Details
| Original language | English |
|---|---|
| Pages (from-to) | 560-568 |
| Number of pages | 9 |
| Journal | Zeitschrift fur Naturforschung - Section C Journal of Biosciences |
| Volume | 55 |
| Issue number | 7-8 |
| Publication status | Published - Aug 2000 |
Abstract
The wild-type yeast strain Zygosaccharomyces bisporus CBS 702 produced a-hydroxy-ketones (acyloins) from amino acid precursors after transamination to the corresponding 2-oxo acids. The key enzyme of the subsequent decarboxylation and C-C bond forming reaction, pyruvate decarboxylase (PDC), was examined for its substrate- and stereo-specific-ity. A wide variety of saturated and unsaturated aliphatic and aromatic aldehydes was successfully converted to acyloins. 19 of the biotransformation products identified had not been reported as natural substances before. Product yields were strongly affected by substrate structure.
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In: Zeitschrift fur Naturforschung - Section C Journal of Biosciences, Vol. 55, No. 7-8, 08.2000, p. 560-568.
Research output: Contribution to journal › Article › Research › peer review
}
TY - JOUR
T1 - Formation of Aliphatic and Aromatic α-Hydroxy Ketones by Zygosaccharomyces bisporus
AU - Neuser, Frauke
AU - Zorn, Holger
AU - Berger, Ralf G.
PY - 2000/8
Y1 - 2000/8
N2 - The wild-type yeast strain Zygosaccharomyces bisporus CBS 702 produced a-hydroxy-ketones (acyloins) from amino acid precursors after transamination to the corresponding 2-oxo acids. The key enzyme of the subsequent decarboxylation and C-C bond forming reaction, pyruvate decarboxylase (PDC), was examined for its substrate- and stereo-specific-ity. A wide variety of saturated and unsaturated aliphatic and aromatic aldehydes was successfully converted to acyloins. 19 of the biotransformation products identified had not been reported as natural substances before. Product yields were strongly affected by substrate structure.
AB - The wild-type yeast strain Zygosaccharomyces bisporus CBS 702 produced a-hydroxy-ketones (acyloins) from amino acid precursors after transamination to the corresponding 2-oxo acids. The key enzyme of the subsequent decarboxylation and C-C bond forming reaction, pyruvate decarboxylase (PDC), was examined for its substrate- and stereo-specific-ity. A wide variety of saturated and unsaturated aliphatic and aromatic aldehydes was successfully converted to acyloins. 19 of the biotransformation products identified had not been reported as natural substances before. Product yields were strongly affected by substrate structure.
UR - http://www.scopus.com/inward/record.url?scp=0033840454&partnerID=8YFLogxK
U2 - 10.1515/znc-2000-7-814
DO - 10.1515/znc-2000-7-814
M3 - Article
AN - SCOPUS:0033840454
VL - 55
SP - 560
EP - 568
JO - Zeitschrift fur Naturforschung - Section C Journal of Biosciences
JF - Zeitschrift fur Naturforschung - Section C Journal of Biosciences
SN - 0939-5075
IS - 7-8
ER -