| Literature DB >> 8358830 |
A E Vainio1, H T Torkkeli, T Tuusa, S A Aho, B R Fagerström, M P Korhola.
Abstract
A cDNA coding for glucoamylase P of Hormoconis resinae was cloned using a synthetic oligonucleotide probe coding for a peptide fragment of the purified enzyme and polyclonal anti-glucoamylase antibodies. Nucleotide-sequence analysis revealed an open reading frame of 1848 base pairs coding for a protein of 616 amino-acid residues. Comparison with other fungal glucoamylase amino-acid sequences showed homologies of 37-48%. The glucoamylase cDNA, when introduced into Saccharomyces cerevisiae under the control of the yeast ADC1 promoter, directed the secretion of active glucoamylase P into the growth medium.Entities:
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Year: 1993 PMID: 8358830 DOI: 10.1007/bf00324663
Source DB: PubMed Journal: Curr Genet ISSN: 0172-8083 Impact factor: 3.886