The replacement of Lys620 by serine desensitizes Escherichia coli phosphoenolpyruvate carboxylase to the effects of the feedback inhibitors L- aspartate and L-malate

European Journal of Biochemistry

Volumn 247, Issue 1, 1997, Pages 74-81

  Yano, Masato ^a,b   Izui, Katsura ^a  

^a KYOTO UNIVERSITY   (Japan)

^b KUMAMOTO UNIVERSITY   (Japan)

Author keywords

Allosteric inhibition; Desensitization to aspartate; Escherichia coli; Phosphoenolpyruvate carboxylase; Site directed mutagenesis

Indexed keywords

ASPARTIC ACID; MALIC ACID; PHOSPHOENOLPYRUVATE CARBOXYLASE;

ALLOSTERISM; AMINO ACID SUBSTITUTION; ARTICLE; CONFORMATIONAL TRANSITION; DESENSITIZATION; ENZYME CONFORMATION; ENZYME INHIBITION; ESCHERICHIA COLI; NEGATIVE FEEDBACK; NONHUMAN; PRIORITY JOURNAL; SITE DIRECTED MUTAGENESIS;

ESCHERICHIA COLI;

EID: 0030877828     PISSN: 00142956     EISSN: None     Source Type: Journal    
DOI: 10.1111/j.1432-1033.1997.t01-1-00074.x     Document Type: Article

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