Novel allosteric properties produced by residue substitutions in the subunit interface of yeast NAD+-specific isocitrate dehydrogenase

Archives of Biochemistry and Biophysics

Volumn 453, Issue 2, 2006, Pages 207-216

  Hu, Gang ^a   McAlister Henn, Lee ^a  

^a UNIVERSITY OF TEXAS HEALTH SCIENCE CENTER AT SAN ANTONIO   (United States)

Author keywords

Allosteric regulation; AMP activation; Cooperativity; Isocitrate dehydrogenase; Subunit interface; Yeast IDH

Indexed keywords

ADENOSINE PHOSPHATE; ALANINE; AMINO ACID; HETERODIMER; ISOCITRATE DEHYDROGENASE (NAD); ISOLEUCINE; NICOTINAMIDE ADENINE DINUCLEOTIDE; SERINE; VALINE;

ALLOSTERISM; AMINO ACID SEQUENCE; AMINO ACID SUBSTITUTION; ARTICLE; ENZYME ACTIVITY; ENZYME DEFECT; ENZYME KINETICS; GEL FILTRATION; HYDROPHOBICITY; LIGAND BINDING; NONHUMAN; PHENOTYPE; PRIORITY JOURNAL; PROTEIN EXPRESSION; SEDIMENTATION RATE; SEQUENCE ANALYSIS; STRUCTURE ANALYSIS; THERMUS THERMOPHILUS;

AMINO ACID SEQUENCE; AMINO ACID SUBSTITUTION; AMINO ACIDS; COMPUTER SIMULATION; ISOCITRATE DEHYDROGENASE; ISOMERISM; MODELS, CHEMICAL; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; MUTAGENESIS, SITE-DIRECTED; PROTEIN CONFORMATION; PROTEIN STRUCTURE, TERTIARY; PROTEIN SUBUNITS; STRUCTURE-ACTIVITY RELATIONSHIP; YEASTS;

EID: 33748419204     PISSN: 00039861     EISSN: 10960384     Source Type: Journal    
DOI: 10.1016/j.abb.2006.06.022     Document Type: Article

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