C-terminal truncation of glutamate decarboxylase from Lactobacillus brevis CGMCC 1306 extends its activity toward near-neutral pH

Enzyme and Microbial Technology

Volumn 50, Issue 4-5, 2012, Pages 263-269

  Yu, Kai ^a   Lin, Ling ^a   Hu, Sheng ^a   Huang, Jun ^b   Mei, Lehe ^a  

^a ZHEJIANG UNIVERSITY   (China)

^b ZHEJIANG UNIVERSITY OF SCIENCE AND TECHNOLOGY   (China)

Author keywords

C terminal truncation; Glutamate decarboxylase; Homology model; PH dependence; Site directed mutagenesis

Indexed keywords

C-TERMINAL TRUNCATION; GLUTAMATE DECARBOXYLASE; HOMOLOGY MODELS; PH DEPENDENCE; SITE DIRECTED MUTAGENESIS;

BIOCHEMISTRY;

ENZYME ACTIVITY;

4 AMINOBUTYRIC ACID; GLUTAMATE DECARBOXYLASE;

ARTICLE; BIOREACTOR; CARBOXY TERMINAL SEQUENCE; CATALYSIS; CRYSTAL STRUCTURE; ENZYME ACTIVE SITE; ENZYME ACTIVITY; ENZYME PURIFICATION; ENZYME SUBSTRATE; LACTOBACILLUS BREVIS; MICROENVIRONMENT; MOLECULAR WEIGHT; MUTANT; NONHUMAN; PH; PROTEIN EXPRESSION; SITE DIRECTED MUTAGENESIS;

AMINO ACID SEQUENCE; BINDING SITES; BIOTECHNOLOGY; CATALYTIC DOMAIN; CIRCULAR DICHROISM; GAMMA-AMINOBUTYRIC ACID; GLUTAMATE DECARBOXYLASE; HYDROGEN-ION CONCENTRATION; LACTOBACILLUS BREVIS; MODELS, MOLECULAR; MUTAGENESIS, SITE-DIRECTED; MUTATION; SEQUENCE ALIGNMENT; SEQUENCE HOMOLOGY, AMINO ACID;

BACTERIA (MICROORGANISMS); LACTOBACILLUS BREVIS;

EID: 84862798002     PISSN: 01410229     EISSN: 18790909     Source Type: Journal    
DOI: 10.1016/j.enzmictec.2012.01.010     Document Type: Article

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