메뉴 건너뛰기




Volumn 259, Issue 4, 1996, Pages 737-748

Mechanism of Fe(III)-Zn(II) purple acid phosphatase based on crystal structures

Author keywords

Metallophosphoesterases; Purple acid phosphatase; Signature sequence; Two metal ion mechanism; X ray crystallography

Indexed keywords

ACID PHOSPHATASE; ANION; FERRIC ION; ZINC;

EID: 0030596529     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1006/jmbi.1996.0354     Document Type: Article
Times cited : (328)

References (41)
  • 1
    • 37049073676 scopus 로고
    • Mechanism of the reaction of different phosphates with the iron(II)iron(III) form of purple acid phosphatase from porcine uteri (uteroferrin)
    • Aquino, M. A. S., Lim, J.-S. & Sykes, A. G. (1994). Mechanism of the reaction of different phosphates with the iron(II)iron(III) form of purple acid phosphatase from porcine uteri (uteroferrin). J. Chem. Soc. Dalton Trans. 429-436.
    • (1994) J. Chem. Soc. Dalton Trans. , pp. 429-436
    • Aquino, M.A.S.1    Lim, J.-S.2    Sykes, A.G.3
  • 2
    • 0021967168 scopus 로고
    • Effects of perturbants on the pink (reduced) active form of uteroferrin
    • Antanaitis, B. C. & Aisen, P. (1985). Effects of perturbants on the pink (reduced) active form of uteroferrin. J. Biol. Chem. 260, 751-756.
    • (1985) J. Biol. Chem. , vol.260 , pp. 751-756
    • Antanaitis, B.C.1    Aisen, P.2
  • 3
    • 0000913086 scopus 로고
    • A fast algorithm of rendering space-filling molecule pictures
    • Bacon, D. J. & Andersen, W. F. (1988). A fast algorithm of rendering space-filling molecule pictures. J. Mol. Graphics, 6, 219-220.
    • (1988) J. Mol. Graphics , vol.6 , pp. 219-220
    • Bacon, D.J.1    Andersen, W.F.2
  • 5
    • 0000947693 scopus 로고
    • Properties of the Fe(II)-Fe(III) derivative of red kidney bean purple phosphatase. Evidence for a binuclear Zn-Fe center in the native enzyme
    • Beck, J. L., de Jersey, J., Zerner, B., Hendrich, M. P. & Debrunner, P. G. (1988). Properties of the Fe(II)-Fe(III) derivative of red kidney bean purple phosphatase. Evidence for a binuclear Zn-Fe center in the native enzyme. J. Am. Chem. Soc. 110, 3317-3318.
    • (1988) J. Am. Chem. Soc. , vol.110 , pp. 3317-3318
    • Beck, J.L.1    De Jersey, J.2    Zerner, B.3    Hendrich, M.P.4    Debrunner, P.G.5
  • 6
    • 85030202686 scopus 로고
    • Magnetic investigations on the active site of purple acid phosphatase from kidney-beans (PAP), a 2 Fe-enzyme
    • Behlendorf, M., Fleischhauer, P., Haase, W., Löcke, R. & Witzel, H. (1995). Magnetic investigations on the active site of purple acid phosphatase from kidney-beans (PAP), a 2 Fe-enzyme. J. Inorg. Biochem. 59, 380.
    • (1995) J. Inorg. Biochem. , vol.59 , pp. 380
    • Behlendorf, M.1    Fleischhauer, P.2    Haase, W.3    Löcke, R.4    Witzel, H.5
  • 8
    • 0022534103 scopus 로고
    • The interaction of phosphate with the purple acid phosphatase from beef spleen: Evidence that phosphate binding is accompanied by oxidation of the iron chromophore
    • Burman, S., Davis, J. C., Weber, H. J. & Averill, B. A. (1986). The interaction of phosphate with the purple acid phosphatase from beef spleen: evidence that phosphate binding is accompanied by oxidation of the iron chromophore. Biochem. Biophys. Res. Commun. 136, 490-497.
    • (1986) Biochem. Biophys. Res. Commun. , vol.136 , pp. 490-497
    • Burman, S.1    Davis, J.C.2    Weber, H.J.3    Averill, B.A.4
  • 9
    • 0026472146 scopus 로고
    • Interaction of porcine uterine fluid purple acid phosphatase with vanadate and vanadyl cation
    • Crans, D. C., Simone, C. M., Holz, R. C. & Que, L. Jr (1992). Interaction of porcine uterine fluid purple acid phosphatase with vanadate and vanadyl cation. Biochemistry, 31, 11731-11739.
    • (1992) Biochemistry , vol.31 , pp. 11731-11739
    • Crans, D.C.1    Simone, C.M.2    Holz, R.C.3    Que L., Jr.4
