Identification and molecular modeling of a novel, plant-like, human purple acid phosphatase

Gene

Volumn 377, Issue 1-2, 2006, Pages 12-20

  Flanagan, J U ^a   Cassady, A I ^a   Schenk, G ^a   Guddat, L W ^a   Hume, D A ^a  

^a UNIVERSITY OF QUEENSLAND   (Australia)

Author keywords

Fenton catalyst; Metalloenzyme; Structure; Tartrate resistant

Indexed keywords

ACID PHOSPHATASE TARTRATE RESISTANT ISOENZYME;

ARTICLE; CATALYSIS; ENZYME ANALYSIS; ENZYME STRUCTURE; INSECT; MAMMAL; MOLECULAR MODEL; NEMATODE; NONHUMAN; NUCLEOTIDE SEQUENCE; PHASEOLUS VULGARIS; PHYLOGENY; PLANT; PREDICTION; PRIORITY JOURNAL; PROTEIN ANALYSIS; SEQUENCE ANALYSIS;

ACID PHOSPHATASE; AMINO ACID SEQUENCE; ANIMALS; CATALYTIC DOMAIN; DIMERIZATION; GLYCOPROTEINS; HUMANS; ISOENZYMES; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; MOLECULAR WEIGHT; PHASEOLUS; PHYLOGENY; PROTEIN STRUCTURE, QUATERNARY; PROTEIN STRUCTURE, SECONDARY; SEQUENCE HOMOLOGY, AMINO ACID; SPECIES SPECIFICITY;

ANIMALIA; FUNGI; HEXAPODA; MAMMALIA; NEMATODA; PHASEOLUS VULGARIS;

EID: 33745953168     PISSN: 03781119     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.gene.2006.02.031     Document Type: Article

References (46)

