title: Burkholderia genome analysis reveals new enzymes belonging to the nitrilase superfamily. The amidase of Burkholderia cepacia (hospital isolate).
abstract: Burkholderia cepacia (formerly Pseudomonas cepacia) grows in media containing acetamide or propionamide as C and N sources. Chromosomal DNA from a hospital isolate of B. cepacia served as a template in PCRs using primers designed for the amplification of the P. aeruginosa amiE gene that encodes an aliphatic amidase. Partial sequencing of the PCR products gave a translated sequence 100% identical with the amino acid sequence of P. aeruginosa amidase. A search of Burkholderia genomes detected a putative amidase in B. cepacia J2315 with high identity to the P. aeruginosa amidase and predicted that other Burkholderia species also possessed CN_hydrolases that use the same catalytic triad (Glu-Lys-Cys) as amidase. Superimposition of theoretical three-dimensional models suggested that differences in the amino acid sequences between amidases from B. cepacia (hospital isolate) and B. cepacia J2315 do not affect their three-dimensional structure.
authors: INETI/DB/UTPAM, Edifi;cio F, Estrada do Paço do Lumiar, 1649-038 Lisboa, Portugal. carlos.novo@ineti.pt
authors: C
authors: C
authors: Novo
authors: R
authors: R
authors: Tata
authors: A
authors: A
authors: Clemente
authors: P R
authors: PR
authors: Brown
mesh_terms: D000581:Amidohydrolases / Q000737:chemistry / Q000235:genetics* / Q000378:metabolism; D000595:Amino Acid Sequence; D000619:Aminohydrolases / Q000235:genetics* / Q000378:metabolism; D016956:Burkholderia cepacia / Q000235:genetics*; D016680:Genome, Bacterial; D006801:Humans; D008969:Molecular Sequence Data; D005810:Multigene Family; D010802:Phylogeny; D011487:Protein Conformation; D011550:Pseudomonas aeruginosa / Q000201:enzymology / Q000235:genetics; D016415:Sequence Alignment; D017386:Sequence Homology, Amino Acid; D040681:Structural Homology, Protein
chemical_list: D000581:Amidohydrolases; C019665:amidase; D000619:Aminohydrolases; C021867:nitrilase