Abstract
Phosphoacetylglucosamine mutase (EC 2.7.5.2) catalyzes the interconversion of N-acetylglucosamine-1-phosphate and of N-acetylglucosamine-6-phosphate. Glucose-1,6-diphosphate activates this mutase through the formation of N-acetylglucosamine-1,6-diphosphate and glucose-6-phosphate. By adding glucose-6-phosphate dehydrogenase and an excess of N-acetylglucosamine-6-phosphate the reaction is pulled to completion with stoichiometric formation of N-acetylglucosamine-1,6-diphosphate with respect to the amount of glucose-1,6-diphosphate present. The isolation, chemical analysis, molar rotation, and cofactor activity of N-acetylglucosamine-1,6-diphosphate are described.
| Original language | English (US) |
|---|---|
| Pages (from-to) | 533-540 |
| Number of pages | 8 |
| Journal | Analytical Biochemistry |
| Volume | 85 |
| Issue number | 2 |
| DOIs | |
| State | Published - Apr 1978 |
ASJC Scopus subject areas
- Biophysics
- Biochemistry
- Molecular Biology
- Cell Biology
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Cheng, P. W., & Carlson, D. M. (1978). Quantitative enzymatic synthesis of 2-acetamido-2-deoxy-α-d-glucopyranosyl-1,6-diphosphate. Analytical Biochemistry, 85(2), 533-540. https://doi.org/10.1016/0003-2697(78)90251-8