메뉴 건너뛰기




Volumn 583, Issue 19, 2009, Pages 3280-3284

Diphosphonucleotide phosphatase/phosphodiesterase (PPD1) from yellow lupin (Lupinus luteus L.) contains an iron-manganese center

Author keywords

Diphosphonucleotide phosphatase; Fe Mn center; Phosphodiesterase; PPD; Purple acid phosphatase

Indexed keywords

ACID PHOSPHATASE TARTRATE RESISTANT ISOENZYME; AMINO ACID; DIPHOSPHONUCLEOTIDE PHOSPHATASE; IRON; MANGANESE; PHOSPHATASE; PHOSPHODIESTERASE; UNCLASSIFIED DRUG;

EID: 70349466506     PISSN: 00145793     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.febslet.2009.09.024     Document Type: Article
Times cited : (13)

References (34)
  • 2
    • 0030596529 scopus 로고    scopus 로고
    • Mechanism of Fe(III)-Zn(II) purple acid phosphatase based on crystal structures
    • Klabunde T., Strater N., Frohlich R., Witzel H., and Krebs B. Mechanism of Fe(III)-Zn(II) purple acid phosphatase based on crystal structures. J. Mol. Biol. 259 (1996) 737-748
    • (1996) J. Mol. Biol. , vol.259 , pp. 737-748
    • Klabunde, T.1    Strater, N.2    Frohlich, R.3    Witzel, H.4    Krebs, B.5
  • 3
    • 2342470541 scopus 로고    scopus 로고
    • Plant purple acid phosphatases - genes, structures and biological function
    • Olczak M., Morawiecka B., and Watorek W. Plant purple acid phosphatases - genes, structures and biological function. Acta Biochim. Pol. 50 (2003) 1245-1256
    • (2003) Acta Biochim. Pol. , vol.50 , pp. 1245-1256
    • Olczak, M.1    Morawiecka, B.2    Watorek, W.3
  • 4
  • 5
    • 0342547111 scopus 로고    scopus 로고
    • Purification and characterization of acid phosphatase from yellow lupin (Lupinus luteus) seeds
    • Olczak M., Watorek W., and Morawiecka B. Purification and characterization of acid phosphatase from yellow lupin (Lupinus luteus) seeds. Biochim. Biophys. Acta 1341 (1997) 14-25
    • (1997) Biochim. Biophys. Acta , vol.1341 , pp. 14-25
    • Olczak, M.1    Watorek, W.2    Morawiecka, B.3
  • 6
    • 0032420375 scopus 로고    scopus 로고
    • Oligosaccharide and polypeptide homology of lupin (Lupinus luteus) acid phosphatase subunits
    • Olczak M., and Watorek W. Oligosaccharide and polypeptide homology of lupin (Lupinus luteus) acid phosphatase subunits. Arch. Biochem. Biophys. 360 (1998) 85-92
    • (1998) Arch. Biochem. Biophys. , vol.360 , pp. 85-92
    • Olczak, M.1    Watorek, W.2
  • 7
    • 0041566980 scopus 로고    scopus 로고
    • Two subfamilies of plant purple acid phosphatases
    • Olczak M., and Watorek W. Two subfamilies of plant purple acid phosphatases. Physiol. Plant. 118 (2003) 491-498
    • (2003) Physiol. Plant. , vol.118 , pp. 491-498
    • Olczak, M.1    Watorek, W.2
  • 8
    • 0034705065 scopus 로고    scopus 로고
    • Characterization of diphosphonucleotide phosphatase/phosphodiesterase from yellow lupin (Lupinus luteus) seeds
    • Olczak M., Kobialka M., and Watorek W. Characterization of diphosphonucleotide phosphatase/phosphodiesterase from yellow lupin (Lupinus luteus) seeds. Biochim. Biophys. Acta 1478 (2000) 239-247
    • (2000) Biochim. Biophys. Acta , vol.1478 , pp. 239-247
    • Olczak, M.1    Kobialka, M.2    Watorek, W.3
  • 9
    • 0034684249 scopus 로고    scopus 로고
