Thermostabilization of glutamate decarboxylase B from Escherichia coli by structure-guided design of its pH-responsive N-terminal interdomain

Journal of Biotechnology

Volumn 174, Issue 1, 2014, Pages 22-28

  Jun, Chanha ^a   Joo, Jeong Chan ^a,c   Lee, Jung Heon ^b   Kim, Yong Hwan ^a  

^a Kwangwoon University   (South Korea)

^b Chosun University   (South Korea)

^c UNIVERSITY OF TORONTO   (Canada)

Author keywords

Glutamate decarboxylase B; Molecular dynamics simulation; PH responsive interdomain; Protein engineering; Thermostability

Indexed keywords

GLUTAMATE DECARBOXYLASE; INTER-DOMAIN; MOLECULAR DYNAMICS SIMULATIONS; PROTEIN ENGINEERING; THERMOSTABILITY;

BIOCHEMICAL ENGINEERING; ENZYME KINETICS; ESCHERICHIA COLI; GENETIC ENGINEERING; MOLECULAR DYNAMICS;

STABILITY;

GLUTAMATE DECARBOXYLASE; GLUTAMATE DECARBOXYLASE B; UNCLASSIFIED DRUG;

ARTICLE; BACTERIAL STRAIN; BIOCATALYST; ENZYME ANALYSIS; ENZYME KINETICS; ENZYME PURIFICATION; ESCHERICHIA COLI; HIGH TEMPERATURE; MOLECULAR DYNAMICS; MOLECULAR INTERACTION; MUTANT; NONHUMAN; PH; PRIORITY JOURNAL; PROTEIN EXPRESSION; SITE DIRECTED MUTAGENESIS; STATIC ELECTRICITY; THERMOSTABILITY; TRIPLE HELIX; WILD TYPE;

GLUTAMATE DECARBOXYLASE B; MOLECULAR DYNAMICS SIMULATION; PH-RESPONSIVE INTERDOMAIN; PROTEIN ENGINEERING; THERMOSTABILITY;

CATALYTIC DOMAIN; ENZYME STABILITY; ESCHERICHIA COLI; ESCHERICHIA COLI PROTEINS; GLUTAMATE DECARBOXYLASE; MEMBRANE PROTEINS; MOLECULAR DYNAMICS SIMULATION; MUTAGENESIS, SITE-DIRECTED; PROTEIN CONFORMATION; PROTEIN STRUCTURE, SECONDARY; PROTEIN STRUCTURE, TERTIARY; THERMODYNAMICS;

EID: 84893650210     PISSN: 01681656     EISSN: 18734863     Source Type: Journal    
DOI: 10.1016/j.jbiotec.2014.01.020     Document Type: Article

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