Alkaline Phosphatases

McComb RB, Bowers GN Jr, Posen S. Alkaline Phosphatase. New York: Plenum 1979.

Millán JL. Mammalian Alkaline Phosphatases. From Biology to Applications in Medicine and Biotechnology. Weinheim, Germany: Wiley-VCH Verlag GmbH & Co, 2006; 1–322.

Stec B, Holtz KM, Kantrowitz ER. A revised mechanism for the alkaline phosphatase reaction involving three metal ions. J Mol Biol 2000; 299: 1303–11.

Le Du MH, Stigbrand T, Taussig MJ et al. Crystal structure of alkaline phosphatase from human placenta at 1.8 A resolution. Implication for substrate specificity. J Biol Chem 2001; 276: 9158–65.

Le Du MH, Millán JL. Structural evidence of functional divergence in human alkaline phosphatases. J Biol Chem 2002; 277: 49808–14.

Kozlenkov A, Manes T, Hoylaerts MF, Millán JL. Function assignment to conserved residues in mammalian alkaline phosphatases. J Biol Chem 2002; 277: 22992–9.

Mornet E, Stura E, Lia-Baldini AS et al. Structural evidence for a functional role of human tissue nonspecific alkaline phosphatase in bone mineralization. J Biol Chem 2001; 276: 31171–8.

Hoylaerts MF, Ding L, Narisawa S et al. Mammalian alkaline phosphatase catalysis requires active site structure stabilization via the N-terminal amino acid microenvironment. Biochemistry 2006; in press.

Hoylaerts MF, Millán JL. Site-directed mutagenesis and epitope-mapped monoclonal antibodies define a catalytically important conformational difference between human placental and germ cell alkaline phosphatase. Eur J Biochem 1991; 202: 605–16.

Hummer C, Millán JL. Gly429 is the major determinant of uncompetitive inhibition of human germ cell alkaline phosphatase by l-leucine. Biochem J 1991; 274: 91–5.

Hoylaerts MF, Manes T, Millán JL. Molecular mechanism of uncompetitive inhibition of human placental and germ-cell alkaline phosphatase. Biochem J 1992; 286: 23–30.

Kozlenkov A, Le Du MH, Cuniasse P et al. Residues determining the binding specificity of uncompetitive inhibitors to tissue-nonspecific alkaline phosphatase. J Bone Miner Res 2004; 19: 1862–72.

Bossi M, Hoylaerts MF, Millán JL. Modifications in a flexible surface loop modulate the isozyme-specific properties of mammalian alkaline phosphatases. J Biol Chem 1993; 268: 25409–16.

Hoylaerts MF, Manes T, Millán JL. Mammalian alkaline phosphatases are allosteric enzymes. J Biol Chem 1997; 272: 22781–7.

Tsonis PA, Argraves WS, Millán JL. A putative functional domain of human placental alkaline phosphatase predicted from sequence comparisons. Biochem J 1988; 254: 623–4.

Vittur F, Stagni N, Moro L, de Bernard B. Alkaline phosphatase binds to collagen; a hypothesis on the mechanism of extravesicular mineralization in epiphyseal cartilage. Experientia 1984; 40: 836–7.

Wu LN, Genge BR, Lloyd GC, Wuthier RE. Collagen-binding proteins in collagenase-released matrix vesicles from cartilage. Interaction between matrix vesicle proteins and different types of collagen. J Biol Chem 1991; 266: 1195–203.

Llinas P, Stura E, Menez A et al. Structural studies of human placental alkaline phosphatase in complex with functional ligands. J Mol Biol 2005; 350: 441–51.

Low MG, Saltiel AR. Structural and functional roles of glycosyl-phosphatidylinositol in membranes. Science 1988; 239: 268–75.

Micanovic R, Bailey CA, Brink L et al. Aspartic acid-484 of nascent placental alkaline phosphatase condenses with a phosphatidylinositol glycan to become the carboxyl terminus of the mature enzyme. Proc Natl Acad Sci USA 1988; 85: 1398–402.

Majeska RJ, Wuthier RE. Studies on matrix vesicles isolated from chick epiphyseal cartilage. Association of pyrophosphatase and ATPase activities with alkaline phosphatase. Biochim Biophys Acta 1975; 391: 51–60.

Fallon MD, Whyte MP, Teitelbaum SL. Stereospecific inhibition of alkaline phosphatase by l-tetramisole prevents in vitro cartilage calcification. Lab Invest 1980; 43: 489–94.

Moss DW, Eaton RH, Smith JK, Whitby LG. Association of inorganic-pyrophosphatase activity with human alkaline-phosphatase preparations. Biochem J 1967; 102: 53–7.

Whyte MP. Hypophosphatasia and the role of alkaline phosphatase in skeletal mineralization. Endocr Rev 1994; 15: 439–61.

Rezende LA, Ciancaglini P, Pizauro JM, Leone FA. Inorganic pyrophosphate-phosphohydrolytic activity associated with rat osseous plate alkaline phosphatase. Cell Mol Biol (Noisy-le-grand). 1998; 44: 293–302.

Whyte MP. Hypophosphatasia. In Scriver CR, Beaudet AL, Sly WS, Valle D, (eds): The Metabolic and Molecular Bases of Inherited Disease. New York: McGraw-Hill 1995; 4095–112.

Hessle L, Johnson KA, Anderson HC et al. Tissue-nonspecific alkaline phosphatase and plasma cell membrane glycoprotein-1 are central antagonistic regulators of bone mineralization. Proc Natl Acad Sci USA 2002; 99: 9445–9.