    • Structural analysis of N-glycans from yellow lupin (Lupinus luteus) seed diphosphonucleotide phosphatase/phosphodiesterase
    • Olczak M., and Watorek W. Structural analysis of N-glycans from yellow lupin (Lupinus luteus) seed diphosphonucleotide phosphatase/phosphodiesterase. Biochim. Biophys. Acta 1523 (2000) 236-245
    • (2000) Biochim. Biophys. Acta , vol.1523 , pp. 236-245
    • Olczak, M.1    Watorek, W.2
  • 10
    • 0037157181 scopus 로고    scopus 로고
    • Diphosphonucleotide phosphatase/phosphodiesterase from yellow lupin (Lupinus luteus) belongs to a novel group of specific metallophosphatases
    • Olczak M., and Olczak T. Diphosphonucleotide phosphatase/phosphodiesterase from yellow lupin (Lupinus luteus) belongs to a novel group of specific metallophosphatases. FEBS Lett. 519 (2002) 159-163
    • (2002) FEBS Lett. , vol.519 , pp. 159-163
    • Olczak, M.1    Olczak, T.2
  • 11
    • 10644280143 scopus 로고    scopus 로고
    • Expression and purification of active plant diphosphonucleotide phosphatase/phosphodiesterase from baculovirus-infected insect cells
    • Olczak M., and Olczak T. Expression and purification of active plant diphosphonucleotide phosphatase/phosphodiesterase from baculovirus-infected insect cells. Protein Expr. Purif. 39 (2005) 116-123
    • (2005) Protein Expr. Purif. , vol.39 , pp. 116-123
    • Olczak, M.1    Olczak, T.2
  • 13
    • 0035830739 scopus 로고    scopus 로고
    • Two isoforms of a nucleotide-sugar pyrophosphatase/phosphodiesterase from barley leaves (Hordeum vulgare L.) are distinct oligomers of HvGLP1, a germin-like protein
    • Rodriguez-Lopez M., Baroja-Fernandez E., Zandueta-Criado A., Moreno-Bruna B., Munoz F.J., Akazawa T., and Pozueta-Romero J. Two isoforms of a nucleotide-sugar pyrophosphatase/phosphodiesterase from barley leaves (Hordeum vulgare L.) are distinct oligomers of HvGLP1, a germin-like protein. FEBS Lett. 490 (2001) 44-48
    • (2001) FEBS Lett. , vol.490 , pp. 44-48
    • Rodriguez-Lopez, M.1    Baroja-Fernandez, E.2    Zandueta-Criado, A.3    Moreno-Bruna, B.4    Munoz, F.J.5    Akazawa, T.6    Pozueta-Romero, J.7
  • 15
    • 0001431264 scopus 로고    scopus 로고
    • Binuclear metallohydrolases
    • Wilcox D.E. Binuclear metallohydrolases. Chem. Rev. 96 (1996) 2435-2458
    • (1996) Chem. Rev. , vol.96 , pp. 2435-2458
    • Wilcox, D.E.1
  • 17
    • 0033559677 scopus 로고    scopus 로고
    • The active site of purple acid phosphatase from sweet potatoes (Ipomoea batatas) metal content and spectroscopic characterization
    • Durmus A., Eicken C., Sift B.H., Kratel A., Kappl R., Huttermann J., and Krebs B. The active site of purple acid phosphatase from sweet potatoes (Ipomoea batatas) metal content and spectroscopic characterization. Eur. J. Biochem. 260 (1999) 709-716
    • (1999) Eur. J. Biochem. , vol.260 , pp. 709-716
    • Durmus, A.1    Eicken, C.2    Sift, B.H.3    Kratel, A.4    Kappl, R.5    Huttermann, J.6    Krebs, B.7
  • 19
    • 56949108503 scopus 로고    scopus 로고
    • Purple acid phosphatase in the wall of tobacco cells
    • Kaida R., Hayashi T., and Kaneko T.S. Purple acid phosphatase in the wall of tobacco cells. Phytochemistry 69 (2008) 2546-25551
