Primary Information |
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BoMiProt ID | Bomi317 |
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Protein Name | Alkaline phosphatase, tissue-nonspecific isozyme |
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Organism | Bos taurus |
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Uniprot ID | P09487 |
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Milk Fraction | Whey, MFGM, Exosome |
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Ref Sequence ID | NP_789828.2 |
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Aminoacid Length | 524 |
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Molecular Weight | 57193 |
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FASTA Sequence |
Download |
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Gene Name | ALPL |
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Gene ID | 280994 |
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Protein Existence Status | Reviewed: Experimental evidence at protein level |
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Secondary Information |
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Protein Function | hydrolysis of phosphate monoesters at basic pH values; bone isoenzyme may be involved in mammalian bone calcification and the intestinal isoenzyme is thought to play a role in the transport of phosphate into epithelial cells of the intestine; alkaline phosphatase is an important serum analyte and its elevation in serum is correlated with the presence of bone,liver, and other diseases. Alkaline phosphatase (ALP) is a ubiquitous membrane-bound glycoprotein capable of providing inorganic phosphate by catalyzing the hydrolysis of organic phosphate esters, or removing inorganic pyrophosphate that inhibits calcification. |
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Biochemical Properties | highest activity
was obtained in ethanolamine buffer (pH
8.2 to 10.49); In CAPS
[3-(cyclohexylamino)-I-propanesulfonic acid[
buffer, activity was maximum between pH
10.5 and 11.1]; The maximum activity in
diethanolamine buffer occurred from pH 10.1
to 10.7; The optimal pH for alkaline phosphatase activity is affected by a number of variables:
the type of buffer, the specific substrate
used, the concentration of the substrate, and
the stability of the enzyme at high pH; Activation of alkaline phosphatase
is observed with Co 2+, Mn2+, and
Mg2+, whereas Zn ions are inhibitory. Calcium
ions have little effect on activity; The highest activities were obtained at pH 10.1 with four substrates containing
aromatic groups: a-naphthyl phosphate, pNPP,
methylumbelliferyl phosphate, and phosphotyrosine.
The alkaline phosphatase hydrolyzed
10 substrates with maximum activity at
pH 9.0. ß Casein, which is a poor substrate,
showed maximum hydrolysis at pH 8.1;Levamisole is a potent inhibitor of mammalian
alkaline phosphatases found in liver, kidney and
bone; Homoarginine inhibits the alkaline phosphatase
from fat globule membranes, microsomes
and liver to a much greater extent than the intestinal
alkaline phosphatase |
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Significance in milk | covalently bound to bovine mammary microsomal membranes and
milk fat globule membranes through linkage to phosphatidylinositol; has been found in the
mammary gland of rat, cow, cat, rabbit, goat,
mare, dog, sheep, and human; as detected in humans, AP decresed from colustrum to mature milk; ALP can dephosphorylate casein, phosphoprotein,
under suitable conditions |
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PTMs | Disulfide bond formation,N-Linked Glycosylation at Asn, GPI-anchor formation, Lipoprotein formation, Phosphorylation at Ser |
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Site(s) of PTM(s)
N-glycosylation,
O-glycosylation,
Phosphorylation
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Predicted Disorder Regions | NA |
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DisProt Annotation | |
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TM Helix Prediction | No TM helices |
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Significance of PTMs | N-glycosylation is absolutely essential for TNAP activity, but not for that of the placental or intestinal enzymes.Asn-213 is a possible N-glycosylation site, and it suggests that this sugar chain plays a key role in enzyme regulation. |
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Bibliography | 1. Bingham, E. W. and Malin, E. L. (1992) ‘Alkaline phosphatase in the lactating bovine mammary gland and the milk fat globule membrane. Release by phosphatidylinositol-specific phospholipase C’, Comparative Biochemistry and Physiology Part B: Comparative Biochemistry, 102(2), pp. 213–218. doi: 10.1016/0305-0491(92)90113-6. 2. Bingham, E. W., Garver, K. and Powlen, D. (1992) ‘Purification and properties of alkaline phosphatase in the lactating bovine mammary gland.’, Journal of dairy science, 75(12), pp. 3394–401. doi: 10.3168/jds.S0022-0302(92)78115-6. 3. Hamilton, T. A., Górnicki, S. Z. and Sussman, H. H. (1979) ‘Alkaline phosphates from human milk. Comparison with isoenzymes from placenta and liver’, Biochemical Journal, 177(1), pp. 197–201. doi: 10.1042/bj1770197. 4.Sato M, Saitoh I, Kiyokawa Y, Iwase Y, Kubota N, Ibano N, Noguchi H, Yamasaki Y, Inada E. Tissue-Nonspecific Alkaline Phosphatase, a Possible Mediator of Cell Maturation: Towards a New Paradigm. Cells. 2021 Nov 28;10(12):3338. doi: 10.3390/cells10123338. PMID: 34943845; PMCID: PMC8699127. 5.Nosjean O, Koyama I, Goseki M, Roux B, Komoda T. Human tissue non-specific alkaline phosphatases: sugar-moiety-induced enzymic and antigenic modulations and genetic aspects. Biochem J. 1997 Jan 15;321 ( Pt 2)(Pt 2):297-303. doi: 10.1042/bj3210297. PMID: 9020858; PMCID: PMC1218068. |