  • 10
    • 0025162350 scopus 로고
    • Anion binding to uteroferrin. Evidence for phosphate coordination to the iron(III) ion of the dinuclear active site and interaction with the hydroxo bridge
    • David, S. S. & Que, L. Jr (1990) Anion binding to uteroferrin. Evidence for phosphate coordination to the iron(III) ion of the dinuclear active site and interaction with the hydroxo bridge. J. Am. Chem. Soc. 112, 6455-6463.
    • (1990) J. Am. Chem. Soc. , vol.112 , pp. 6455-6463
    • David, S.S.1    Que L., Jr.2
  • 11
    • 0025909426 scopus 로고
    • Purple acid phosphatase from bovine spleen. Interactions at the active site in relation to the reaction mechanism
    • Dietrich, M., Münstermann, D., Suerbaum, H. & Witzel, H. (1991). Purple acid phosphatase from bovine spleen. Interactions at the active site in relation to the reaction mechanism. Eur. J. Biochem. 199, 105-113.
    • (1991) Eur. J. Biochem. , vol.199 , pp. 105-113
    • Dietrich, M.1    Münstermann, D.2    Suerbaum, H.3    Witzel, H.4
  • 12
    • 0023664464 scopus 로고
    • Spectroscopic studies on the interaction of phosphate with uteroferrin
    • Doi, K., Gupta, R. & Aisen, P. (1987). Spectroscopic studies on the interaction of phosphate with uteroferrin. J. Biol. Chem. 262, 6982-6985.
    • (1987) J. Biol. Chem. , vol.262 , pp. 6982-6985
    • Doi, K.1    Gupta, R.2    Aisen, P.3
  • 13
    • 0002272476 scopus 로고
    • The binuclear iron centers of uteroferrin and the purple acid phosphatases
    • Doi, K., Antanaitis, B. L. & Aisen, P. (1988a). The binuclear iron centers of uteroferrin and the purple acid phosphatases. Struct. Bonding, 70, 1-26.
    • (1988) Struct. Bonding , vol.70 , pp. 1-26
    • Doi, K.1    Antanaitis, B.L.2    Aisen, P.3
  • 15
    • 0028181017 scopus 로고
    • An algorithm for automatically generating protein topology cartoons
    • Flores, T. P., Moss, D. S. & Thornton, J. (1994). An algorithm for automatically generating protein topology cartoons. Protein Eng. 7, 31-37.
    • (1994) Protein Eng. , vol.7 , pp. 31-37
    • Flores, T.P.1    Moss, D.S.2    Thornton, J.3
  • 16
    • 0029094754 scopus 로고
    • Three-dimensional structure of the catalytic subunit of protein serine/threonine phosphatase-1
    • Goldberg, J., Huang, H., Kwon, Y., Greengard, P., Nairn, A. C. & Kuriyan, J. (1995). Three-dimensional structure of the catalytic subunit of protein serine/threonine phosphatase-1. Nature, 376, 745-753.
    • (1995) Nature , vol.376 , pp. 745-753
    • Goldberg, J.1    Huang, H.2    Kwon, Y.3    Greengard, P.4    Nairn, A.C.5    Kuriyan, J.6
  • 18
    • 0028009805 scopus 로고
    • Purple acid phosphatase of the human macrophage and osteoclast
    • Hayman, A. R. & Cox, T. M. (1994). Purple acid phosphatase of the human macrophage and osteoclast. J. Biol. Chem. 269, 1294-1300.
    • (1994) J. Biol. Chem. , vol.269 , pp. 1294-1300
    • Hayman, A.R.1    Cox, T.M.2
  • 19
    • 84889120137 scopus 로고
    • Improved methods for building protein models in electron density maps and the location of errors in these models
    • Jones, T. A., Zou, J.-Y. & Cowan, S. W. (1991). Improved methods for building protein models in electron density maps and the location of errors in these models. Acta Crystallogr. sect. A, 47, 110-119.
    • (1991) Acta Crystallogr. Sect. A , vol.47 , pp. 110-119
    • Jones, T.A.1    Zou, J.-Y.2    Cowan, S.W.3
  • 21
    • 0027988448 scopus 로고
    • The amino acid sequence of the red kidney bean Fe(III)-Zn(II) purple acid phosphatase. Determination of the amino acid sequence by a combination of matrix-assisted laser desorption/ionization mass spectrometry and automated Edman sequencing