Harmey D, Hessle L, Narisawa S et al. Concerted regulation of inorganic pyrophosphate and osteopontin by Akp2, Enpp1, and Ank: An integrated model of the pathogenesis of mineralization disorders. Am J Pathol 2004; 164: 1199–209.

Smith GP, Peters TJ. Subcellular localization and properties of pyridoxal phosphate phosphatases of human polymorphonuclear leukocytes and their relationship to acid and alkaline phosphatase. Biochim Biophys Acta 1981; 661: 287–94.

Wilson PD, Smith GP, Peters TJ. Pyridoxal 5’-phosphate: A possible physiological substrate for alkaline phosphatase in human neutrophils. Histochem J 1983; 15: 257–64.

Fedde KN, Lane CC, Whyte MP. Alkaline phosphatase is an ectoenzyme that acts on micromolar concentrations of natural substrates at physiologic pH in human osteosarcoma (SAOS-2) cells. Arch Biochem Biophys 1988; 264: 400–9.

Di Mauro S, Manes T, Hessle H et al. Kinetic characterization of hypophosphatasia mutations with physiological substrates. J Bone Miner Res 2002; 17: 1383–91.

Farley JR, Tarbaux NM, Lau KH, Baylink DJ. Monofluorophosphate is hydrolyzed by alkaline phosphatase and mimics the actions of NaF on skeletal tissues, in vitro. Calcif Tissue Int 1987; 40: 35–42.

Sumikawa K, Okochi T, Adachi K. Differences in phosphatidate hydrolytic activity of human alkaline phosphatase isozymes. Biochim Biophys Acta 1990; 1046: 27–31.

Lorenz B, Schroder HC. Mammalian intestinal alkaline phosphatase acts as highly active exopolyphosphatase. Biochim Biophys Acta 2001; 1547: 254–61.

Say JC, Ciuffi K, Furriel RP et al. Alkaline phosphatase from rat osseous plates: Purification and biochemical characterization of a soluble form. Biochim Biophys Acta 1991; 1074: 256–62.

Demenis MA, Leone FA. Kinetic characteristics of ATP hydrolysis by a detergent-solubilized alkaline phosphatase from rat osseous plate. IUBMB. Life 2000; 49: 113–9.

Pizauro JM, Demenis MA, Ciancaglini P, Leone FA. Kinetic characterization of a membrane-specific ATPase from rat osseous plate and its possible significance on endochodral ossification. Biochim Biophys Acta 1998; 1368: 108–14.

Ohkubo S, Kimura J, Matsuoka I. Ecto-alkaline phosphatase in NG108-15 cells: A key enzyme mediating P1 antagonist-sensitive ATP response. Br J Pharmacol 2000; 131: 1667–72.

Picher M, Burch LH, Hirsh AJ et al. Ecto 5’-nucleotidase and nonspecific alkaline phosphatase. Two AMP-hydrolyzing ectoenzymes with distinct roles in human airways. J Biol Chem 2003; 278: 13468–79.

Nayudu RV, de Meis L. Energy transduction at the catalytic site of enzymes: Hydrolysis of phosphoester bonds and synthesis of pyrophosphate by alkaline phosphatase. FEBS Lett 1989; 255: 163–6.

Rindi G, Ricci V, Gastaldi G, Patrini C. Intestinal alkaline phosphatase can transphosphorylate thiamin to thiamin monophosphate during intestinal transport in the rat. Arch Physiol Biochem 1995; 103: 33–8.

Rezende AA, Pizauro JM, Ciancaglini P, Leone FA. Phosphodiesterase activity is a novel property of alkaline phosphatase from osseous plate. Biochem J 1994; 301: 517–22.

Zhang L, Balcerzak M, Radisson J et al. Phosphodiesterase activity of alkaline phosphatase in ATP-initiated Ca2+ and phosphate deposition in isolated chicken matrix vesicles. J Biol Chem 2005; doi:10.1074/jbc.M504260200.

Sarrouilhe D, Lalegerie P, Baudry M. Endogenous phosphorylation and dephosphorylation of rat liver plasma membrane proteins, suggesting a 18 kDa phosphoprotein as a potential substrate for alkaline phosphatase. Biochim Biophys Acta 1992; 1118: 116–22.

Fedde KN, Michel MP, Whyte MP. Evidence against a role for alkaline phosphatase in the dephosphorylation of plasma membrane proteins: Hypophosphatasia fibroblast study. J Cell Biochem 1993; 53: 43–50.

Scheibe RJ, Moeller-Runge I, Mueller WH. Retinoic acid induces the expression of alkaline phosphatase in P19 teratocarcinoma cells. J Biol Chem 1991; 266: 21300–5.

Galperin MY, Bairoch A, Koonin EV. A superfamily of metalloenzymes unifies phosphopentomutase and cofactor-independent phosphoglycerate mutase with alkaline phosphatases and sulfatases. Protein Sci 1998; 7: 1829–35.

Breathnach R, Knowles JR. Phosphoglycerate mutase from wheat germ: Studies with 18O-labeled substrate, investigations of the phosphatase and phosphoryl transfer activities, and evidence for a phosphoryl-enzyme intermediate. Biochemistry 1977; 16: 3054–60.

Gijsbers R, Ceulemans H, Stalmans W, Bollen M. Structural and catalytic similarities between nucleotide pyrophosphatases/phosphodiesterases and alkaline phosphatases. J Biol Chem 2001; 276: 1361–8.

Galperin MY, Jedrzejas MJ. Conserved core structure and active site residues in alkaline phosphatase superfamily enzymes. Proteins 2001; 45: 318–24