Abstract
Alkaline phosphatase (AP) (orthophosphoric-monoester phosphohydrolase) is a nonspecific phosphomonoesterase that functions through a phosphoseryl intermediate to produce free inorganic phosphate or to transfer the phosphoryl group to other alcohols. This enzyme is abundant in both prokaryotes and eukaryotes. In Escherichia coli , AP is involved in recovering phosphate from esters when free inorganic phosphate is depleted. The precise function of mammalian APs is still unclear. With a single mutation in its structural gene causing a fatal human hereditary disease—hypophosphotasia—it is postulated that AP participates in modulating bone mineralization. This chapter describes the purification procedure and the biochemical characteristics of the AP from the hyperthermophilic gram-negative eubacterium Thermotoga neapolitana and of the recombinant enzyme expressed in E. coli. Biochemical properties of this enzyme are compared to those of its calf intestine and E. coli homologs.
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