Journal article

Authors list: Neuser, F; Zorn, H; Richter, U; Berger, RG

Publication year: 2000

Pages: 349-353

Journal: Biological Chemistry

Volume number: 381

Issue number: 4

ISSN: 1431-6730

DOI Link: https://doi.org/10.1515/BC.2000.046

Publisher: De Gruyter Brill

Abstract: 
Cells of the wild-type yeast strain Zygosaccharomyces bisporus CBS 702 form alpha-hydroxy ketones from aromatic amino acid precursors during fermentation, Pyruvate decarboxylase (PDC, E.C. 4.1.1.1), the key enzyme of this biotransformation catalysing the nonoxidative decarboxylation of pyruvate and other 2-oxo-acids, was purified and characterised. The active enzyme is homotetrameric (alpha(4)) with a molecular mass of about 244 kDa, Activation of PDC by its substrate pyruvate results in a sigmoidal dependence of the reaction rate from substrate concentration (apparent K-m value 1.73 mM; Hill coefficient 2.10).A cDNA library was screened using a PCR-based procedure, and a 1856 bp cDNA of PDC was identified and sequenced. The cDNA encodes a polypeptide of 563 amino acid residues (monomeric unit), Sequence alignments demonstrate high homologies (> 80%) to PDC genes from Saccharomyces cerevisiae, Kluyveromyces lactis and Kluyveromyces marxianus.

Harvard Citation style: Neuser, F., Zorn, H., Richter, U. and Berger, R. (2000) Purification, characterisation and cDNA sequencing of pyruvate decarboxylase from Zygosaccharomyces bisporus, Biological Chemistry, 381(4), pp. 349-353. https://doi.org/10.1515/BC.2000.046

APA Citation style: Neuser, F., Zorn, H., Richter, U., & Berger, R. (2000). Purification, characterisation and cDNA sequencing of pyruvate decarboxylase from Zygosaccharomyces bisporus. Biological Chemistry. 381(4), 349-353. https://doi.org/10.1515/BC.2000.046