Molecular evolution of thyroid peroxidase

Biochimie

Volumn 81, Issue 5, 1999, Pages 557-562

  Taurog, Alvin ^a  

^a UNIVERSITY OF TEXAS SOUTHWESTERN MEDICAL CENTER   (United States)

Author keywords

Animal peroxidases; Evolution; Peroxidase; Thyroid peroxidase; TPO

Indexed keywords

ARGININE; ASPARAGINE; HISTIDINE; LACTOPEROXIDASE; MYELOPEROXIDASE; PEROXIDASE; THYROID PEROXIDASE;

ALTERNATIVE RNA SPLICING; AMINO ACID SEQUENCE; ARTICLE; EVOLUTION; HYDROGEN BOND; MULTIGENE FAMILY; NONHUMAN; PROTEIN SECONDARY STRUCTURE; PROTEIN TERTIARY STRUCTURE; SEQUENCE HOMOLOGY;

ANIMALIA; BACTERIA (MICROORGANISMS); INVERTEBRATA; MAMMALIA;

EID: 0032730385     PISSN: 03009084     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0300-9084(99)80110-2     Document Type: Article

References (45)

1. Taurog A. Biosynthesis of Thyroid Hormone, Proceedings of the VIth Pan American Congress of Endocrinology Excerpta Medica International Congress Series No. 112. 1965;367-374.
2. Astwood E.B. Mechanism of action of antithyroid compounds. Brookhaven Symp. Biol. 7:1955;61-73.
3. Shaw P.D., Hager L.J. Chloroperoxidase: A component of the β-keto-adipate-chlorinase system. J. Biol. Chem. 236:1961;1626-1630.
4. Taurog A., Howells E.M. Enzymatic iodination of tyrosine and thyroglobulin with chloroperoxidase. J. Biol. Chem. 241:1966;1329-1339.
5. Hosoya T., Morrison M. The isolation and purification of thyroid peroxidase. J. Biol. Chem. 242:1967;2828-2836.
6. Coval M.L., Taurog A. Purification and iodinating activity of hog thyroid peroxidase. J. Biol. Chem. 242:1967;5510-5523.
7. Taurog A. Hormone synthesis: Thyroid iodine metabolism. Braverman L.E, Utiger R.D. Werner and Ingbar's The Thyroid, 7th edition. 1996;47-81 Philadelphia, Lippincott-Raven.
8. McLachlan S.M., Rapoport B. The molecular biology of thyroid peroxidase: Cloning, expression and role as autoantigen in autoimmune thyroid disease. Endocrine Rev. 13:1992;192-206.
9. Fenna R., Zeng J., Davey C. Research report; Structure of the green heme in myeloperoxidase. Arch. Biochem. Biophys. 316:1995;653-656.
10. Andersson L.A., Bylkas S.A., Wilson A.E. Spectral analysis of lactoperoxidase; Evidence for a common heme in mammalian peroxidases. J. Biol. Chem. 271:1996;3406-3412.
11. Rae T.D., Goff H.M. Lactoperoxidase heme structure characterized by paramagnetic proton NMR spectroscopy. J. Am. Chem. Soc. 118:1996;2103-2104.
12. Depillis G.D., Ozaki S.I., Kuo J.M., Maltby D.A., Ortiz de Montellano P.R. Autocatalytic processing of heme by lactoperoxidase produces the native protein-bound prosthetic group. J. Biol. Chem. 272:1997;8857-8860.
13. Poulos T.L., Freer S.T., Alden R.A., Edwards S.L., Skogland U., Takio K., Eriksson B., Xuong N.H., Yonetani T., Kraut J. The crystal structure of cytochrome c peroxidase. J. Biol. Chem. 255:1980;575-580.
14. Finzel B.C., Poulos T.L., Kraut J. Crystal structure of yeast cytochrome c peroxidase refined at 1.7-Å resolution. J. Biol. Chem. 259:1984;13027-13036.
15. Poulos T.L. Heme enzyme crystal structures. Adv. Inorg. Biochem. 7:1988;1-36.
16. Schuller D.J., Ban N., van Huystee R.B., McPherson A., Poulos T.L. The crystal structure of peanut peroxidase. Structure. 4:1996;311-321.
17. Gajhede M., Schuller D.J., Henriksen A., Smith A.T., Poulos T.L. Crystal structure of horseradish peroxidase C at 2.15 Å resolution. Nature Struct. Biol. 4:1997;1032-1038.
18. Zeng J., Fenna R.E. X-ray crystal structure of canine myeloperoxidase at 3 Å resolution. J. Mol. Biol. 226:1992;185-207.
19. Poulos T.L. Peroxidases. Curr. Opin. Biotechnol. 4:1993;484-489.
20. Jacquet A., Garcia-Quintana L., Deleersnyder V., Fenna R., Bollen A., Moguilevsky N. Site-directed mutagenesis of human myeloperoxidase: Further identification of residues involved in catalytic activity and heme interaction. Biochem. Biophys. Res. Commun. 202:1994;73-81.
21. Poulos T.L., Fenna R.E. Peroxidases: Structure, function, and engineering. Sigel H, Sigel A. Metal Ions in Biological Systems. 1994;25-75 New York, Marcel Dekker, Inc.
22. Kimura S., Ikeda-Saito M. Human myeloperoxidase and thyroid peroxidase, two enzymes with separate and distinct physiological functions, are evolutionarily related members of the same gene family. Proteins Struct. Funct. Genet. 3:1988;113-120.