1. Altschul S.F., and Koonin E.V. Iterated profile searches with PSI-BLAST: a tool for discovery in protein databases. Trends Biochem. Sci. 23 (1998) 444-447
2. Antanaitis B.C., Aisen P., and Lilienthal H.R. Physical characterization of two-iron uteroferrin: evidence for a spin-coupled binuclear iron cluster. J. Biol. Chem. 258 (1983) 3166-3172
3. Beck J.L., McConaghie L.A., Summors A.C., Arnold W.N., de Jersey J., and Zerner B. Properties of a purple acid phosphatase from red kidney bean: a zinc-iron metalloenzyme. Biochim. Biophys. Acta 869 (1986) 61-68
4. Bozzo G.G., Raghothama K.G., and Plaxton W.C. Purification and characterization of two secreted purple acid phosphatase isozymes from phosphate-starved tomato (Lycopersicon esculentum) cell cultures. Eur. J. Biochem. 269 (2002) 6278-6286
5. Cuff J.A., and Barton G.J. Application of multiple sequence alignment profiles to improve protein secondary structure prediction. Proteins 40 (2000) 502-511
6. Duff S.M., Sarath G., and Plaxton W.C. The role of acid phosphatases in plant phosphorus metabolism. Physiol. Plant 90 (1994) 791-800
7. Durmus A., et al. The active site of purple acid phosphatase from sweet potatoes (Ipomoea batatas). Eur. J. Biochem. 260 (1999) 709-716
8. Durmus A., Eicken C., Spener F., and Krebs B. Cloning and comparative modeling of two purple acid phosphatase isozymes from sweet potatoes (Ipomoea batatas). Biochim. Biophys. Acta 1434 (1999) 202-209
9. Ek-Rylander B., Flores M., Wendel M., Heinegard D., and Andersson G. Dephosphorylation of osteopontin and bone sialoprotein by osteoclastic tartrate-resistant acid phosphatase. J. Biol. Chem. 269 (1994) 14853-14856
10. Ek-Rylander B., Barkhem T., Ljusberg J., Ohman L., Andersson K.K., and Andersson G. Comparative studies of rat recombinant purple acid phosphatase and bone tartrate-resistant acid phosphatase. Biochem. J. 321 (1997) 305-311
11. Funhoff E.G., Wang Y., Andersson G., and Averill B.A. Substrate positioning by His92 is important in catalysis by purple acid phosphatase. FEBS J. 272 (2005) 2968-2977
12. Grimes R., et al. Assignment of the mouse tartrate-resistant acid phosphatase gene (Acp5) to chromosome 9. Genomics 15 (1993) 421-422
13. Guddat L.W., McAlpine A.S., Hume D., Hamilton S., de Jersey J., and Martin J.L. Crystal structure of mammalian purple acid phosphatase. Structure 7 (1999) 757-767
14. Halleen J.M., et al. Intracellular fragmentation of bone resorption products by reactive oxygen species generated by osteoclastic tartrate-resistant acid phosphatase. J. Biol. Chem. 274 (1999) 22907-22910
15. Halleen J.M., Raisänen S.R., Alatalo S.L., and Väänänen H.K. Potential function for the ROS-generating activity of TRACP. J. Bone Miner. Res. 18 (2003) 1908-1911
16. Hayman A.R., Warburton M.J., Pringle J.A., Coles B., and Chambers T.J. Purification and characterisation of a tartrate-resistant acid phosphatase from human osteoclastomas. Biochem. J. 261 (1989) 601-609
17. Hayman A.R., et al. Mice lacking tartrate-resistant acid phosphatase (Acp5) have disrupted endochondral ossification and mild osteopetrosis. Development 122 (1996) 3151-3162
18. Kaija H., et al. Phosphatase and oxygen radical-generating activities of mammalian purple acid phosphatase are functionally independent. Biochem. Biophys. Res. Commun. 292 (2002) 128-132
19. Klabunde T., and Krebs B. The dimetal centre in purple acid phosphatases. Struct. and Bond. 89 (1997) 177-198
20. Klabunde T., Sträter N., Fröhlich 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
21. Laskowski R.A., Moss D.A., and Thornton J.M. Main-chain bond lengths and bond angles in protein structures. J. Mol. Biol. 231 (1993) 1049-1067
22. Leach R.J., Reus B.E., Hundley J.E., Johnson-Pais T.L., and Windle J.J. Confirmation of the assignment of the human tartrate-resistant acid phosphatase gene (ACP5) to chromosome 19. Genomics 19 (1994) 180-181
23. Li D., et al. Purple acid phosphatases of Arabidopsis thaliana. Comparative analysis and differential regulation by phosphate deprivation. J. Biol. Chem. 277 (2002) 27772-27781
24. Lindqvist Y., Johansson E., Kaija H., Vihko P., and Schneider G. Three-dimensional structure of a mammalian purple acid phosphatase at 2.2 Å resolution with a μ-(hydr)oxo bridged di-iron center. J. Mol. Biol. 291 (1999) 135-147
25. Ling P., and Roberts R.M. Uteroferrin and intracellular tartrate-resistant acid phosphatases are the products of the same gene. J. Biol. Chem. 268 (1993) 6896-6902
26. Ljusberg J., Ek-Rylander B., and Andersson G. Tartrate-resistant purple acid phosphatase is synthesized as a latent proenzyme and activated by cysteine proteinases. Biochem. J. 343 (1999) 63-69
27. Marshall K., et al. Recombinant human and mouse purple acid phosphatases: expression and characterization. Arch. Biochem. Biophys. 345 (1997) 230-236
28. McGuffin L.J., Bryson K., and Jones D.T. The PSIPRED protein structure prediction server. Bioinformatics 16 (2000) 404-405
29. Mitić N., et al. Human tartrate-resistant acid phosphatase becomes an effective ATPase upon proteolytic activation. Arch. Biochem. Biophys. 439 (2005) 154-164
30. Nash K., Feldmuller M., de Jersey J., Alewood P., and Hamilton S. Continuous and discontinuous assays for phosphotyrosyl protein phosphatase activity using phosphotyrosyl peptide substrates. Anal. Biochem. 213 (1993) 303-309
31. Oddie G.W., et al. Structure, function and regulation of tartrate resistant acid phosphatase. Bone 27 (2000) 575-584
32. Raisänen S.R., et al. Macrophages overexpressing tartrate-resistant acid phosphatase show altered profile of free radical production and enhanced capacity of bacterial killing. Biochem. Biophys. Res. Commun. 331 (2005) 120-126
33. Rost B. PHD: predicting one-dimensional protein structure by profile based neural networks. Methods Enzymol. 266 (1996) 525-539
34. Saftig P., et al. Mice deficient in lysosomal acid phosphatase develop lysosomal storage in the kidney and central nervous system. J. Biol. Chem. 272 (1997) 18628-18635
35. Schenk G., et al. Binuclear metal centers in plant purple acid phosphatases. Fe-Mn in sweet potato and Fe-Zn in soybean. Arch. Biochem. Biophys. 370 (1999) 183-189
36. Schenk G., Korsinczky M.L.J., Hume D.A., Hamilton S., and de Jersey J. Purple acid phosphatases from bacteria: similarities to mammalian and plant enzymes. Gene 255 (2000) 419-424
37. Schenk G., et al. Identification of mammalian-like purple acid phosphatases in a wide range of plants. Gene 250 (2000) 117-125
38. Schenk G., et al. A purple acid phosphatase from sweet potato contains an antiferromagnetically coupled binuclear Fe-Mn center. J. Biol. Chem. 276 (2001) 19084-19088
39. Schenk G., et al. Phosphate forms an unusual tripodal complex with the Fe-Mn center of sweet potato purple acid phosphatase. Proc. Natl. Acad. Sci. U. S. A. 102 (2005) 273-278
40. Sibille J.C., Doi K., and Aisen P. Hydroxyl radical formation and iron-binding proteins. Stimulation by the purple acid phosphatases. J. Biol. Chem. 262 (1987) 59-62
41. Sträter 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
42. Sträter N., et al. Crystal structures of recombinant human purple acid phosphatase with and without an inhibitory conformation of the repression loop. J. Mol. Biol. 351 (2005) 233-246
43. Uppenberg J., Lindqvist F., Svensson C., Ek-Rylander B., and Andersson G. Crystal structure of a mammalian purple acid phosphatase. J. Mol. Biol. 290 (1999) 201-211
44. Valizadeh M., et al. Phosphotyrosyl peptides and analogues as substrates and inhibitors of purple acid phosphatases. Arch. Biochem. Biophys. 424 (2004) 154-162
45. Wynne C.J., Hamilton S.E., Dionysius D.A., Beck J.L., and de Jersey J. Studies on the catalytic mechanism of pig purple acid phosphatase. Arch. Biochem. Biophys. 319 (1995) 133-141
46. Zimmermann P., Regierer B., Kossmann J., Frossard E., Amrhein N., and Bucher M. Differential expression of three purple acid phosphatases from potato. Plant Biol. 6 (2004) 519-528