The role of the conserved Lys68*:Glu265 intersubunit salt bridge in aspartate aminotransferase kinetics: Multiple forced covariant amino acid substitutions in natural variants

Protein Science

Volumn 11, Issue 5, 2002, Pages 1062-1073

  Deu, Edgar ^a   Koch, Keith A ^a   Kirsch, Jack F ^a,b  

^a UNIVERSITY OF CALIFORNIA   (United States)

^b 229 Stanley Hall 3206 ^*  (United States)

Author keywords

Aspartate aminotranferase; Context dependence; Covariance; Double mutant cycles; Evolution; Impact; Kinetics; Salt bridge; Venn diagram

Indexed keywords

ASPARTATE AMINOTRANSFERASE; GLUTAMINE; LYSINE; METHIONINE; SODIUM CHLORIDE;

AMINO ACID SUBSTITUTION; ARTICLE; CHIMERA; COVARIANCE; ENERGY; ENZYME KINETICS; ESCHERICHIA COLI; LINEAR SYSTEM; MUTAGENICITY; MUTANT; MUTATION; NONHUMAN; PRIORITY JOURNAL;

AMINO ACID SEQUENCE; AMINO ACID SUBSTITUTION; ASPARTATE AMINOTRANSFERASES; KINETICS; MODELS, BIOLOGICAL; MOLECULAR SEQUENCE DATA; PHYLOGENY; PROTEIN STRUCTURE, QUATERNARY; SEQUENCE ALIGNMENT; SUBSTRATE SPECIFICITY;

ANIMALIA; ESCHERICHIA COLI;

EID: 0036231393     PISSN: 09618368     EISSN: None     Source Type: Journal    
DOI: 10.1110/ps.0200902     Document Type: Article

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