Site-directed mutagenesis of Cys-92 from the α-polypeptide of Phaseolus vulgaris glutamine synthetase reveals that this highly conserved residue is not essential for enzyme activity but it is involved in thermal stability

Plant Science

Volumn 154, Issue 2, 2000, Pages 189-197

  Clemente, M Teresa ^a   Márquez, Antonio J ^a  

^a UNIVERSITY OF SEVILLE   (Spain)

Author keywords

Glutamine synthetase; Phaseolus vulgaris; Plant nitrogen assimilation; Recombinant enzymes; Site directed mutagenesis; Structure function

Indexed keywords

GLUTAMATE AMMONIA LIGASE; HYDROXYMERCURIBENZOIC ACID; POLYPEPTIDE;

AMINO ACID SUBSTITUTION; ARTICLE; CATALYSIS; ENZYME ACTIVITY; ENZYME DENATURATION; ENZYME INHIBITION; ENZYMOLOGY; ESCHERICHIA COLI; MUTATION; NITROGEN FIXATION; NONHUMAN; PLANT; SITE DIRECTED MUTAGENESIS; STRUCTURE ACTIVITY RELATION; THERMOSTABILITY;

PHASEOLUS VULGARIS;

EID: 0343091299     PISSN: 01689452     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0168-9452(00)00197-7     Document Type: Article

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