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Volumn 184, Issue 2, 2013, Pages 182-192

Crystal structure of rat intestinal alkaline phosphatase - Role of crown domain in mammalian alkaline phosphatases

Author keywords

Crown domain; Glycosylation; Metal ion requirements; Rat intestinal alkaline phosphatase structure

Indexed keywords

ALKALINE PHOSPHATASE; INTESTINE ENZYME; MAGNESIUM ION; PHOSPHATE; PRODRUG; ZINC ION;

EID: 84887230068     PISSN: 10478477     EISSN: 10958657     Source Type: Journal    
DOI: 10.1016/j.jsb.2013.09.017     Document Type: Article
Times cited : (27)

References (42)
  • 2
    • 0027373184 scopus 로고
    • Modifications in a flexible surface loop modulate the isoenzyme-specific properties of mammalian alkaline phosphatase
    • Bossi M., Hoylaerts M.F., Millain J.L. Modifications in a flexible surface loop modulate the isoenzyme-specific properties of mammalian alkaline phosphatase. J. Biol. Chem. 1993, 268:25409-25416.
    • (1993) J. Biol. Chem. , vol.268 , pp. 25409-25416
    • Bossi, M.1    Hoylaerts, M.F.2    Millain, J.L.3
  • 3
    • 0034536884 scopus 로고    scopus 로고
    • Differences between duodenal and jejunal rat alkaline phosphatase
    • Calhau C., Martel F., Hipolito-Reis C., Azevedo I. Differences between duodenal and jejunal rat alkaline phosphatase. Clin. Biochem. 2000, 33:571-577.
    • (2000) Clin. Biochem. , vol.33 , pp. 571-577
    • Calhau, C.1    Martel, F.2    Hipolito-Reis, C.3    Azevedo, I.4
  • 5
    • 82955246714 scopus 로고    scopus 로고
    • Active site detection by spatial conformity and electrostatic analysis-unravelling a proteolytic function in shrimp alkaline phosphatase
    • Chakraborty S., Minda R., Salaye L., Bhattacharjee S.K., Rao B.J. Active site detection by spatial conformity and electrostatic analysis-unravelling a proteolytic function in shrimp alkaline phosphatase. PLoS ONE 2011, 6(12):e28470.
    • (2011) PLoS ONE , vol.6 , Issue.12
    • Chakraborty, S.1    Minda, R.2    Salaye, L.3    Bhattacharjee, S.K.4    Rao, B.J.5
  • 6
    • 0026773209 scopus 로고
    • Structure and mechanism of alkaline phosphatase
    • Coleman J.E. Structure and mechanism of alkaline phosphatase. Annu. Rev. Biophys. Biomol. Struct. 1992, 21:441-483.
    • (1992) Annu. Rev. Biophys. Biomol. Struct. , vol.21 , pp. 441-483
    • Coleman, J.E.1
  • 7
    • 0028103275 scopus 로고
    • The CCP4 suite: programs for protein crystallography
    • Collaborative Computational Project N
    • Collaborative Computational Project N The CCP4 suite: programs for protein crystallography. Acta Crystallogr. D 1994, 50:760-763.
    • (1994) Acta Crystallogr. D , vol.50 , pp. 760-763
  • 8
    • 34547592557 scopus 로고    scopus 로고
    • MolProbity: all-atom contacts and structure validation for proteins and nucleic acids
    • Davis I.W., Leaver-Fay A., Chen V.B., Block J.N., Kapral G.J., et al. MolProbity: all-atom contacts and structure validation for proteins and nucleic acids. Nucl. Acids Res. 2007, 35:W375-W383.
    • (2007) Nucl. Acids Res. , vol.35
    • Davis, I.W.1    Leaver-Fay, A.2    Chen, V.B.3    Block, J.N.4    Kapral, G.J.5
  • 10
    • 16644387077 scopus 로고    scopus 로고
    • Ligand-binding and metal exchange crystallographic studies on shrimp alkaline phosphatase
    • De Backer M.M.E., McSweeney S., Lindley P.F., Hough E. Ligand-binding and metal exchange crystallographic studies on shrimp alkaline phosphatase. Acta Crystallogr. D 2004, 60:1555-1561.
    • (2004) Acta Crystallogr. D , vol.60 , pp. 1555-1561
    • De Backer, M.M.E.1    McSweeney, S.2    Lindley, P.F.3    Hough, E.4
  • 13
    • 0015245862 scopus 로고
    • Organ-specific inhibition of human alkaline phosphatase isoenzymes of liver, bone, intestine and placenta; l-phenylalanine, l-tryptophan and l-homoarginine
