Details
| Originalsprache | Englisch |
|---|---|
| Seiten (von - bis) | 369-377 |
| Seitenumfang | 9 |
| Fachzeitschrift | Journal of Molecular Catalysis B: Enzymatic |
| Jahrgang | 6 |
| Ausgabenummer | 3 |
| Publikationsstatus | Veröffentlicht - 11 März 1999 |
| Extern publiziert | Ja |
Abstract
The enzymatic synthesis of isotopically labeled D-sedoheptulose 7- phosphate from either labeled D-glucose or labeled L-serine is described. [7- 14C, 7-3H]Sedoheptulose 7-phosphate is prepared with transketolase from xylulose 5-phosphate, as C2 donor, and D-[5-14C, 5-3H]ribose 5-phosphate, which in turn is generated from D-[6-14C, 6-3H]glucose with the glycolytic enzymes. [1-13C]Sedoheptulose 7-phosphate is obtained in a one-pot reaction in 69% yield from unlabeled ribose 5-phosphate and L-[3-13C]serine via hydroxypyruvate as the C2 donor using the enzymes alanine racemase, D-amino acid oxidase, catalase and transketolase. By the latter route labeled 1- 13C]ido-heptulose 7-phosphate was also prepared when xylose 5-phosphate was substituted for the ribose 5-phosphate.
ASJC Scopus Sachgebiete
- Chemische Verfahrenstechnik (insg.)
- Katalyse
- Chemische Verfahrenstechnik (insg.)
- Bioengineering
- Biochemie, Genetik und Molekularbiologie (insg.)
- Biochemie
- Chemische Verfahrenstechnik (insg.)
- Prozesschemie und -technologie
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in: Journal of Molecular Catalysis B: Enzymatic, Jahrgang 6, Nr. 3, 11.03.1999, S. 369-377.
Publikation: Beitrag in Fachzeitschrift › Artikel › Forschung › Peer-Review
}
TY - JOUR
T1 - Enzymatic synthesis of [7-14C, 7-3H]- and [1-13C]sedoheptulose 7- phosphate and [1-13C]ido-heptulose 7-phosphate
AU - Lee, Sungsook
AU - Kirschning, Andreas
AU - Müller, Michael
AU - Way, Chris
AU - Floss, Heinz G.
N1 - Funding information: We are greatly indebted to Professor Kenji Soda, Kansai University, and Professor Nobuyoshi Esaki, Kyoto University, for their generous gifts of alanine dehydrogenase and alanine racemase and to Dr. Michael Breuer, BASF Ludwigshafen, for kindly providing several transaminases. Financial support of this work by Bayer and by the US Public Health Service through NIH grant AI20264 is gratefully acknowledged. A.K. thanks the Alexander v. Humboldt Foundation for a Lynen fellowship and M.M. thanks the Deutsche Forschungsgemeinschaft for postdoctoral fellowship support.
PY - 1999/3/11
Y1 - 1999/3/11
N2 - The enzymatic synthesis of isotopically labeled D-sedoheptulose 7- phosphate from either labeled D-glucose or labeled L-serine is described. [7- 14C, 7-3H]Sedoheptulose 7-phosphate is prepared with transketolase from xylulose 5-phosphate, as C2 donor, and D-[5-14C, 5-3H]ribose 5-phosphate, which in turn is generated from D-[6-14C, 6-3H]glucose with the glycolytic enzymes. [1-13C]Sedoheptulose 7-phosphate is obtained in a one-pot reaction in 69% yield from unlabeled ribose 5-phosphate and L-[3-13C]serine via hydroxypyruvate as the C2 donor using the enzymes alanine racemase, D-amino acid oxidase, catalase and transketolase. By the latter route labeled 1- 13C]ido-heptulose 7-phosphate was also prepared when xylose 5-phosphate was substituted for the ribose 5-phosphate.
AB - The enzymatic synthesis of isotopically labeled D-sedoheptulose 7- phosphate from either labeled D-glucose or labeled L-serine is described. [7- 14C, 7-3H]Sedoheptulose 7-phosphate is prepared with transketolase from xylulose 5-phosphate, as C2 donor, and D-[5-14C, 5-3H]ribose 5-phosphate, which in turn is generated from D-[6-14C, 6-3H]glucose with the glycolytic enzymes. [1-13C]Sedoheptulose 7-phosphate is obtained in a one-pot reaction in 69% yield from unlabeled ribose 5-phosphate and L-[3-13C]serine via hydroxypyruvate as the C2 donor using the enzymes alanine racemase, D-amino acid oxidase, catalase and transketolase. By the latter route labeled 1- 13C]ido-heptulose 7-phosphate was also prepared when xylose 5-phosphate was substituted for the ribose 5-phosphate.
KW - Enzymatic synthesis
KW - Hydroxypyruvate
KW - ido- Heptulose 7-phosphate
KW - Labeled compounds
KW - Sedoheptulose 7-phosphate
KW - Transketolase
UR - http://www.scopus.com/inward/record.url?scp=0033545532&partnerID=8YFLogxK
U2 - 10.1016/S1381-1177(98)00131-3
DO - 10.1016/S1381-1177(98)00131-3
M3 - Article
AN - SCOPUS:0033545532
VL - 6
SP - 369
EP - 377
JO - Journal of Molecular Catalysis B: Enzymatic
JF - Journal of Molecular Catalysis B: Enzymatic
SN - 1381-1177
IS - 3
ER -