Functional importance of Asp56 from the α-polypeptide of Phaseolus vulgaris glutamine synthetase. An essential residue for transferase but not for biosynthetic enzyme activity

European Journal of Biochemistry

Volumn 264, Issue 2, 1999, Pages 453-460

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

^a UNIVERSITY OF SEVILLE   (Spain)

^b NONE

Author keywords

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

Indexed keywords

ALANINE; AMMONIA; ASPARTIC ACID; GLUTAMATE AMMONIA LIGASE; GLUTAMIC ACID; MUTANT PROTEIN; POLYPEPTIDE; TRANSFERASE;

AMINO ACID SUBSTITUTION; ARTICLE; ENZYME ACTIVITY; ENZYME CONFORMATION; ENZYME MECHANISM; ESCHERICHIA COLI; NITROGEN METABOLISM; NONHUMAN; PLASMID; PRIORITY JOURNAL; PROTEIN AGGREGATION; SITE DIRECTED MUTAGENESIS;

BINDING SITES; ESCHERICHIA COLI; FABACEAE; GLUTAMATE-AMMONIA LIGASE; KINETICS; MAGNESIUM; MUTAGENESIS, SITE-DIRECTED; PLANT PROTEINS; PLANTS, MEDICINAL; PROTEIN CONFORMATION; SULFHYDRYL COMPOUNDS; TRANSFERASES;

EMBRYOPHYTA; ESCHERICHIA COLI; PHASEOLUS VULGARIS;

EID: 0033198858     PISSN: 00142956     EISSN: None     Source Type: Journal    
DOI: 10.1046/j.1432-1327.1999.00636.x     Document Type: Article

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