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Volumn 391, Issue 2, 2005, Pages 285-289

Mutating His29, His125, His133 or His 158 abolishes glycosylphosphatidylinositol-specific phospholipase D catalytic activity

Author keywords

propeller domain; Catalytic activity; Glycosylphosphatidylinositol; Histidine; Mutagenesis; Phospholipase D

Indexed keywords

ALCOHOLS; AMINO ACIDS; CATALYSIS; ENZYMES;

EID: 27444433845     PISSN: 02646021     EISSN: None     Source Type: Journal    
DOI: 10.1042/BJ20050656     Document Type: Article
Times cited : (8)

References (33)
  • 1
    • 21844433800 scopus 로고    scopus 로고
    • Enzymes cleaving the phosphodiester bond in the GPI anchor
    • (Hoessli, D. C. and Ilangumaran, S., eds.), R.G. Landes, Austin
    • Low, M. G. and Brodbeck, U. (1999) Enzymes cleaving the phosphodiester bond in the GPI anchor. In GPI-anchored Membrane Proteins and Carbohydrates (Hoessli, D. C. and Ilangumaran, S., eds.), pp. 167-186, R.G. Landes, Austin
    • (1999) GPI-anchored Membrane Proteins and Carbohydrates , pp. 167-186
    • Low, M.G.1    Brodbeck, U.2
  • 2
    • 0028107582 scopus 로고
    • Expression and secretion of glycosylphosphatidylinositol-specific phospholipase D by myeloid cell lines
    • Xie, M. and Low, M. G. (1994) Expression and secretion of glycosylphosphatidylinositol-specific phospholipase D by myeloid cell lines. Biochem. J. 297, 547-554
    • (1994) Biochem. J. , vol.297 , pp. 547-554
    • Xie, M.1    Low, M.G.2
  • 3
    • 0002916646 scopus 로고    scopus 로고
    • Structure and function of GPI-specific phospholipases
    • (Young, N. G. and Moss, J., eds.), Academic Press, San Diego, CA
    • Low, M. G. (2000) Structure and function of GPI-specific phospholipases. In PNH and the GPI-linked Proteins (Young, N. G. and Moss, J., eds.), pp. 239-268, Academic Press, San Diego, CA
    • (2000) PNH and the GPI-linked Proteins , pp. 239-268
    • Low, M.G.1
  • 4
    • 0027377230 scopus 로고
    • Distribution of glycosylphosphatidylinositol-specific phospholipase D mRNA in bovine tissue sections
    • Stadelmann, B., Zurbiggen, A. and Brodbeck, U. (1993) Distribution of glycosylphosphatidylinositol-specific phospholipase D mRNA in bovine tissue sections. Cell Tissue Res. 274, 547-552
    • (1993) Cell Tissue Res. , vol.274 , pp. 547-552
    • Stadelmann, B.1    Zurbiggen, A.2    Brodbeck, U.3
  • 5
    • 0031662709 scopus 로고    scopus 로고
    • Mouse glycosylphosphatidylinositol-specific phospholipase D (Gpld1) characterization
    • LeBoeuf, R. C., Caldwell, M., Guo, Y., Metz, C., Davitz, M. A., Olson, L. K. and Deeg, M. A. (1998) Mouse glycosylphosphatidylinositol-specific phospholipase D (Gpld1) characterization. Mam. Gen. 9, 710-714
    • (1998) Mam. Gen. , vol.9 , pp. 710-714
    • LeBoeuf, R.C.1    Caldwell, M.2    Guo, Y.3    Metz, C.4    Davitz, M.A.5    Olson, L.K.6    Deeg, M.A.7
  • 6
    • 0028324598 scopus 로고
    • An endogenous glycosylphosphatidylinositol-specific phospholipase D releases basic fibroblast growth factor-heparan sulfate proteoglycan complexes from human bone marrow cultures
