Cysteine-191 in aspartate aminotransferases appears to be conserved due to the lack of a neutral mutation pathway to the functional equivalent, alanine-191

Proteins: Structure, Function and Genetics

Volumn 24, Issue 2, 1996, Pages 195-208

  Gloss, Lisa M ^a   Spencer, Daniel E ^a   Kirsch, Jack F ^a  

^a UNIVERSITY OF CALIFORNIA   (United States)

Author keywords

Conserved cysteine; Protein evolution; Pyridoxal phosphate

Indexed keywords

ALANINE; ASPARTATE AMINOTRANSFERASE; BACTERIAL ENZYME; CYSTEINE; MUTANT PROTEIN; PYRIDOXAL 5 PHOSPHATE;

ARTICLE; ENZYME KINETICS; ENZYME STRUCTURE; ESCHERICHIA COLI; EVOLUTION; GENE MUTATION; GENETIC CONSERVATION; NONHUMAN; PHENOTYPE; PRIORITY JOURNAL; PROTEIN STABILITY;

ALANINE; AMINO ACID SEQUENCE; ASPARTATE AMINOTRANSFERASES; CONSERVED SEQUENCE; CYSTEINE; ESCHERICHIA COLI; MODELS, CHEMICAL; MODELS, MOLECULAR; MUTAGENESIS, SITE-DIRECTED; MUTATION; PROTEIN DENATURATION; STRUCTURE-ACTIVITY RELATIONSHIP; UREA;

EID: 0029931777     PISSN: 08873585     EISSN: None     Source Type: Journal    
DOI: 10.1002/(SICI)1097-0134(199602)24:2<195::AID-PROT6>3.0.CO;2-I     Document Type: Article

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