Analysis of the C-terminal domain of Burkholderia sp. strain LB400 BphK reveals a conserved motif that affects catalytic activity

FEMS Microbiology Letters

Volumn 249, Issue 1, 2005, Pages 23-30

  Gilmartin, Niamh ^a,b   Ryan, David ^a   Dowling, David N ^a  

^a Ireland   (Ireland)

^b UNIVERSITÉ DE STRASBOURG   (France)

Author keywords

bphK; Burkholderia LB400; Glutathione S transferase; PCB; Site directed mutagenesis

Indexed keywords

4 CHLOROBENZOIC ACID; GLUTATHIONE TRANSFERASE; POLYCHLORINATED BIPHENYL;

ARTICLE; BACTERIAL STRAIN; BURKHOLDERIA; CARBOXY TERMINAL SEQUENCE; CATALYSIS; DECHLORINATION; ENZYME ACTIVITY; ENZYME SPECIFICITY; ENZYME SUBSTRATE; GENETIC CONSERVATION; HYDROGEN BOND; MOLECULAR INTERACTION; NONHUMAN; NUCLEOTIDE SEQUENCE; OPERON; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN DOMAIN; PROTEIN MOTIF; SEQUENCE ALIGNMENT; SITE DIRECTED MUTAGENESIS;

AMINO ACID MOTIFS; AMINO ACID SEQUENCE; BURKHOLDERIA; CATALYSIS; ENZYME STABILITY; GLUTATHIONE TRANSFERASE; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; MUTAGENESIS, SITE-DIRECTED; SUBSTRATE SPECIFICITY; TEMPERATURE;

BURKHOLDERIA; BURKHOLDERIA SP.; EUKARYOTA;

EID: 22144468363     PISSN: 03781097     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.femsle.2005.05.056     Document Type: Article

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