    • Brunner, G., Metz, C. N., Nguyen, H., Gabrilove, J., Patel, S. R., Davitz, M. A., Rifkin, D. B. and Wilson, E. L. (1994) An endogenous glycosylphosphatidylinositol-specific phospholipase D releases basic fibroblast growth factor-heparan sulfate proteoglycan complexes from human bone marrow cultures. Blood 83, 2115-2125
    • (1994) Blood , vol.83 , pp. 2115-2125
    • Brunner, G.1    Metz, C.N.2    Nguyen, H.3    Gabrilove, J.4    Patel, S.R.5    Davitz, M.A.6    Rifkin, D.B.7    Wilson, E.L.8
  • 7
    • 0026350732 scopus 로고
    • Biosynthesis of carcinoembryonic antigen (CEA) gene family members expressed in human tumor cell lines: Evidence for cleavage of the glycosyl phosphatidyl inositol (GPI) anchor by GPI-PLC and GPI-PLD
    • Khan, W. N. and Hammarstrom, S. (1991) Biosynthesis of carcinoembryonic antigen (CEA) gene family members expressed in human tumor cell lines: evidence for cleavage of the glycosyl phosphatidyl inositol (GPI) anchor by GPI-PLC and GPI-PLD. Biochem. Int. 25, 723-731
    • (1991) Biochem. Int. , vol.25 , pp. 723-731
    • Khan, W.N.1    Hammarstrom, S.2
  • 8
    • 0028075137 scopus 로고
    • Generation by limited proteolysis of a catalytically active 39-kDa protein from the 115-kDa form of phosphatidylinositolglycan-specific phospholipase D from bovine serum
    • Heller, M., Bütikofer, P. and Brodbeck, U. (1994) Generation by limited proteolysis of a catalytically active 39-kDa protein from the 115-kDa form of phosphatidylinositolglycan-specific phospholipase D from bovine serum. Eur. J. Biochem. 224, 823-833
    • (1994) Eur. J. Biochem. , vol.224 , pp. 823-833
    • Heller, M.1    Bütikofer, P.2    Brodbeck, U.3
  • 9
    • 0031013031 scopus 로고    scopus 로고
    • Folding of the N-terminal, ligand-binding region of integrin alpha-subunits into a beta-propeller domain
    • Springer, T. A. (1997) Folding of the N-terminal, ligand-binding region of integrin alpha-subunits into a beta-propeller domain. Proc. Natl. Acad. Sci. U.S.A. 94, 65-72
    • (1997) Proc. Natl. Acad. Sci. U.S.A. , vol.94 , pp. 65-72
    • Springer, T.A.1
  • 10
    • 0035664074 scopus 로고    scopus 로고
    • WD-repeat proteins: Structure characteristics, biological function, and their involvement in human diseases
    • Li, D. and Roberts, R. (2001) WD-repeat proteins: structure characteristics, biological function, and their involvement in human diseases. Cell. Mol. Life Sci. 58, 2085-2097
    • (2001) Cell. Mol. Life Sci. , vol.58 , pp. 2085-2097
    • Li, D.1    Roberts, R.2
  • 11
    • 0037274724 scopus 로고    scopus 로고
    • Beta-propellers: Associated functions and their role in human diseases
    • Pons, T., Gomez, R., Chinea, G. and Valencia, A. (2003) Beta-propellers: associated functions and their role in human diseases. Curr. Med. Chem. 10, 505-524
    • (2003) Curr. Med. Chem. , vol.10 , pp. 505-524
    • Pons, T.1    Gomez, R.2    Chinea, G.3    Valencia, A.4
  • 12
    • 0033570245 scopus 로고    scopus 로고
    • Midportion antibodies stimulate glycosylphosphatidylinositol-specific phospholipase D activity
    • Deeg, M. A. and Bowen, R. F. (1999) Midportion antibodies stimulate glycosylphosphatidylinositol-specific phospholipase D activity. Arch. Biochem. Biophys. 370, 278-284
    • (1999) Arch. Biochem. Biophys. , vol.370 , pp. 278-284
    • Deeg, M.A.1    Bowen, R.F.2
  • 13
