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. 2007 Jul 25;2(3):169–176. doi: 10.1155/2008/549759

Table 2.

Substrate specificity of α-glucan phosphorylase from Pyrococcus furiosus in the synthetic and phosphorolytic directions in the presence of glucose-1-phosphate (G-1-P) after 30 min. Percent conversions were calculated as the amount of sugar phosphate remaining in the reaction after incubation at a specified time, divided by the amount of substrate used in the reaction, and then multiplied by 100. The percent G-1-P produced was expressed as percent relative intensity (RI) which was calculated as: (RI of G-1-P from oligosaccharide)/(RI of G-1-P from maltoheptaose) × 100. Substrate concentration was 7 mg ml–1 for glycogen and 7 mM for maltose through maltoheptaose.

Substrate G-1-P consumed (Synthetic) G-1-P produced (Phosphorolytic)

Maltose 100 0
Maltotriose 95 35
Maltotetraose 90 61
Maltopentaose 86 78
Maltohexaose 82 85
Maltoheptaose 80 100
Glycogen 75 64