Abstract
A partially purified yeast enzyme is described which catalyzes specifically the conversion of α-mannose-1-phosphate to mannos-6-phosphate. This enzyme has been named phosphomannomutase. The enzyme is inactive in the absence of α-glucose-1,6-diphosphate or α-mannose-1,6-diphosphate. The apparent Michaelis constant of either coenzyme is approximately 1.5·10-4 M. Evidence is presented that phosphomannomutase is distinct from phosphoglucomutase.
| Original language | English |
|---|---|
| Pages (from-to) | 522-526 |
| Number of pages | 5 |
| Journal | BBA - Biochimica et Biophysica Acta |
| Volume | 33 |
| Issue number | 2 |
| DOIs | |
| State | Published - Jun 1959 |
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