    • 0342378149 scopus 로고    scopus 로고
    • The C-terminus of glycosylphosphatidylinositol-specific phospholipase D is essential for biological activity. Biochim
    • Stadelmann, B., Butikofer, P., Konig, A. and Brodbeck, U. (1997) The C-terminus of glycosylphosphatidylinositol-specific phospholipase D is essential for biological activity. Biochim. Biophys. Acta 1355, 107-113
    • (1997) Biophys. Acta , vol.1355 , pp. 107-113
    • Stadelmann, B.1    Butikofer, P.2    Konig, A.3    Brodbeck, U.4
  • 15
    • 0034686027 scopus 로고    scopus 로고
    • The transactivation domain within cysteine/histidine-rich region 1 of CBP comprises two novel zinc-binding modules
    • Newton, A. L., Sharpe, B. K., Kwan, A., Mackay, J. P. and Crossley, M. (2000) The transactivation domain within cysteine/histidine-rich region 1 of CBP comprises two novel zinc-binding modules. J. Biol. Chem. 275, 15128-15134
    • (2000) J. Biol. Chem. , vol.275 , pp. 15128-15134
    • Newton, A.L.1    Sharpe, B.K.2    Kwan, A.3    Mackay, J.P.4    Crossley, M.5
  • 16
    • 0028457594 scopus 로고
    • Zinc mining for protein domains
    • Schwabe, J. W. and Klug, A. (1994) Zinc mining for protein domains. Nat. Struct. Biol. 1, 345-349
    • (1994) Nat. Struct. Biol. , vol.1 , pp. 345-349
    • Schwabe, J.W.1    Klug, A.2
  • 17
    • 0032482941 scopus 로고    scopus 로고
    • Catalytic mechanism of the phospholipase D superfamily proceeds via a covalent phosphohistidine intermediate
    • Gottlin, E. B., Rudolph, A. E., Zhao, Y., Matthews, H. R. and Dixon, J. E. (1998) Catalytic mechanism of the phospholipase D superfamily proceeds via a covalent phosphohistidine intermediate. Proc. Natl. Acad. Sci. U.S.A. 95, 9202-9207
    • (1998) Proc. Natl. Acad. Sci. U.S.A. , vol.95 , pp. 9202-9207
    • Gottlin, E.B.1    Rudolph, A.E.2    Zhao, Y.3    Matthews, H.R.4    Dixon, J.E.5
  • 18
    • 3042686936 scopus 로고    scopus 로고
    • A distant evolutionary relationship between GPI-specific phospholipase D and bacterial phosphatidylcholine-preferring phospholipase C
    • Rigden, D. J. (2004) A distant evolutionary relationship between GPI-specific phospholipase D and bacterial phosphatidylcholine-preferring phospholipase C. FEBS Lett. 569, 229-234
    • (2004) FEBS Lett. , vol.569 , pp. 229-234
    • Rigden, D.J.1
  • 19
    • 0033934808 scopus 로고    scopus 로고
    • Glycosylphosphatidylinositol-specific phospholipase D of human serum activity modulation by naturally occurring amphiphiles
    • Rhode, H., Schulze, M., Cumme, G. A., Gohlert, A., Blume, E., Bublitz, R., Schilling, K. and Horn, A. (2000) Glycosylphosphatidylinositol-specific phospholipase D of human serum activity modulation by naturally occurring amphiphiles. Biol. Chem. 381, 471-485
    • (2000) Biol. Chem. , vol.381 , pp. 471-485
    • Rhode, H.1    Schulze, M.2    Cumme, G.A.3    Gohlert, A.4    Blume, E.5    Bublitz, R.6    Schilling, K.7    Horn, A.8
  • 20
    • 0030803536 scopus 로고    scopus 로고
    • Mutagenesis of phospholipase D defines a superfamily including a trans-Golgi viral protein required for poxvirus pathogenicity
