A molecular design that stabilizes active state in bacterial allosteric l-lactate dehydrogenases

Journal of Biochemistry

Volumn 150, Issue 5, 2011, Pages 579-591

  Arai, Kazuhito ^a   Ichikawa, Jun ^a   Nonaka, Shinta ^a   Miyanaga, Akimasa ^a   Uchikoba, Hiroyuki ^b   Fushinobu, Shinya ^b   Taguchi, Hayao ^a  

^a TOKYO UNIVERSITY OF SCIENCE   (Japan)

^b UNIVERSITY OF TOKYO   (Japan)

Author keywords

allosteric regulation; bacteria; catalysis; glycolysis; site directed mutagenesis

Indexed keywords

BACTERIAL ENZYME; FRUCTOSE 1,6 BISPHOSPHATE; LACTATE DEHYDROGENASE; MALATE DEHYDROGENASE; MANGANESE; PYRUVIC ACID;

ALLOSTERISM; ARTICLE; BACTERIUM MUTANT; CONTROLLED STUDY; DENATURATION; ENTHALPY; ENZYME ACTIVATION; ENZYME ACTIVE SITE; ENZYME ACTIVITY; ENZYME INACTIVATION; ENZYME STABILITY; ENZYME SUBUNIT; LACTOBACILLUS CASEI; MOLECULAR EVOLUTION; NONHUMAN; PH; WILD TYPE;

ALLOSTERIC REGULATION; BACTERIAL PROTEINS; BINDING SITES; L-LACTATE DEHYDROGENASE; LACTOBACILLUS CASEI; MUTAGENESIS, SITE-DIRECTED;

BACTERIA (MICROORGANISMS); LACTOBACILLUS CASEI; LACTOBACILLUS PENTOSUS;

EID: 80455156050     PISSN: 0021924X     EISSN: 17562651     Source Type: Journal    
DOI: 10.1093/jb/mvr100     Document Type: Article

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