Investigation of the role of conserved residues Ser13, Asn48 and Pro49 in the catalytic mechanism of the tau class glutathione transferase from Glycine max

Biochimica et Biophysica Acta - Proteins and Proteomics

Volumn 1804, Issue 4, 2010, Pages 662-667

  Axarli, Irene ^a   Georgiadou, Christiana ^a   Dhavala, Prathusha ^b   Papageorgiou, Anastassios C ^b   Labrou, Nikolaos E ^a  

^a AGRICULTURAL UNIVERSITY OF ATHENS   (Greece)

^b UNIVERSITY OF TURKU   (Finland)

Author keywords

Herbicide detoxification; Kinetic mechanism, Tau class glutathione transferase; Site directed mutagenesis

Indexed keywords

1 CHLORO 2,4 DINITROBENZENE; ASPARAGINE; GLUTATHIONE TRANSFERASE; PROLINE; SERINE; TAU PROTEIN;

AMINO ACID SEQUENCE; ARTICLE; BINDING SITE; CATALYSIS; ENZYME STABILITY; ENZYME STRUCTURE; NONHUMAN; NUCLEOTIDE SEQUENCE; PRIORITY JOURNAL; PROTEIN BINDING; SEQUENCE ALIGNMENT; SITE DIRECTED MUTAGENESIS; SOYBEAN; THERMOSTABILITY; WILD TYPE;

AMINO ACID SEQUENCE; AMINO ACID SUBSTITUTION; BASE SEQUENCE; CATALYTIC DOMAIN; CONSERVED SEQUENCE; DINITROCHLOROBENZENE; DNA PRIMERS; ENZYME STABILITY; GLUTATHIONE; GLUTATHIONE TRANSFERASE; HYDROGEN-ION CONCENTRATION; KINETICS; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; MUTAGENESIS, SITE-DIRECTED; PROTEIN CONFORMATION; RECOMBINANT PROTEINS; SEQUENCE HOMOLOGY, AMINO ACID; SOYBEANS; SUBSTRATE SPECIFICITY; THERMODYNAMICS;

GLYCINE MAX;

EID: 77149132452     PISSN: 15709639     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbapap.2009.10.016     Document Type: Article

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