Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: EC:3.1.3.1 (alkaline phosphatase)
 47,916 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The ability of alkaline phosphatase in purified preparations from human neutrophils and liver to utilize ATP or inorganic pyrophosphate as substrate depended upon the Mg2+ concentration. With pyrophosphate present (1.0 mmol/l), activity peaked at Mg2+ concentrations of 0.25 to 0.50 mmol/l and fell sharply above this. By contrast, p-nitrophenylphosphatase activity was activated with Mg2+ concentration up to 0.75 mmol/l but above this was constant to 5.0 mmol/l. Hydrolysis was abolished by L-levamisole, a specific inhibitor of alkaline phosphatase. Testing butanol extracts of neutrophils from 50 healthy subjects showed good correlation of enzyme activity with p-nitrophenylphosphate and ADP (r = 0.90), and between p-nitrophenylphosphate and pyridoxal phosphate (r = 0.96) as substrate, consistent with hydrolysis of all three phosphoesters by one enzyme. Inhibition studies yielded no evidence of a specific pyridoxal phosphatase. Alkaline phosphatase from human neutrophils has the same broad substrate specificity as other molecular forms of the human enzyme and, like other forms, has little or no activity towards phosphoesters complexed with Mg2+.
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PMID:Substrate specificity of alkaline phosphatase from human polymorphonuclear leukocytes. 380 35

The intracellular localization of pyridoxal phosphatase activity was demonstrated in human neutrophils by electron microscope cytochemistry. Under alkaline conditions, an enzyme active against pyridoxal phosphate was localized to a cytoplasmic granule population, the phosphasome. These granules have previously been shown by electron microscope cytochemical techniques and by subcellular fractionation to be rich in alkaline phosphatase. Under acidic conditions, a phosphatase activity against pyridoxal phosphate was localized to intracellular multilamellar bodies resembling secondary lysosomes. These were quite distinct from the primary, secondary and phosphasome granules and this unique localization corresponds to that previously demonstrated (tertiary granules) by subcellular fractionation studies of these cells. The similarity in the enzyme reaction requirements of alkaline pyridoxal phosphatase and alkaline phosphatase, and their localization to the same subcellular organelle, suggests that pyridoxal phosphate may be a physiological substrate for human neutrophil alkaline phosphatase.
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PMID:Pyridoxal 5'-phosphate: a possible physiological substrate for alkaline phosphatase in human neutrophils. 630 89

Two observations stimulated the interest in vitamin B-6 and alkaline phosphatase in brain: the marked increase in plasma pyridoxal phosphate and the occurrence of pyridoxine responsive seizures in hypophosphatasia. The increase in plasma pyridoxal phosphate indicates the importance of tissue non-specific alkaline phosphatase (TNAP) in transferring vitamin B-6 into the tissues. Vitamin B-6 is involved in the biosynthesis of most of the neurotransmitters. Decreased gamma-aminobutyrate (GABA) appears to be most directly related to the development of seizures in vitamin B-6 deficiency. Cytosolic pyridoxal phosphatase/chronophin may interact with vitamin B-6 metabolism and neuronal development and function. Ethanolaminephosphate phospholyase interacts with phosphoethanolamine metabolism. Extracellular pyridoxal phosphate may interact with purinoceptors and calcium channels. In conclusion, TNAP clearly influences extracellular and intracellular metabolism of vitamin B-6 in brain, particularly during developmental stages. While effects on GABA metabolism appear to be the major contributor to seizures, multiple other intra- and extra-cellular metabolic systems may be affected directly and/or indirectly by altered vitamin B-6 hydrolysis and uptake resulting from variations in alkaline phosphatase activity.
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PMID:Vitamin B-6 Metabolism and Interactions with TNAP. 2621 14