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

Biochimica et Biophysica Acta - Proteins and Proteomics

Volumn 1794, Issue 1, 2009, Pages 94-102

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

^a JILIN UNIVERSITY   (China)

Author keywords

hydrolase; Acylpeptide hydrolase; Molecular dynamics simulation; Site directed mutagenesis; Steady state kinetic

Indexed keywords

ACYLAMINO ACID RELEASING ENZYME; ARGININE; CHLORIDE ION; GLUTAMIC ACID;

ARTICLE; CATALYSIS; ELECTRICITY; ENZYME ACTIVE SITE; ENZYME ACTIVITY; ENZYME STRUCTURE; IONIC STRENGTH; KINETICS; MODULATION; MOLECULAR DYNAMICS; MUTANT; PH; PRIORITY JOURNAL; PROTEIN FUNCTION; PROTEIN STABILITY; SIMULATION; SITE DIRECTED MUTAGENESIS; STEADY STATE; SURFACE CHARGE; THERMODYNAMICS; THERMOSTABILITY;

AEROPYRUM; ARGININE; CATALYTIC DOMAIN; COMPUTER SIMULATION; ENZYME ACTIVATION; ENZYME STABILITY; ESTERASES; GLUTAMIC ACID; HYDROGEN-ION CONCENTRATION; KINETICS; MOLECULAR CONFORMATION; MUTATION; PEPTIDE HYDROLASES; SODIUM CHLORIDE; SUBSTRATE SPECIFICITY; THERMODYNAMICS;

AEROPYRUM PERNIX;

EID: 56449093034     PISSN: 15709639     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbapap.2008.09.007     Document Type: Article

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