    • Fishman W.H., Sie H.G. Organ-specific inhibition of human alkaline phosphatase isoenzymes of liver, bone, intestine and placenta; l-phenylalanine, l-tryptophan and l-homoarginine. Enzymologia 1971, 41:140-167.
    • (1971) Enzymologia , vol.41 , pp. 140-167
    • Fishman, W.H.1    Sie, H.G.2
  • 14
    • 0342832999 scopus 로고    scopus 로고
    • Improved oral drug delivery: solubility limitations overcome by the use of prodrugs
    • Fleisher D., Bong R., Stewart B.H. Improved oral drug delivery: solubility limitations overcome by the use of prodrugs. Adv. Drug Deliv. Rev. 1996, 19:115-130.
    • (1996) Adv. Drug Deliv. Rev. , vol.19 , pp. 115-130
    • Fleisher, D.1    Bong, R.2    Stewart, B.H.3
  • 15
    • 67649398906 scopus 로고    scopus 로고
    • Evaluation of in vitro models for screening alkaline phosphatase-mediated bioconversion of phosphate ester prodrugs
    • Haodan Y., Na L., Lai Y. Evaluation of in vitro models for screening alkaline phosphatase-mediated bioconversion of phosphate ester prodrugs. Drug Metab. Dispos. 2009, 37:1443-1447.
    • (2009) Drug Metab. Dispos. , vol.37 , pp. 1443-1447
    • Haodan, Y.1    Na, L.2    Lai, Y.3
  • 16
    • 18944395290 scopus 로고    scopus 로고
    • Characterization of structural and catalytic differences in rat intestinal alkaline phosphatase isozymes
    • Harada T., Koyama I., Matsunaga T., Kikuno A., Kasahara T., Hassimoto M., Alpers D.H., Komoda T. Characterization of structural and catalytic differences in rat intestinal alkaline phosphatase isozymes. FEBS J. 2005, 272:2477-2486.
    • (2005) FEBS J. , vol.272 , pp. 2477-2486
    • Harada, T.1    Koyama, I.2    Matsunaga, T.3    Kikuno, A.4    Kasahara, T.5    Hassimoto, M.6    Alpers, D.H.7    Komoda, T.8
  • 17
    • 0026713191 scopus 로고
    • Different missense mutations at the tissue-nonspecific alkaline phosphatase gene locus in autosomal recessively inherited forms of mild and severe hypophosphatasia
    • Henthorn P.S., Raducha M., Fedde K., Lafferty M.A., Whyte M.P. Different missense mutations at the tissue-nonspecific alkaline phosphatase gene locus in autosomal recessively inherited forms of mild and severe hypophosphatasia. Proc. Natl. Acad. Sci. USA 1992, 89:9924-9928.
    • (1992) Proc. Natl. Acad. Sci. USA , vol.89 , pp. 9924-9928
    • Henthorn, P.S.1    Raducha, M.2    Fedde, K.3    Lafferty, M.A.4    Whyte, M.P.5
  • 18
    • 0030928122 scopus 로고    scopus 로고
    • Mammalian alkaline phosphatases are allosteric enzymes
    • Hoylaerts M.F., Manes T., Millan J.L. Mammalian alkaline phosphatases are allosteric enzymes. J. Biol. Chem. 1997, 272:22781-22787.
    • (1997) J. Biol. Chem. , vol.272 , pp. 22781-22787
    • Hoylaerts, M.F.1    Manes, T.2    Millan, J.L.3
  • 19
    • 0035106703 scopus 로고    scopus 로고
    • Differentiation of the slow-binding mechanism for magnesium ion activation and zinc ion inhibition of human placental alkaline phosphatase
    • Hung H.C., Chang G.G. Differentiation of the slow-binding mechanism for magnesium ion activation and zinc ion inhibition of human placental alkaline phosphatase. Protein Sci. 2001, 10:34-45.
    • (2001) Protein Sci. , vol.10 , pp. 34-45
    • Hung, H.C.1    Chang, G.G.2
  • 20
    • 0023046909 scopus 로고
    • Preparation of oligodeoxynucleotide-alkaline phosphatase conjugates and their use hybridization probes
    • Jablonski E., Moomaw E.W., Tullis R.H., Ruth J.L. Preparation of oligodeoxynucleotide-alkaline phosphatase conjugates and their use hybridization probes. Nucl. Acids Res. 1986, 14:6115-6128.
    • (1986) Nucl. Acids Res. , vol.14 , pp. 6115-6128
    • Jablonski, E.1    Moomaw, E.W.2    Tullis, R.H.3    Ruth, J.L.4
  • 21
    • 0025777694 scopus 로고
