title: Purification of 2,3-dihydroxybiphenyl 1,2-dioxygenase from Pseudomonas putida OU83 and characterization of the gene (bphC).
abstract: The 2,3-dihydroxybiphenyl 1,2-dioxygenase (2,3-DBPD) of Pseudomonas putida OU83 was constitutively expressed and purified to apparent homogeneity. The apparent molecular mass of the native enzyme was 256 kDa, and the subunit molecular mass was 32 kDa. The data suggested that 2,3-DBPD was an octamer of identical subunits. The nucleotide sequence of a DNA fragment containing the bphC region was determined. The deduced protein sequence for 2,3-DBPD consisted of 292 amino acid residues, with a calculated molecular mass of 31.9 kDa, which was in agreement with data for the purified 2,3-DBPD. Nucleotide and amino acid sequence analyses of the bphC gene and its product, respectively, revealed that there was a high degree of homology between the OU83 bphC gene and the bphC genes of Pseudomonas cepacia LB400 and Pseudomonas pseudoalcaligenes KF707.
authors.affiliation: Microbiology Division, Food and Drug Administration, Jefferson, Arkansas 72079, USA.
authors.forename: A A
authors.initials: AA
authors.lastname: Khan
authors.forename: R F
authors.initials: RF
authors.lastname: Wang
authors.forename: M S
authors.initials: MS
authors.lastname: Nawaz
authors.forename: W W
authors.initials: WW
authors.lastname: Cao
authors.forename: C E
authors.initials: CE
authors.lastname: Cerniglia
mesh_terms: D000595:Amino Acid Sequence; D001483:Base Sequence; D008969:Molecular Sequence Data; D010088:Oxidoreductases / Q000235:genetics / Q000302:isolation & purification*; D010802:Phylogeny; D016958:Pseudomonas putida / Q000201:enzymology* / Q000235:genetics; D016415:Sequence Alignment; D017421:Sequence Analysis
chemical_list: D010088:Oxidoreductases; C061969:2-desacetyl-2-hydroxyethyl bacteriochlorophyllide a dehydrogenase