Abstract
TRAP, expressed mainly in osteoclasts and related monohistiocytic cells, has the capacity to hydrolyze phosphoproteins, ATP and other nucleotide triphosphates, and arylphosphates [73].Although it has been known for many years that osteoclasts express this membrane enzyme, its role in osteoclast activity has remained elusive. The porcine homolog, uteroferrin, may have as its function the delivery of iron that is secreted by the endometrium in utero [29]. However, there is no indication that the enzyme fills this potential role in osteoclasts. Although there is only limited sequence similarity between the kidney bean purple acid phosphatase and TRAP, the fact that the conformation of what is thought to be the active site of TRAP resembles that of the known catalytic domain of the bean phosphatase strengthens the inference that the presumed site in TRAP is in fact the active site [111]. The crystal structure of TRAP also revealed a protease sensitive surface loop near the active site [111]. This Introduction
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