The effects of mutations at position 253 on the thermostability of the Bacillus subtilis 3-isopropylmalate dehydrogenase subunit interface

Journal of Biochemistry

Volumn 141, Issue 6, 2007, Pages 791-797

  Ohkuri, Takatoshi ^a,b   Yamagishi, Akihiko ^a  

^a TOKYO UNIVERSITY OF PHARMACY AND LIFE SCIENCES   (Japan)

^b KYUSHU UNIVERSITY   (Japan)

Author keywords

Dimeric enzyme; Hydrophobic core; Isopropylmalate dehydrogenase; Subunit interaction; Thermostability

Indexed keywords

3 ISOPROPYLMALATE DEHYDROGENASE; ENZYME; MAGNESIUM CHLORIDE;

ARTICLE; BACILLUS SUBTILIS; CATALYSIS; CONTROLLED STUDY; ENVIRONMENTAL TEMPERATURE; ENZYME ACTIVITY; GENE MUTATION; HEAT TREATMENT; HYDROPHOBICITY; NONHUMAN; PROTEIN BINDING; PROTEIN SECONDARY STRUCTURE; THERMOSTABILITY; CHEMISTRY; CONFORMATION; DIMERIZATION; ENVIRONMENT; ENZYME STABILITY; ENZYMOLOGY; GENETICS; HEAT; KINETICS; METABOLISM; METHODOLOGY; MUTATION; TEMPERATURE; THERMUS THERMOPHILUS; X RAY CRYSTALLOGRAPHY;

BACILLUS SUBTILIS;

3-ISOPROPYLMALATE DEHYDROGENASE; BACILLUS SUBTILIS; CATALYSIS; CRYSTALLOGRAPHY, X-RAY; DIMERIZATION; ENVIRONMENT; ENZYME STABILITY; ENZYMES; HEAT; KINETICS; MAGNESIUM CHLORIDE; MOLECULAR CONFORMATION; MUTATION; TEMPERATURE; THERMUS THERMOPHILUS;

EID: 38449100935     PISSN: 0021924X     EISSN: 17562651     Source Type: Journal    
DOI: 10.1093/jb/mvm082     Document Type: Article

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