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para-Nitrophenylphosphate (pNPP) is a non-proteinaceous chromogenic substrate for alkaline and acid phosphatases used in ELISA and conventional spectrophotometric assays. [1] Phosphatases catalyze the hydrolysis of pNPP liberating inorganic phosphate and the conjugate base of para -nitrophenol (pNP).
The enzyme alkaline phosphatase (ALP, alkaline phenyl phosphatase, also abbreviated PhoA) 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 ...
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4-Nitrophenol is a product of the enzymatic cleavage of several synthetic substrates such as 4-nitrophenyl phosphate (used as a substrate for alkaline phosphatase), 4-nitrophenyl acetate (for carbonic anhydrase), 4-nitrophenyl-β-D-glucopyranoside and other sugar derivatives which are used to assay various glycosidase enzymes.
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.
Protein phosphatase 2 (PP2), also known as PP2A, is an enzyme that in humans is encoded by the PPP2CA gene. [ 2 ] [ 3 ] The PP2A heterotrimeric protein phosphatase is ubiquitously expressed, accounting for a large fraction of phosphatase activity in eukaryotic cells. [ 4 ]
The major function of alkaline phosphatase is transporting chemicals across cell membranes. [1] Alkaline phosphatases are present in many human tissues, including bone, intestine, kidney, liver, placenta and white blood cells. [2] Damage to these tissues causes the release of ALP into the bloodstream.
This type of phosphatase includes metal-dependent protein phosphatases (PPMs) and aspartate-based phosphatases. PP1 has been found to be important in the control of glycogen metabolism, muscle contraction , cell progression, neuronal activities, splicing of RNA , mitosis , [ 1 ] cell division, apoptosis , protein synthesis, and regulation of ...