23. Banga J.P., Mahadevan D., Barton G.J., Sutton B.J., Saldanha J.W., Odell E., McGregor A.M. Prediction of domain organisation and secondary structure of thyroid peroxidase, a human autoantigen involved in destructive thyroiditis. FEBS Lett. 266:1990;133-141.
24. Nishikawa T., Rapoport B., McLachlan S.M. Exclusion of two major areas of thyroid peroxidase from the immunodominant region containing the conformational epitopes recognized by human autoantibodies. J. Clin. Endocrinol. Metab. 79:1994;1648-1654.
25. Bikker H., Baas F., De Vijlder J.J.M. Molecular analysis of mutated thyroid peroxidase detected in patients with total iodide organification defects. J. Clin. Endocrinol. Metab. 82:1997;649-653.
26. Kimura S., Kontani T., McBride O.W., Umeki K., Hirai K., Nakayama T., Ohtaki S. Human thyroid peroxidase: Complete cDNA and protein sequence, chromosome mapping, and identification of two alternately spliced mRNAs. Proc. Natl. Acad. Sci. USA. 84:1987;5555-5559.
27. Kimura S., Hong Y.S., Kotani T., Ohtaki S., Kikkawa F. Structure of the human thyroid peroxidase gene: Comparison and relationship to the human myeloperoxidase gene. Biochemistry. 28:1989;4481-4489.
28. Elisei R., Vassart G., Ludgate M. Demonstration of the existence of the alternatively spliced form of thyroid peroxidase in normal thyroid. J. Clin. Endocrinol. Metab. 72:1991;700-702.
29. Bikker H., Waelkens J.J.J., Bravenboer B., De Vijlder J.J.M. Congenital hypothyroidism caused by a premature termination signal in exon 10 of the human thyroid peroxidase gene. J. Clin. Endocrinol. Metab. 81:1996;2076-2079.
30. Niccoli P., Fayadat L., Panneels V., Lanet J., Franc J.L. Human thyroperoxidase in its alternatively spliced form (TPO2) is enzymatically inactive and exhibits changes in intracellular processing and trafficking. J. Biol. Chem. 272:1997;29487-29492.
31. Johansson M.W., Lind M.I., Holmblad T., Thörnqvist P.O., Söderhäll K. Peroxinectin, a novel cell adhesion protein from crayfish blood. Biochem. Biophys. Res. Commun. 216:1995;1079-1087.
32. Nelson R.E., Fessler L.I., Takagi Y., Blumberg B., Keene D.R., Olson P.F., Parker C.G., Fessler J.H. Peroxidasin: a novel enzyme-matrix protein of Drosophila development. EMBO J. 13:1994;3438-3447.
33. Palumbo A., Jackson I.J. Peroxidase activity in the ink gland of Sepia officinalis and partial nucleotide sequence of a candidate cDNA encoding the enzyme. Biochim. Biophys. Acta. 1247:1995;173-178.
34. Tomarev S.I., Zinovieva R.D., Weis V.M., Chepelinsky A.B., Piatigorsky J., Mc Fall-Ngai M.J. Abundant mRNAs in the squid light organ encode proteins with a high similarity to mammalian peroxidases. Gene. 132:1993;219-226.
35. Wilson R., Ainscough R., Anderson K., Baynes C., Berks M., Bonfield J., Burton J., Connell T. 2.2 Mb of contiguous nucleotide sequence from chromosome III of C. elegans. Nature. 368:1994;32-38.
36. Suzuki N. Direct submission to the DDBJ/EMBL/GenBank databases, Apr. 15. accession number AB003145:1997.
37. Johansson M.W., Soderhall K. Isolation and purification of a cell adhesion factor from crayfish blood cells. J. Cell. Biol. 106:1988;1795-1803.
38. Nomura K., Suzuki N. Sea urchin ovoperoxidase: Solubilization and isolation from the fertilization envelope, some structural and functional properties, and degradation by hatching enzyme. Arch. Biochem. Biophys. 319:1995;525-534.
39. Welinder K.G. Superfamily of plant, fungal and bacterial peroxidases. Curr. Opin Struct. Biol. 2:1992;388-393.
40. Welinder K.G., Gajhede M. Structure and evolution of peroxidases. Welinder K.G, Rasmussen S.K, Penel C, Greppin H. Plant Peroxidases: Biochemistry and Physiology. 1993;35-42 Univ. of Geneva.
41. Kraulis P. Molscript: a program to produce both detailed and schematic plots of proteins. J. Appl. Cryst. 24:1991;946-950.
42. Dawson J.H. Probing structure-function relations in heme-containing oxygenases and peroxidases. Science. 240:1988;433-439.
43. 2 integrin (Mac-1, CD11b/CD18). J. Cell Sci. 110:1997;1133-1139.
44. Blow D. More of the catalytic triad. Nature. 343:1990;694-695.
45. Liao D.I., Remington S.J. Structure of wheat serine carboxypeptidase II at 3.5-Å resolution; A new class of serine proteinase. J. Biol. Chem. 265:1990;6528-6531.