Catalytic activity of the N-terminal domain of Escherichia coli asparagine synthetase B can be reengineered by single-point mutation

Journal of the American Chemical Society

Volumn 119, Issue 25, 1997, Pages 5785-5791

  Boehlein, Susan K ^b   Rosa Rodriguez, José G ^a   Schuster, Sheldon M ^b,c   Richards, Nigel G J ^a  

^a University of Florida ^*  (United States)

^b UNIVERSITY OF FLORIDA COLLEGE OF MEDICINE   (United States)

^c UNIVERSITY OF FLORIDA   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ASPARAGINE; ASPARTATE AMMONIA LIGASE; ASPARTIC ACID; BACTERIAL ENZYME; GLUTAMIC ACID; GLUTAMINE; HYDROLYASE; MUTANT PROTEIN;

ARTICLE; ENZYME ACTIVITY; ENZYME MECHANISM; ESCHERICHIA COLI; GENETIC ENGINEERING; POINT MUTATION; PROTEIN DOMAIN; PROTEIN MODIFICATION;

EID: 0030849770     PISSN: 00027863     EISSN: None     Source Type: Journal    
DOI: 10.1021/ja9613668     Document Type: Article

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