Preparation and properties of phosphomannomutase from baker's yeast

Luis Glaser, Stuart Kornfeld, David H. Brown

Research output: Contribution to journalArticlepeer-review

18 Scopus citations

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 languageEnglish
Pages (from-to)522-526
Number of pages5
JournalBBA - Biochimica et Biophysica Acta
Volume33
Issue number2
DOIs
StatePublished - Jun 1959

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