Switch of substrate specificity of hyperthermophilic acylaminoacyl peptidase by combination of protein and solvent engineering

Protein and Cell

Volumn 2, Issue 6, 2011, Pages 497-506

  Liu, Chang ^b,c   Yang, Guangyu ^a   Wu, Lie ^b   Tian, Guohe ^b   Zhang, Zuoming ^b   Feng, Yan ^a,b  

^a Shanghai Jiao Tong University   (China)

^b JILIN UNIVERSITY   (China)

^c Changchun Institute of Biological Products   (China)

Author keywords

acylaminoacyl peptidase; esterase; protein engineering; solvent engineering; substrate specificity

Indexed keywords

4 NITROPHENYLCAPRYLATE; 4 NITROPHENYLLAURATE; ACETONITRILE; ACYLAMINOACYL PEPTIDASE; LAURIC ACID; OCTANOIC ACID; PEPTIDASE; UNCLASSIFIED DRUG;

AEROPYRUM PERNIX; ARTICLE; BIOENGINEERING; CATALYSIS; CONTROLLED STUDY; ENZYME ACTIVE SITE; ENZYME ACTIVITY; ENZYME CONFORMATION; ENZYME KINETICS; ENZYME SPECIFICITY; HYDROLYSIS; MOLECULAR DOCKING; MOLECULAR DYNAMICS; NONHUMAN; PRIORITY JOURNAL; PROTEIN ENGINEERING; SITE DIRECTED MUTAGENESIS; SOLVENT ENGINEERING; THERMOSTABILITY;

AEROPYRUM PERNIX; ARCHAEA;

EID: 80053057731     PISSN: 1674800X     EISSN: 16748018     Source Type: Journal    
DOI: 10.1007/s13238-011-1057-7     Document Type: Article

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