    • Reaction mechanism of alkaline phosphatase based on crystal structures. Two-metal ion catalysis
    • Kim E.E., Wyckoff H.W. Reaction mechanism of alkaline phosphatase based on crystal structures. Two-metal ion catalysis. J. Mol. Biol. 1991, 218:449-464.
    • (1991) J. Mol. Biol. , vol.218 , pp. 449-464
    • Kim, E.E.1    Wyckoff, H.W.2
  • 23
    • 0035937857 scopus 로고    scopus 로고
    • Crystal structure of alkaline phosphatase from human placenta at 1.8Å resolution
    • Le Du M.H., Stigbrand T., Taussig M.J., Menez A., Stura E.A. Crystal structure of alkaline phosphatase from human placenta at 1.8Å resolution. J. Biol. Chem. 2001, 276:9158-9165.
    • (2001) J. Biol. Chem. , vol.276 , pp. 9158-9165
    • Le Du, M.H.1    Stigbrand, T.2    Taussig, M.J.3    Menez, A.4    Stura, E.A.5
  • 25
    • 20444506123 scopus 로고    scopus 로고
    • Structural studies of human placental alkaline phosphatase in complex with functional ligands
    • Llinas P., Stura E.A., Menez A., Kiss Z., Stigbrand T., Millan J.L., Le Du M.H. Structural studies of human placental alkaline phosphatase in complex with functional ligands. J. Mol. Biol. 2005, 350:441-451.
    • (2005) J. Mol. Biol. , vol.350 , pp. 441-451
    • Llinas, P.1    Stura, E.A.2    Menez, A.3    Kiss, Z.4    Stigbrand, T.5    Millan, J.L.6    Le Du, M.H.7
  • 26
    • 4143121255 scopus 로고    scopus 로고
    • Evaluation of fluorescence-based thermal shift assays for hit identification in drug discovery
    • Lo M.C., Aulabaugh A., Jin G.X., Cowling R., Bard J., Malamas M., Ellestad G. Evaluation of fluorescence-based thermal shift assays for hit identification in drug discovery. Anal. Biochem. 2004, 332:153-159.
    • (2004) Anal. Biochem. , vol.332 , pp. 153-159
    • Lo, M.C.1    Aulabaugh, A.2    Jin, G.X.3    Cowling, R.4    Bard, J.5    Malamas, M.6    Ellestad, G.7
  • 27
    • 0026526071 scopus 로고
    • Placental alkaline phosphatase has a binding site for the human immunoglobulin-G FC portion
    • Makiya R., Stigbrand T. Placental alkaline phosphatase has a binding site for the human immunoglobulin-G FC portion. Eur. J. Biochem. 1992, 205:341-345.
    • (1992) Eur. J. Biochem. , vol.205 , pp. 341-345
    • Makiya, R.1    Stigbrand, T.2
  • 28
    • 0032483442 scopus 로고    scopus 로고
    • Genetic complexity, structure, and characterization of highly active bovine intestinal alkaline phosphatases
    • Manes T., Hoylaerts M.F., Muller R., Lottspeich F., Holke W., Millan J.L. Genetic complexity, structure, and characterization of highly active bovine intestinal alkaline phosphatases. J. Biol. Chem. 1998, 273:23353-23360.
    • (1998) J. Biol. Chem. , vol.273 , pp. 23353-23360
    • Manes, T.1    Hoylaerts, M.F.2    Muller, R.3    Lottspeich, F.4    Holke, W.5    Millan, J.L.6
  • 29
    • 0034113511 scopus 로고    scopus 로고
    • Hypophosphatasia: the mutations in the tissue-nonspecific alkaline phosphatase gene
    • Mornet E. Hypophosphatasia: the mutations in the tissue-nonspecific alkaline phosphatase gene. Hum. Mutat. 2000, 15:309-315.
    • (2000) Hum. Mutat. , vol.15 , pp. 309-315
    • Mornet, E.1
  • 30
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data collected in oscillation mode
    • Otwinowski Z., Minor W. Processing of X-ray diffraction data collected in oscillation mode. Method Enzymol. 1997, 276:307-326.
    • (1997) Method Enzymol. , vol.276 , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 33
    • 77955435288 scopus 로고    scopus 로고
    • Refined structures of placental alkaline phosphatase show a consistent pattern of interactions at the peripheral site
    • Stec B., Cheltsov A., Millan J.L. Refined structures of placental alkaline phosphatase show a consistent pattern of interactions at the peripheral site. Acta Crystallogr. 2010, F66:866-870.
