EC 1.11.1.8 - Iodide peroxidase

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IntEnz Enzyme Nomenclature
EC 1.11.1.8

Names

Accepted name:
iodide peroxidase
Other names:
iodide peroxidase-tyrosine iodinase
iodinase
iodoperoxidase (heme type)
iodotyrosine deiodase
iodotyrosine deiodinase
monoiodotyrosine deiodinase
thyroid peroxidase
thyroperoxidase
tyrosine iodinase
TPO
Systematic name:
iodide:hydrogen-peroxide oxidoreductase

Reactions

Cofactor

Comments:

Thyroid peroxidase catalyses the biosynthesis of the thyroid hormones L-thyroxine and triiodo-L-thyronine. It catalyses both the iodination of tyrosine residues in thyroglobulin (forming mono- and di-iodinated forms) and their coupling to form either L-thyroxine or triiodo-L-thyronine.

Links to other databases

Enzymes and pathways: NC-IUBMB , BRENDA , ExplorEnz , ENZYME@ExPASy , KEGG , MetaCyc , UniPathway
Protein domains and families: PROSITE:PDOC00394
Structural data: CSA , EC2PDB
Gene Ontology: GO:0004447
CAS Registry Number: 9031-28-1
UniProtKB/Swiss-Prot:

References

  1. Cunningham, B. A., Kirkwood, S.
    Enzyme systems concerned with the synthesis of monoiodotyrosine. III. Ion requirements of the soluble system.
    J. Biol. Chem. 236: 485-489 (1961). [PMID: 13718859]
  2. Hosoya, T., Kondo, Y., Ui, N.
    Peroxidase activity in thyroid gland and partial purification of the enzyme.
    J. Biochem. 52: 180-189 (1962). [PMID: 13964156]
  3. Coval, M. L., Taurog, A.
    Purification and iodinating activity of hog thyroid peroxidase.
    J. Biol. Chem. 242: 5510-5523 (1967). [PMID: 12325367]
  4. Gavaret, J. M., Cahnmann, H. J., Nunez, J.
    Thyroid hormone synthesis in thyroglobulin. The mechanism of the coupling reaction.
    J. Biol. Chem. 256: 9167-9173 (1981). [PMID: 7021557]
  5. Ohtaki, S., Nakagawa, H., Nakamura, M., Yamazaki, I.
    One- and two-electron oxidations of tyrosine, monoiodotyrosine, and diiodotyrosine catalyzed by hog thyroid peroxidase.
    J. Biol. Chem. 257: 13398-13403 (1982). [PMID: 7142155]
  6. Magnusson, R. P., Taurog, A., Dorris, M. L.
    Mechanism of iodide-dependent catalatic activity of thyroid peroxidase and lactoperoxidase.
    J. Biol. Chem. 259: 197-205 (1984). [PMID: 6706930]
  7. Virion, A., Courtin, F., Deme, D., Michot, J. L., Kaniewski, J., Pommier, J.
    Spectral characteristics and catalytic properties of thyroid peroxidase-H2O2 compounds in the iodination and coupling reactions.
    Arch. Biochem. Biophys. 242: 41-47 (1985). [PMID: 2996435]
  8. Rawitch, A. B., Pollock, G., Yang, S. X., Taurog, A.
    Thyroid peroxidase glycosylation: the location and nature of the N-linked oligosaccharide units in porcine thyroid peroxidase.
    Arch. Biochem. Biophys. 297: 321-327 (1992). [PMID: 1497352]
  9. Sun, W., Dunford, H. B.
    Kinetics and mechanism of the peroxidase-catalyzed iodination of tyrosine.
    Biochemistry 32: 1324-1331 (1993). [PMID: 8448141]
  10. Taurog, A., Dorris, M. L., Doerge, D. R.
    Mechanism of simultaneous iodination and coupling catalyzed by thyroid peroxidase.
    Arch. Biochem. Biophys. 330: 24-32 (1996). [PMID: 8651700]
  11. Ruf, J., Carayon, P.
    Structural and functional aspects of thyroid peroxidase.
    Arch. Biochem. Biophys. 445: 269-277 (2006). [PMID: 16098474]

[EC 1.11.1.8 created 1961, modified 2012]