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 |
Externally published | Yes |
ASJC Scopus subject areas
- Biophysics
- Biochemistry
- Molecular Biology
- Cell Biology