Details
| Original language | English |
|---|---|
| Pages (from-to) | 349-353 |
| Number of pages | 5 |
| Journal | Biological chemistry |
| Volume | 381 |
| Issue number | 4 |
| Publication status | Published - Apr 2000 |
Abstract
Cells of the wild-type yeast strain Zygosaccharomyces bisporus CBS 702 form α-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 non-oxidative decarboxylation of pyruvate and other 2oxo-acids, was purified and characterised. The active enzyme is homotetrameric (α4) 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.
Keywords
- Acyloin formation, Enzyme purification, Non-conventional yeast, Sequence alignment, α-Hydroxy ketones
ASJC Scopus subject areas
- Biochemistry, Genetics and Molecular Biology(all)
- Biochemistry
- Biochemistry, Genetics and Molecular Biology(all)
- Molecular Biology
- Biochemistry, Genetics and Molecular Biology(all)
- Clinical Biochemistry
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In: Biological chemistry, Vol. 381, No. 4, 04.2000, p. 349-353.
Research output: Contribution to journal › Article › Research › peer review
}
TY - JOUR
T1 - Purification, characterisation and cDNA sequencing of pyruvate decarboxylase from Zygosaccharomyces bisporus
AU - Neuser, Frauke
AU - Zorn, Holger
AU - Richter, Ulla
AU - Berger, Ralf G.
N1 - Funding information: Frauke Neuser and Ulla Richter were financially supported by the Deutsche Forschungsgemeinschaft.
PY - 2000/4
Y1 - 2000/4
N2 - Cells of the wild-type yeast strain Zygosaccharomyces bisporus CBS 702 form α-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 non-oxidative decarboxylation of pyruvate and other 2oxo-acids, was purified and characterised. The active enzyme is homotetrameric (α4) 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.
AB - Cells of the wild-type yeast strain Zygosaccharomyces bisporus CBS 702 form α-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 non-oxidative decarboxylation of pyruvate and other 2oxo-acids, was purified and characterised. The active enzyme is homotetrameric (α4) 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.
KW - Acyloin formation
KW - Enzyme purification
KW - Non-conventional yeast
KW - Sequence alignment
KW - α-Hydroxy ketones
UR - http://www.scopus.com/inward/record.url?scp=0034056364&partnerID=8YFLogxK
U2 - 10.1515/BC.2000.046
DO - 10.1515/BC.2000.046
M3 - Article
C2 - 10839465
AN - SCOPUS:0034056364
VL - 381
SP - 349
EP - 353
JO - Biological chemistry
JF - Biological chemistry
SN - 1431-6730
IS - 4
ER -