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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
 

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Purification, separation and characterization of phosphoglucomutase and phosphomannomutase from maize leaves.

Different phosphomutases-phosphoglucomutase (EC 2.7.5.1; PGM) and phosphomannomutase (EC 2.7.5.7; PMM) from maize (Zea mays L.) leaves have been purified. PGM and PMM were completely separated from each other. The purified PGM was shown to be electrophoretically homogeneous. The PGM from maize leaves was found to be a homodimer with an apparent molecular mass of 132 kDa, the size of the subunits was 66 kDa. The PGM is a bifunctional enzyme, which can use both glucose-1-phosphate and mannose-1-phosphate as substrates. In contrast, the PMM appears to be monospecific for mannose-1-phosphate. Evidence is presented that PMM differs from PGM. Some properties of the maize leaves PGM and PMM differ in many respects (K(m) for substrates, pH optimum). However, some properties of PGM and PMM were similar (influence of Mg2+ and Mn2+ ions).[1]

References

  1. Purification, separation and characterization of phosphoglucomutase and phosphomannomutase from maize leaves. Popova, T.N., Matasova, L.V., Lapot'ko, A.A. Biochem. Mol. Biol. Int. (1998) [Pubmed]
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