    • Sung, T. C., Roper, R. L., Zhang, Y., Rudge, S. A., Temel, R., Hammond, S. M., Morris, A. J., Moss, B., Engebrecht, J. and Frohman, M. A. (1997) Mutagenesis of phospholipase D defines a superfamily including a trans-Golgi viral protein required for poxvirus pathogenicity. EMBO J. 16, 4519-4530
    • (1997) EMBO J. , vol.16 , pp. 4519-4530
    • Sung, T.C.1    Roper, R.L.2    Zhang, Y.3    Rudge, S.A.4    Temel, R.5    Hammond, S.M.6    Morris, A.J.7    Moss, B.8    Engebrecht, J.9    Frohman, M.A.10
  • 21
    • 0346097951 scopus 로고    scopus 로고
    • Anti-mouse GPI-PLD antisera highlight structural differences between murine and bovine GPI-PLDs
    • Gregory, P., Ziemiecki, A., Zurcher, G., Brodbeck, U. and Butikofer, P. (2003) Anti-mouse GPI-PLD antisera highlight structural differences between murine and bovine GPI-PLDs. Biol. Chem. 384, 1575-1582
    • (2003) Biol. Chem. , vol.384 , pp. 1575-1582
    • Gregory, P.1    Ziemiecki, A.2    Zurcher, G.3    Brodbeck, U.4    Butikofer, P.5
  • 23
    • 0036203636 scopus 로고    scopus 로고
    • Phosphorylation decreases trypsin activation and apolipoprotein al binding to glycosylphosphatidylinositol-specific phospholipase D
    • Deeg, M. A. and Bowen, R. F. (2002) Phosphorylation decreases trypsin activation and apolipoprotein al binding to glycosylphosphatidylinositol- specific phospholipase D. Biochem. Cell. Biol. 80, 253-260
    • (2002) Biochem. Cell. Biol. , vol.80 , pp. 253-260
    • Deeg, M.A.1    Bowen, R.F.2
  • 24
    • 0017632673 scopus 로고
    • Modification of histidyl residues in proteins by diethylpyrocarbonate
    • Miles, E. W. (1977) Modification of histidyl residues in proteins by diethylpyrocarbonate. Methods Enzymol. 47, 431-442
    • (1977) Methods Enzymol. , vol.47 , pp. 431-442
    • Miles, E.W.1
  • 26
    • 0033485263 scopus 로고    scopus 로고
    • Calreticulin functions in vitro as a molecular chaperone for both glycosylated and non-glycosylated proteins
    • Saito, Y., Ihara, Y., Leach, M. R., Cohen-Doyle, M. F. and Williams, D. B. (1999) Calreticulin functions in vitro as a molecular chaperone for both glycosylated and non-glycosylated proteins. EMBO J. 18, 6718-6729
    • (1999) EMBO J. , vol.18 , pp. 6718-6729
    • Saito, Y.1    Ihara, Y.2    Leach, M.R.3    Cohen-Doyle, M.F.4    Williams, D.B.5
  • 27
    • 0039702796 scopus 로고    scopus 로고
    • Mutation of the five conserved histidines in the endothelial nitric-oxide synthase hemoprotein domain. No evidence for a non-heme metal requirement for catalysis
    • Rodriguez-Crespo, I., Nishida, C. R., Knudsen, G. M. and de Montellano, P. R. (1999) Mutation of the five conserved histidines in the endothelial nitric-oxide synthase hemoprotein domain. No evidence for a non-heme metal requirement for catalysis. J. Biol. Chem. 274, 21617-21624
    • (1999) J. Biol. Chem. , vol.274 , pp. 21617-21624
    • Rodriguez-Crespo, I.1    Nishida, C.R.2    Knudsen, G.M.3    De Montellano, P.R.4
  • 28
    • 0038047060 scopus 로고    scopus 로고
    • Electrostatic interactions in leucine zippers: Thermodynamic analysis of the contributions of Glu and His residues and the effect of mutating salt bridges
    • Marti, D. N. and Bosshard, H. R. (2003) Electrostatic interactions in leucine zippers: thermodynamic analysis of the contributions of Glu and His residues and the effect of mutating salt bridges. J. Mol. Biol. 330, 621-637