    • (2010) Acta Crystallogr. , vol.F66 , pp. 866-870
    • Stec, B.1    Cheltsov, A.2    Millan, J.L.3
  • 35
    • 0029931998 scopus 로고    scopus 로고
    • Kinetic and structural consequences of replacing the aspartate bridge by asparagine in the catalytic metal triad of Escherichia coli alkaline phosphatase
    • Tibbitts T.T., Murphy J.E., Kantrowitz E.R. Kinetic and structural consequences of replacing the aspartate bridge by asparagine in the catalytic metal triad of Escherichia coli alkaline phosphatase. J. Mol. Biol. 1996, 257:700-715.
    • (1996) J. Mol. Biol. , vol.257 , pp. 700-715
    • Tibbitts, T.T.1    Murphy, J.E.2    Kantrowitz, E.R.3
  • 36
    • 0000560808 scopus 로고    scopus 로고
    • MOLREP: an automated program for molecular replacement
    • Vagin A., Teplyakov A. MOLREP: an automated program for molecular replacement. J. Appl. Crystallogr. 1997, vol. 30:1022-1025.
    • (1997) J. Appl. Crystallogr. , vol.30 , pp. 1022-1025
    • Vagin, A.1    Teplyakov, A.2
  • 37
    • 0017170293 scopus 로고
    • Alkaline phosphatase. I. Kinetics and inhibition by levamisole of purified isoenzymes from humans
    • Van Belle H. Alkaline phosphatase. I. Kinetics and inhibition by levamisole of purified isoenzymes from humans. Clin. Chem. 1976, 22:972-976.
    • (1976) Clin. Chem. , vol.22 , pp. 972-976
    • Van Belle, H.1
  • 38
    • 0011322884 scopus 로고
    • A missense mutation in the human liver/bone/kidney alkaline phosphatase gene causing a lethal form of hypophosphatasia
    • Weiss M., Cole D.E.C., Ray K., Whyte M., Laffeerty M.A., Mulivor R.A., Harris H. A missense mutation in the human liver/bone/kidney alkaline phosphatase gene causing a lethal form of hypophosphatasia. Proc. Natl. Acad. Sci. USA 1988, 85:7666-7669.
    • (1988) Proc. Natl. Acad. Sci. USA , vol.85 , pp. 7666-7669
    • Weiss, M.1    Cole, D.E.C.2    Ray, K.3    Whyte, M.4    Laffeerty, M.A.5    Mulivor, R.A.6    Harris, H.7
  • 39
    • 0346299194 scopus 로고    scopus 로고
    • The two isozymes of rat intestinal alkaline phosphatase are products of two distinct genes
    • Xie Q., Alpers D.H. The two isozymes of rat intestinal alkaline phosphatase are products of two distinct genes. Physiol. Genomics 2000, 3:1-8.
    • (2000) Physiol. Genomics , vol.3 , pp. 1-8
    • Xie, Q.1    Alpers, D.H.2
  • 40
    • 0026048285 scopus 로고
    • A water-mediated salt link in the catalytic site of Escherichia coli alkaline phosphatase may influence activity
    • Xu X., Kantrowitz E.R. A water-mediated salt link in the catalytic site of Escherichia coli alkaline phosphatase may influence activity. Biochemistry 1991, 30:7789-7796.
    • (1991) Biochemistry , vol.30 , pp. 7789-7796
    • Xu, X.1    Kantrowitz, E.R.2
  • 41
    • 56949087215 scopus 로고    scopus 로고
    • Comparative enzymology in the alkaline phosphatase superfamily to determine the catalytic role of an active site metal ion
    • Zalatan J.G., Fenn T.D., Herschlag D. Comparative enzymology in the alkaline phosphatase superfamily to determine the catalytic role of an active site metal ion. J. Mol. Biol. 2008, 384:1174-1189.
    • (2008) J. Mol. Biol. , vol.384 , pp. 1174-1189
    • Zalatan, J.G.1    Fenn, T.D.2    Herschlag, D.3
  • 42
    • 29144531187 scopus 로고    scopus 로고
    • Distinct structure and activity recoveries reveal differences in metal binding between mammalian and Escherichia coli alkaline phosphatases
    • Zhang L., Buchet R., Azzar G. Distinct structure and activity recoveries reveal differences in metal binding between mammalian and Escherichia coli alkaline phosphatases. Biochem. J. 2005, 392:407-441.
    • (2005) Biochem. J. , vol.392 , pp. 407-441
    • Zhang, L.1    Buchet, R.2    Azzar, G.3


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