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Structural characterization of the bglH gene encoding a beta-glucosidase-like enzyme in an endophytic Bacillus pumilus strain Genet. Mol. Biol.
Bogas,Andréa C.; Watanabe,Maria Angelica E.; Barbosa,Aneli; Vilas-Boas,Laurival A.; Bonatto,Ana C.; Dekker,Robert; Souza,Emanuel M.; Fungaro,Maria Helena P..
A beta-glucosidase-like enzyme-encoding gene (bglH) of an endophytic Bacillus pumilus strain (CL16) was cloned using a shotgun genomic library constructed in Escherichia coli. The nucleotide sequence of the entire cloned fragment (2484 bp) was determined and characterized. An incomplete open reading frame (ORF) of 534 bp (ORF1) designated bglP and a complete ORF of 1419 bp (ORF2) designated bglH, located in the fragment, are organized in an operon. The protein deduced from 1419 bp (ORF2) had 472 amino acid residues without a characteristic signal peptide sequence, suggesting that the enzyme is localized in the cytoplasm. The amino acid sequence deduced from bglH gene had high similarity with beta-glucosidases from the glycosyl hydrolase family 1....
Tipo: Info:eu-repo/semantics/article Palavras-chave: Bacillus pumilus; BglH; Glucosidase; Glycosyl hydrolase 1; PTS.
Ano: 2007 URL: http://www.scielo.br/scielo.php?script=sci_arttext&pid=S1415-47572007000100018
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