    • (2003) J. Mol. Biol. , vol.330 , pp. 621-637
    • Marti, D.N.1    Bosshard, H.R.2
  • 29
    • 0345161637 scopus 로고    scopus 로고
    • In vitro phosphorylation of purified glycosylphosphatidylinositol- specific phospholipase D
    • Civenni, G., Butikofer, P., Stadelmann, B. and Brodbeck, U. (1999) In vitro phosphorylation of purified glycosylphosphatidylinositol-specific phospholipase D. Biol. Chem. 380, 585-588
    • (1999) Biol. Chem. , vol.380 , pp. 585-588
    • Civenni, G.1    Butikofer, P.2    Stadelmann, B.3    Brodbeck, U.4
  • 30
    • 0029921149 scopus 로고    scopus 로고
    • A novel family of phospholipase D homologues that includes phospholipid synthases and putative endonucleases: Identification of duplicated repeats and potential active site residues
    • Ponting, C. P. and Kerr, I. D. (1996) A novel family of phospholipase D homologues that includes phospholipid synthases and putative endonucleases: identification of duplicated repeats and potential active site residues. Protein Sci. 5, 914-922
    • (1996) Protein Sci. , vol.5 , pp. 914-922
    • Ponting, C.P.1    Kerr, I.D.2
  • 31
    • 0030200347 scopus 로고    scopus 로고
    • A duplicated catalytic motif in a new superfamily of phosphohydrolases and phospholipid synthases that includes poxvirus envelope proteins
    • Koonin, E. V. (1996) A duplicated catalytic motif in a new superfamily of phosphohydrolases and phospholipid synthases that includes poxvirus envelope proteins. Trends Biochem. Sci. 21, 242-243
    • (1996) Trends Biochem. Sci. , vol.21 , pp. 242-243
    • Koonin, E.V.1
  • 32
    • 0030054720 scopus 로고    scopus 로고
    • Lipoprotein lipase binds to low density lipoprotein receptors and induces receptor-mediated catabolism of very low density lipoproteins in vitro
    • Medh, J. D., Bowen, S. L., Fry, G. L., Ruben, S., Andracki, M., Inoue, I., Lalouel, J. M., Strickland, D. K. and Chapped, D. A. (1996) Lipoprotein lipase binds to low density lipoprotein receptors and induces receptor-mediated catabolism of very low density lipoproteins in vitro. J. Biol. Chem. 271, 17073-17080
    • (1996) J. Biol. Chem. , vol.271 , pp. 17073-17080
    • Medh, J.D.1    Bowen, S.L.2    Fry, G.L.3    Ruben, S.4    Andracki, M.5    Inoue, I.6    Lalouel, J.M.7    Strickland, D.K.8    Chapped, D.A.9
  • 33
    • 0032506219 scopus 로고    scopus 로고
    • Catalytically inactive lipoprotein lipase expression in muscle of transgenic mice increases very low density lipoprotein uptake: Direct evidence that lipoprotein lipase bridging occurs in vivo
    • Merkel, M., Kako, Y., Radner, H., Cho, I. S., Ramasamy, R., Brunzell, J. D., Goldberg, I. J. and Breslow, J. L. (1998) Catalytically inactive lipoprotein lipase expression in muscle of transgenic mice increases very low density lipoprotein uptake: direct evidence that lipoprotein lipase bridging occurs in vivo. Proc. Natl. Acad. Sci. U.S.A. 95, 13841-13846
    • (1998) Proc. Natl. Acad. Sci. U.S.A. , vol.95 , pp. 13841-13846
    • Merkel, M.1    Kako, Y.2    Radner, H.3    Cho, I.S.4    Ramasamy, R.5    Brunzell, J.D.6    Goldberg, I.J.7    Breslow, J.L.8


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