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. © 1993 Springer-Verlag.
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Vainio, A. E. I., Torkkeli, H. T., Tuusa, T., Aho, S. A., Fagerström, B. R., & Korhola, M. P. (1993). Cloning and expression of Hormoconis resinae glucoamylase P cDNA in Saccharomyces cerevisiae. Current Genetics, 24(1–2), 38–44. https://doi.org/10.1007/BF00324663
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