Title: Anomerization of glucose 6-phosphate: Catalysis by phosphoglucose isomerase
Abstract: The anomerase (1-epimerase) activity of phosphoglucose isomerase (d-glucose 6-phosphate ketol-isomerase EC 5.3.1.9) has been studied. The pH-Vmax profile, assayed by two different methods, shows a dependence on two ionizable groups in the enzyme with pK values of 7.0 and 9.3 at 0 °C. Additionally, an unusual reversal of the basic leg of the normal profile to yield a large increase in Vmax is observed above pH 9.5. Deuterium solvent isotope effects of Vmax(H2O)Vmax(D2O) = 1.39 and 2.07 are observed for isomerase and anomerase activities respectively. An anomerase mechanism similar to noncatalyzed anomerization is postulated with a discussion of the catalytic groups involved.
Publication Year: 1979
Publication Date: 1979-01-01
Language: en
Type: article
Indexed In: ['crossref', 'pubmed']
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Cited By Count: 4
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