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The enzyme alkaline phosphatase (ALP, alkaline phenyl phosphatase) is a phosphatase with the physiological role of dephosphorylating compounds. The enzyme is found across a multitude of organisms, prokaryotes and eukaryotes alike, with the same general function, but in different structural forms suitable to the environment they function in. Alkaline phosphatase is found in the periplasmic ...
Alkaline phosphatase levels are usually high in hyperparathyroidism due to high bone turn over. In primary hyperparathyroidism, levels may remain within the normal range, but this is inappropriately normal given the increased levels of plasma calcium. [citation needed]
Elevated levels of the alkaline phosphatase enzyme are reported among those who have obesity. A study reported there were higher serum levels of alkaline phosphatase in obese than in the non-obese. With elevated alkaline phosphatase levels, there is an increase in disproportionate intracellular fat depots and thereby releasing itself into the ...
Tertiary hyperparathyroidism is a condition involving the overproduction of the hormone, parathyroid hormone, produced by the parathyroid glands. [1] The parathyroid glands are involved in monitoring and regulating blood calcium levels and respond by either producing or ceasing to produce parathyroid hormone.
Laboratory findings include low-normal serum calcium, moderately low serum phosphate, elevated serum alkaline phosphatase, and low serum 1,25 dihydroxy-vitamin D levels, hyperphosphaturia, and no evidence of hyperparathyroidism. [8] Hypophosphatemia decreases 2,3-bisphosphoglycerate (2,3-BPG) causing a left shift in the oxyhemoglobin curve.
Alkaline phosphatase allows for mineralization of calcium and phosphorus by bones and teeth. [21] ALPL gene mutation leads to insufficient TNAP enzyme and allows for an accumulation of chemicals such as inorganic pyrophosphate [ 21 ] to indirectly cause elevated calcium levels in the body and lack of bone calcification.
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Alkaline phosphatase primarily hydrolyzes phosphate monoester bonds, but it shows some promiscuity towards hydrolyzing phosphate diester bonds, making it a sort of opposite to NPP. The active sites of these two enzymes show marked similarities, namely in the presence of nearly superimposable Zn 2+ bimetallo catalytic centers.
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