1985
DOI: 10.1093/nar/13.17.6273
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Nucleotide sequence ofCandida pelliculosaβ-glucosidase gene

Abstract: The nucleotide sequence of the DNA fragment containing the beta-glucosidase gene of Candida pelliculosa was determined. Analysis of the sequence revealed three open reading frames which could encode 65,825, and 412 amino acid residues. The presence of the second frame was found to be sufficient for the expression of the beta-glucosidase gene in a heterologous host Saccharomyces cerevisiae. Putative protein encoded by this gene had hydrophobic amino acids, resembling a signal peptide, at its N-terminal region a… Show more

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Cited by 52 publications
(21 citation statements)
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“…In all the sequences examined by Barnett et al (1991) the two conserved motifs were separated by 12 amino acid residues. It is now clear that there are some glucosidases, including those encoded by the celD gene for (1→4)-β-D-glucan glucohydrolase from P. fluorescens (Rixon et al, 1992), a β-glucosidasehomologous (LacZ) gene from Listeria monocytogenes (He et al (1996), accession no: U78883), a β-glucosidase gene from Candida pelliculosa (Kohchi and Toh-e, 1985) and the β-glucosidase bgln gene from Pichia capsulata (Janbon et al, 1995), in which the two motifs are separated by more than 20 residues. However, the nasturtium enzyme and the barley exohydrolase are uniquely different from all other sequences so far reported, showing the motifs S-D-W and G-I-D-M, separated by a sequence of 24 amino acids which is almost perfectly conserved (Figure 7).…”
Section: Discussionmentioning
confidence: 99%
“…In all the sequences examined by Barnett et al (1991) the two conserved motifs were separated by 12 amino acid residues. It is now clear that there are some glucosidases, including those encoded by the celD gene for (1→4)-β-D-glucan glucohydrolase from P. fluorescens (Rixon et al, 1992), a β-glucosidasehomologous (LacZ) gene from Listeria monocytogenes (He et al (1996), accession no: U78883), a β-glucosidase gene from Candida pelliculosa (Kohchi and Toh-e, 1985) and the β-glucosidase bgln gene from Pichia capsulata (Janbon et al, 1995), in which the two motifs are separated by more than 20 residues. However, the nasturtium enzyme and the barley exohydrolase are uniquely different from all other sequences so far reported, showing the motifs S-D-W and G-I-D-M, separated by a sequence of 24 amino acids which is almost perfectly conserved (Figure 7).…”
Section: Discussionmentioning
confidence: 99%
“…It has been proposed that ,-glucosidase in some bacteria and yeasts is a periplasmic protein (1,12,28). One characteristic structure associated with many periplasmic proteins and other secreted proteins is a leader sequence, which targets a protein for transport across membranes (24).…”
Section: And Discussionmentioning
confidence: 99%
“…At present, only the following two complete ,-glucosidase gene sequences are known: abg (this work) and the Candida pelliculosa gene, cpb (12). Part of the (21).…”
Section: And Discussionmentioning
confidence: 99%
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“…Both enzymes are aryl-,-glucosidases, but only Bgll is able to hydrolyze cellobiose. Clhq from Candida pelliculosa (17) and Cbgl are 29% identical and 54% similar in sequence. Clhq also has a signal peptide for transport into the periplasmic space.…”
Section: Gcttgccaca Gaccttcccg Aaggcgctca Cggataattc Cgccattacc Gacgamentioning
confidence: 99%