    • Klabunde, T., Stahl, B., Suerbaum, H., Hahner, S., Karas, M., Hillenkamp, F., Krebs, B. & Witzel, H. (1994). The amino acid sequence of the red kidney bean Fe(III)-Zn(II) purple acid phosphatase. Determination of the amino acid sequence by a combination of matrix-assisted laser desorption/ionization mass spectrometry and automated Edman sequencing. Eur. J. Biochem. 226, 369-375.
    • (1994) Eur. J. Biochem. , vol.226 , pp. 369-375
    • Klabunde, T.1    Stahl, B.2    Suerbaum, H.3    Hahner, S.4    Karas, M.5    Hillenkamp, F.6    Krebs, B.7    Witzel, H.8
  • 22
    • 0029003660 scopus 로고
    • Structural relationship between the mammalian Fe(III)-Fe(II) and the Fe(III)-Zn(II) plant purple acid phosphatases
    • Klabunde, T., Sträter, N., Krebs, B. & Witzel, H. (1995). Structural relationship between the mammalian Fe(III)-Fe(II) and the Fe(III)-Zn(II) plant purple acid phosphatases. FEBS Letters, 367, 56-60.
    • (1995) FEBS Letters , vol.367 , pp. 56-60
    • Klabunde, T.1    Sträter, N.2    Krebs, B.3    Witzel, H.4
  • 23
    • 0028268627 scopus 로고
    • Conserved sequence pattern in a wide variety of phosphoesterases
    • Koonin, E. V. (1994). Conserved sequence pattern in a wide variety of phosphoesterases. Protein Sci. 3, 356-358.
    • (1994) Protein Sci. , vol.3 , pp. 356-358
    • Koonin, E.V.1
  • 25
    • 0026244229 scopus 로고
    • Molscript: A program to produce both detailed and schematic plots of protein structures
    • Kraulis, P. (1991). Molscript: a program to produce both detailed and schematic plots of protein structures. J. Appl. Crystallog. 24, 946-950.
    • (1991) J. Appl. Crystallog. , vol.24 , pp. 946-950
    • Kraulis, P.1
  • 26
    • 0022849991 scopus 로고
    • Mechanistic aspects of the low-molecular-weight phosphatase acitivity of the calmodulin-activated phosphatase calcineurin
    • Martin, B. L. & Graves, D. J. (1986). Mechanistic aspects of the low-molecular-weight phosphatase acitivity of the calmodulin-activated phosphatase calcineurin. J. Biol. Chem. 261, 14545-14550.
    • (1986) J. Biol. Chem. , vol.261 , pp. 14545-14550
    • Martin, B.L.1    Graves, D.J.2
  • 27
    • 0028337360 scopus 로고
    • Isotope effects on the mechanism of calcineurin catalysis: Kinetic solvent isotope and isotope exchange studies
    • Martin, B. L. & Graves, D. J. (1994). Isotope effects on the mechanism of calcineurin catalysis: kinetic solvent isotope and isotope exchange studies. Biochim. Biophys. Acta, 1206, 136-142.
    • (1994) Biochim. Biophys. Acta , vol.1206 , pp. 136-142
    • Martin, B.L.1    Graves, D.J.2
  • 28
    • 85021609916 scopus 로고
    • Purple acid phosphatase: A diiron enzyme that catalyzes a direct phospho group transfer to water
    • Mueller, E. G., Crowder, M. W., Averill, B. A. & Knowles, J. R. (1993). Purple acid phosphatase: a diiron enzyme that catalyzes a direct phospho group transfer to water. J. Am. Chem. Soc. 115, 2974-2975.
    • (1993) J. Am. Chem. Soc. , vol.115 , pp. 2974-2975
    • Mueller, E.G.1    Crowder, M.W.2    Averill, B.A.3    Knowles, J.R.4
  • 29
    • 0026319199 scopus 로고
    • Protein folding and association: Insights from the interfacial and thermodynamic properties of hydrocarbons
    • Nicholls, A., Sharp, K. A. & Honig, B. (1991). Protein folding and association: insights from the interfacial and thermodynamic properties of hydrocarbons. Proteins: Struct. Funct. Genet. 11, 281-296.
    • (1991) Proteins: Struct. Funct. Genet. , vol.11 , pp. 281-296
    • Nicholls, A.1    Sharp, K.A.2    Honig, B.3
  • 30
    • 0023002899 scopus 로고
    • The interaction of phosphate with uteroferrin. Charaterization of a reduced uteroferrin-phosphate complex
    • Pyrz, J. W., Sage, J. T., Debrunner, P. G. & Que, L. Jr (1986). The interaction of phosphate with uteroferrin. Charaterization of a reduced uteroferrin-phosphate complex. J. Biol. Chem. 261, 11015-11020.
    • (1986) J. Biol. Chem. , vol.261 , pp. 11015-11020