    • (2008) Phytochemistry , vol.69 , pp. 2546-25551
    • Kaida, R.1    Hayashi, T.2    Kaneko, T.S.3
  • 20
    • 33646859762 scopus 로고    scopus 로고
    • Recombinant purple acid phosphatase isoform 3 from sweet potato is an enzyme with a diiron metal center
    • Waratrujiwong T., Krebs B., Spener F., and Visoottiviseth P. Recombinant purple acid phosphatase isoform 3 from sweet potato is an enzyme with a diiron metal center. FEBS J. 273 (2006) 1649-1659
    • (2006) FEBS J. , vol.273 , pp. 1649-1659
    • Waratrujiwong, T.1    Krebs, B.2    Spener, F.3    Visoottiviseth, P.4
  • 21
    • 0029640070 scopus 로고
    • Crystal structure of a purple acid phosphatase containing a dinuclear Fe(III)-Zn(II) active site
    • Strater N., Klabunde T., Tucker P., Witzel H., and Krebs B. Crystal structure of a purple acid phosphatase containing a dinuclear Fe(III)-Zn(II) active site. Science 268 (1995) 1489-1492
    • (1995) Science , vol.268 , pp. 1489-1492
    • Strater, N.1    Klabunde, T.2    Tucker, P.3    Witzel, H.4    Krebs, B.5
  • 24
    • 35948930227 scopus 로고    scopus 로고
    • Synthesis and characterization of the tetranuclear iron(III) complex of a new asymmetric multidentate ligand. A structural model for purple acid phosphatases
    • Boudalis A.K., Aston R.E., Smith S.J., Mirams R.E., Riley M.J., Schenk G., Blackman A.G., Hanton L.R., and Gahan L.R. Synthesis and characterization of the tetranuclear iron(III) complex of a new asymmetric multidentate ligand. A structural model for purple acid phosphatases. Dalton Trans. 44 (2007) 5132-5139
    • (2007) Dalton Trans. , vol.44 , pp. 5132-5139
    • Boudalis, A.K.1    Aston, R.E.2    Smith, S.J.3    Mirams, R.E.4    Riley, M.J.5    Schenk, G.6    Blackman, A.G.7    Hanton, L.R.8    Gahan, L.R.9
  • 25
    • 33750632730 scopus 로고    scopus 로고
    • Comparison of different signal peptides for protein secretion in non-lytic insect cell system
    • Olczak M., and Olczak T. Comparison of different signal peptides for protein secretion in non-lytic insect cell system. Anal. Biochem. 359 (2006) 45-53
    • (2006) Anal. Biochem. , vol.359 , pp. 45-53
    • Olczak, M.1    Olczak, T.2
  • 26
    • 0030339738 scopus 로고    scopus 로고
    • AQUA and PROCHECK-NMR: programs for checking the quality of protein structures solved by NMR
    • Laskowski R.A., Rullmann J.A., MacArthur M.W., Kaptein R., and Thornton J.M. AQUA and PROCHECK-NMR: programs for checking the quality of protein structures solved by NMR. J. Biomol. NMR 8 (1996) 477-486
    • (1996) J. Biomol. NMR , vol.8 , pp. 477-486
    • Laskowski, R.A.1    Rullmann, J.A.2    MacArthur, M.W.3    Kaptein, R.4    Thornton, J.M.5
  • 27
    • 0026610767 scopus 로고
    • Assessment of protein models with three-dimensional profiles
    • Luthy R., Bowie J.U., and Eisenberg D. Assessment of protein models with three-dimensional profiles. Nature 35 (1992) 83-85
    • (1992) Nature , vol.35 , pp. 83-85
    • Luthy, R.1    Bowie, J.U.2    Eisenberg, D.3
  • 28
    • 0019888476 scopus 로고
    • Purification, enzymatic properties, and active site environment of a novel manganese(III)-containing acid phosphatase
