Comparison of the binuclear metalloenzymes diphosphoglycerate-independent phosphoglycerate mutase and alkaline phosphatase: Their mechanism of catalysis via a phosphoserine intermediate

A comparison between binuclear metalloenzymes was performed by studying their mechanism of catalysis. Diphosphoglycerate-independent phosphoglycerate mutase and alkaline phosphatase can catalyze a phosphatase and a phosphotransferase reaction as a part of their overall catalytic cycle. The crystal structure of enzymes were studied and similarities between their active site, utilization of two divalent metal ions and catalytic mechanism were found. Results showed that both enzymes evolved from a common ancestral enzyme and unite both types of enzymes in a single class.