EC 1.11.1.8 - Iodide peroxidase
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ENZYME view
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 [incorrect]
iodotyrosine deiodinase [incorrect]
monoiodotyrosine deiodinase [incorrect]
thyroid peroxidase
thyroperoxidase
tyrosine iodinase
TPO
iodinase
iodoperoxidase (heme type)
iodotyrosine deiodase [incorrect]
iodotyrosine deiodinase [incorrect]
monoiodotyrosine deiodinase [incorrect]
thyroid peroxidase
thyroperoxidase
tyrosine iodinase
TPO
Systematic name:
iodide:hydrogen-peroxide oxidoreductase
Reactions
- (1) 2 iodide + H2O2 + 2 H+ = diiodine + 2 H2O
- (2) thyroglobulin-L-tyrosine + iodide + H2O2 = thyroglobulin-3-iodo-L-tyrosine + 2 H2O
- (3) thyroglobulin-3-iodo-L-tyrosine + iodide + H2O2 = thyroglobulin-3,5-diiodo-L-tyrosine + 2 H2O
- (4) 2 thyroglobulin-3,5-diiodo-L-tyrosine + H2O2 = thyroglobulin-L-thyroxine + thyroglobulin-aminoacrylate + 2 H2O
- (5) thyroglobulin-3-iodo-L-tyrosine + thyroglobulin-3,5-diiodo-L-tyrosine + H2O2 = thyroglobulin-3,5,3'-triiodo-L-thyronine + thyroglobulin-aminoacrylate + 2 H2O
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
Protein domains and families:
PROSITE:PDOC00394
Gene Ontology:
GO:0004447
CAS Registry Number:
9031-28-1
References
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Enzyme systems concerned with the synthesis of monoiodotyrosine. III. Ion requirements of the soluble system.J. Biol. Chem. 236 : 485-489 (1961). [PMID: 13718859]
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Peroxidase activity in thyroid gland and partial purification of the enzyme.J. Biochem. 52 : 180-189 (1962). [PMID: 13964156]
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Purification and iodinating activity of hog thyroid peroxidase.J. Biol. Chem. 242 : 5510-5523 (1967). [PMID: 12325367]
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Thyroid hormone synthesis in thyroglobulin. The mechanism of the coupling reaction.J. Biol. Chem. 256 : 9167-9173 (1981). [PMID: 7021557]
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One- and two-electron oxidations of tyrosine, monoiodotyrosine, and diiodotyrosine catalyzed by hog thyroid peroxidase.J. Biol. Chem. 257 : 13398-13403 (1982). [PMID: 7142155]
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Mechanism of iodide-dependent catalatic activity of thyroid peroxidase and lactoperoxidase.J. Biol. Chem. 259 : 197-205 (1984). [PMID: 6706930]
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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]
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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]
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Kinetics and mechanism of the peroxidase-catalyzed iodination of tyrosine.Biochemistry 32 : 1324-1331 (1993). [PMID: 8448141]
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Mechanism of simultaneous iodination and coupling catalyzed by thyroid peroxidase.Arch. Biochem. Biophys. 330 : 24-32 (1996). [PMID: 8651700]
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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]