A novel quasi-species of glutathione transferase with high activity towards naturally occurring isothiocyanates evolves from promiscuous low-activity variants

Journal of Molecular Biology

Volumn 401, Issue 3, 2010, Pages 451-464

  Runarsdottir, Arna ^a   Mannervik, Bengt ^a  

^a UPPSALA UNIVERSITY   (Sweden)

Author keywords

Activity profiles; Functional quasi species; Glutathione transferase; Isothiocyanates; Multivariate analysis

Indexed keywords

1 CHLORO 2,4 DINITROBENZENE; ACETIC ACID DERIVATIVE; ENZYME VARIANT; GLUTATHIONE; GLUTATHIONE TRANSFERASE; GLUTATHIONE TRANSFERASE M1; GLUTATHIONE TRANSFERASE M2; ISOTHIOCYANIC ACID DERIVATIVE; PHENETHYL ISOTHIOCYANATE; RECOMBINANT ENZYME; 4-NITROPHENYL ACETATE; BACTERIAL PROTEIN; NITROPHENOL; RECOMBINANT PROTEIN;

AMINO ACID SEQUENCE; ARTICLE; BACTERIAL GENETICS; CATALYSIS; CONJUGATION; DNA SEQUENCE; ENZYME ACTIVE SITE; ENZYME ACTIVITY; ENZYME STRUCTURE; ENZYME SUBSTRATE; MOLECULAR CLONING; MULTIVARIATE ANALYSIS; NONHUMAN; PRIORITY JOURNAL; ENZYME SPECIFICITY; GENETICS; HUMAN; METABOLISM;

BACTERIA (MICROORGANISMS);

BACTERIAL PROTEINS; CATALYTIC DOMAIN; DINITROCHLOROBENZENE; GLUTATHIONE TRANSFERASE; HUMANS; ISOTHIOCYANATES; NITROPHENOLS; RECOMBINANT PROTEINS; SUBSTRATE SPECIFICITY;

EID: 77955277097     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2010.06.033     Document Type: Article

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