Engineering of helicobacter pylori lasparaginase: Characterization of two functionally distinct groups of mutants e0117025

PLoS ONE

Volumn 10, Issue 2, 2015, Pages

  Maggi, Maristella ^a   Chiarelli, Laurent R ^a   Valentini, Giovanna ^a   Scotti, Claudia ^a  

^a UNIVERSITY OF PAVIA   (Italy)

Author keywords

[No Author keywords available]

Indexed keywords

ASPARAGINASE; ASPARAGINE; GLUTAMINASE; AMIDASE; GLUTAMIN-(ASPARAGIN-)ASE; RECOMBINANT PROTEIN; THREONINE;

AMINO ACID SUBSTITUTION; ARTICLE; CONTROLLED STUDY; ENZYME ACTIVITY; ENZYME ENGINEERING; ENZYME PURIFICATION; ENZYME REGULATION; ENZYME STABILITY; ENZYME SUBSTRATE COMPLEX; HL 60 CELL LINE; HYDROLYSIS; IN VITRO STUDY; MOLECULAR CLONING; NONHUMAN; PROTEIN EXPRESSION; SITE DIRECTED MUTAGENESIS; WILD TYPE; CELL PROLIFERATION; CHEMISTRY; DRUG EFFECTS; ENZYME ACTIVE SITE; ENZYMOLOGY; GENETIC ENGINEERING; GENETICS; HELICOBACTER PYLORI; HUMAN; ISOLATION AND PURIFICATION; METABOLISM; MUTATION; PROCEDURES;

BACTERIA (MICROORGANISMS); HELICOBACTER PYLORI;

AMIDOHYDROLASES; ASPARAGINASE; CATALYTIC DOMAIN; CELL PROLIFERATION; GENETIC ENGINEERING; GLUTAMINASE; HELICOBACTER PYLORI; HL-60 CELLS; HUMANS; MUTATION; RECOMBINANT PROTEINS; THREONINE;

EID: 84922598682     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0117025     Document Type: Article

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