Structure, function, and evolution of phosphoglycerate mutases: comparison with fructose-2,6-bisphosphatase, acid phosphatase, and alkaline phosphatase.

2. Cofactor dependent Saccharomyces cerevisiae phosphoglycerate mutase . . . . . . . . . . . . . . . . 265 2.1. Structural aspects of Saccharomyces cerevisiae phosphoglycerate mutase . . . . . . . . . . 265 2.2. Mechanism of catalysis of the S. cerevisiae dPGM . . . . . . . . . . . . . . . . . . . . . . . . . . 270 2.3. Structural comparison of dPGM with other enzymes . . . . . . . . . . . . . . . . . . . . . . . . 270 2.3.1. Structural comparison of S. cerevisiae dPGM with 6-phosphofructo-2-kinase/ fructose-2,6-bisphosphatase . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 271 2.3.2. Structural comparison of S. cerevisiae dPGM with acid phosphatase . . . . . . . 272 2.3.3. Overall comparison of active sites of dPGM, Fru26P2ase, and AcPase . . . . . 273

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