    • Sugiura Y., Kawabe H., Tanaka H., Fujimoto S., and Ohara A. Purification, enzymatic properties, and active site environment of a novel manganese(III)-containing acid phosphatase. J. Biol. Chem. 256 (1981) 10664-10670
    • (1981) J. Biol. Chem. , vol.256 , pp. 10664-10670
    • Sugiura, Y.1    Kawabe, H.2    Tanaka, H.3    Fujimoto, S.4    Ohara, A.5
  • 29
    • 0023653239 scopus 로고
    • The "manganese(III)-containing" purple acid phosphatase from sweet potatoes is an iron enzyme
    • Hefler S.K., and Averill B.A. The "manganese(III)-containing" purple acid phosphatase from sweet potatoes is an iron enzyme. Biochem. Biophys. Res. Commun. 146 (1987) 1173-1177
    • (1987) Biochem. Biophys. Res. Commun. , vol.146 , pp. 1173-1177
    • Hefler, S.K.1    Averill, B.A.2
  • 30
    • 0032990435 scopus 로고    scopus 로고
    • Irreversible inactivation of purple acid phosphatase by hydrogen peroxide and ascorbate
    • Beck J.L., Durack M.C.A., Hamilton S.E., and de Jersey J. Irreversible inactivation of purple acid phosphatase by hydrogen peroxide and ascorbate. J. Inorg. Biochem. 73 (1999) 245-252
    • (1999) J. Inorg. Biochem. , vol.73 , pp. 245-252
    • Beck, J.L.1    Durack, M.C.A.2    Hamilton, S.E.3    de Jersey, J.4
  • 31
    • 0033520085 scopus 로고    scopus 로고
    • Evidence for nonbridged coordination for p-nitrophenyl phosphate to the dinuclear Fe(III)-M(II) center in bovine spleen purple acid phosphatase during enzymatic turnover
    • Merkx M., Pinkse M.W.H., and Averill B.A. Evidence for nonbridged coordination for p-nitrophenyl phosphate to the dinuclear Fe(III)-M(II) center in bovine spleen purple acid phosphatase during enzymatic turnover. Biochemistry 38 (1999) 9914-9925
    • (1999) Biochemistry , vol.38 , pp. 9914-9925
    • Merkx, M.1    Pinkse, M.W.H.2    Averill, B.A.3
  • 32
    • 22744439891 scopus 로고    scopus 로고
    • Structure-function relationships of purple acid phosphatase from red kidney beans based on heterologously expressed mutants
    • Truong N.T., Naseri J.I., Vogel A., Rompel A., and Krebs B. Structure-function relationships of purple acid phosphatase from red kidney beans based on heterologously expressed mutants. Arch. Biochem. Biophys. 440 (2005) 38-45
    • (2005) Arch. Biochem. Biophys. , vol.440 , pp. 38-45
    • Truong, N.T.1    Naseri, J.I.2    Vogel, A.3    Rompel, A.4    Krebs, B.5
  • 33
    • 0029003660 scopus 로고
    • Structural relationship between the mammalian Fe(III)-Fe(II) and the Fe(III)-Zn(II) plant purple acid phosphatases
    • Klabunde T., Strater N., Krebs B., and Witzel H. Structural relationship between the mammalian Fe(III)-Fe(II) and the Fe(III)-Zn(II) plant purple acid phosphatases. FEBS Lett. 367 (1995) 56-60
    • (1995) FEBS Lett. , vol.367 , pp. 56-60
    • Klabunde, T.1    Strater, N.2    Krebs, B.3    Witzel, H.4
  • 34
    • 0032063303 scopus 로고    scopus 로고
    • Presence of a fibronectin type III domain in a plant protein
    • Tsyguelnaia I., and Doolittle R.F. Presence of a fibronectin type III domain in a plant protein. J. Mol. Evol. 46 (1998) 612-614
    • (1998) J. Mol. Evol. , vol.46 , pp. 612-614
    • Tsyguelnaia, I.1    Doolittle, R.F.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.