    • Pyrz, J.W.1    Sage, J.T.2    Debrunner, P.G.3    Que L., Jr.4
  • 31
    • 0003098544 scopus 로고
    • Dinuclear iron- and manganese-oxo sites in biology
    • Que, L. Jr & True, A. E. (1990). Dinuclear iron- and manganese-oxo sites in biology. Prog. Inorg. Chem. 38, 97-200.
    • (1990) Prog. Inorg. Chem. , vol.38 , pp. 97-200
    • Que L., Jr.1    True, A.E.2
  • 32
    • 0025285237 scopus 로고
    • NMR Studies of the dinuclear iron site in reduced uteroferrin and its oxoanion complexes
    • Scarrow, R. C., Pyrz, J. W. & Que, L. Jr (1990). NMR Studies of the dinuclear iron site in reduced uteroferrin and its oxoanion complexes. J. Am. Chem. Soc. 112, 657-665.
    • (1990) J. Am. Chem. Soc. , vol.112 , pp. 657-665
    • Scarrow, R.C.1    Pyrz, J.W.2    Que L., Jr.3
  • 33
    • 0026538492 scopus 로고
    • Crystallization and prelimary crystallographic data of purple acid phosphatase from red kidney bean
    • Sträter, N., Fröhlich, R., Schiemann, A., Krebs, B., Körner, M., Suerbaum, H. & Witzel, H. (1992). Crystallization and prelimary crystallographic data of purple acid phosphatase from red kidney bean. J. Mol. Biol. 224, 511-513.
    • (1992) J. Mol. Biol. , vol.224 , pp. 511-513
    • Sträter, N.1    Fröhlich, R.2    Schiemann, A.3    Krebs, B.4    Körner, M.5    Suerbaum, H.6    Witzel, H.7
  • 34
    • 0029640070 scopus 로고
    • Crystal structure of a purple acid phosphatase containing a dinuclear Fe(III)-Zn(II) active site
    • Sträter, N., Klabunde, T., Tucker, P., Witzel, H. & Krebs, B. (1995). Crystal structure of a purple acid phosphatase containing a dinuclear Fe(III)-Zn(II) active site. Science, 268, 1489-1492.
    • (1995) Science , vol.268 , pp. 1489-1492
    • Sträter, N.1    Klabunde, T.2    Tucker, P.3    Witzel, H.4    Krebs, B.5
  • 35
    • 0027336220 scopus 로고
    • Zn-exchange and Mössbauer studies on the [Fe-Fe] derivatives of the purple acid Fe(III)-Zn(II)-phosphatase from kidney beans
    • Suerbaum, H., Körner, M., Witzel, H., Althaus, E., Mosel, B.-D. & Müller-Warmuth, W. (1993). Zn-exchange and Mössbauer studies on the [Fe-Fe] derivatives of the purple acid Fe(III)-Zn(II)-phosphatase from kidney beans. Eur. J. Biochem. 269, 313-321.
    • (1993) Eur. J. Biochem. , vol.269 , pp. 313-321
    • Suerbaum, H.1    Körner, M.2    Witzel, H.3    Althaus, E.4    Mosel, B.-D.5    Müller-Warmuth, W.6
  • 37
    • 0008116110 scopus 로고
    • Proteins containing oxo-bridged dinuclear iron centers: A bioinorganic perspective
    • Vincent, J. B., Olivier-Lilley, G. L. & Averill, B. A. (1991a). Proteins containing oxo-bridged dinuclear iron centers: a bioinorganic perspective. Chem. Rev. 90, 1447-1467.
    • (1991) Chem. Rev. , vol.90 , pp. 1447-1467
    • Vincent, J.B.1    Olivier-Lilley, G.L.2    Averill, B.A.3
  • 38
    • 0025803775 scopus 로고
    • Spectroscopic and kinetic studies of a high-salt-stabilized form of the purple acid phosphatase from bovine spleen
    • Vincent, J. B., Crowder, M. W. & Averill, B. A. (1991b). Spectroscopic and kinetic studies of a high-salt-stabilized form of the purple acid phosphatase from bovine spleen. Biochemistry, 30, 3025-3034.
    • (1991) Biochemistry , vol.30 , pp. 3025-3034
    • Vincent, J.B.1    Crowder, M.W.2    Averill, B.A.3
  • 41
    • 0027944142 scopus 로고
    • Mutational analysis of a Ser/Thr phosphatase. Identification of residues important in phosphoesterase substrate binding and catalysis
    • Zhuo, S., Clemens, J. C., Stone, R. L. & Dixon, J. E. (1994). Mutational analysis of a Ser/Thr phosphatase. Identification of residues important in phosphoesterase substrate binding and catalysis. J. Biol. Chem. 269, 26234-26238.
    • (1994) J. Biol. Chem. , vol.269 , pp. 26234-26238
    • Zhuo, S.1    Clemens, J.C.2    Stone, R.L.3    Dixon, J.E.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.