics

Author:

Yang Guangyu,Bai Aixi,Gao Le,Zhang Zuoming,Zheng Baisong,Feng Yan

Publisher

Elsevier BV

Subject

Molecular Biology,Biochemistry,Biophysics,Analytical Chemistry

Reference30 articles.

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3. Removal of N-acetyl groups from blocked peptides with acylpeptide hydrolase. Stabilization of the enzyme and its application to protein sequencing;Farries;Eur. J. Biochem.,1991

4. Purification and partial characterization of alpha-N-acylpeptide hydrolase from bovine liver;Gade;J. Biol. Chem.,1978

5. Bovine lens acylpeptide hydrolase. Purification and characterization of a tetrameric enzyme resistant to urea denaturation and proteolytic inactivation;Sharma;Eur. J. Biochem.,1993

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