Jodid peroksidaza
Jodid peroksidaza | |||||||||
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Jodid peroksidaza monomer, Zobellia galactanivorans | |||||||||
Identifikatori | |||||||||
EC broj | 1.11.1.8 | ||||||||
CAS broj | 9031-28-1 | ||||||||
IntEnz | IntEnz view | ||||||||
BRENDA | BRENDA entry | ||||||||
ExPASy | NiceZyme view | ||||||||
KEGG | KEGG entry | ||||||||
MetaCyc | metabolic pathway | ||||||||
PRIAM | profile | ||||||||
PDB | RCSB PDB PDBe PDBj PDBsum | ||||||||
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Jodid peroksidaza (EC 1.11.1.8, tiroidna peroksidaza, jodotirozinska dejodaza, jodinaza, jodoperoksidaza (hem tip), jodidna peroksidaza-tirozinska jodinaza, jodotirozinska dejodinaza, monojodotirozinska dejodinaza, tiroperoksidaza, tirozinska jodinaza, TPO) je enzim sa sistematskim imenom jod:vodonik-peroksid oksidoreduktaza.[1][2][3][4][5][6][7][8][9][10][11] Ovaj enzim katalizuje sledeću hemijsku reakciju
- (1) 2 jodid + H2O2 + 2 H+ dijodin + 2H2O
- (2) [tiroglobulin]-L-tirozin + jodid + H2O2 [tiroglobulin]-3-jodo-L-tirozin + 2H2O
- (3) [tiroglobulin]-3-jodo-L-tirozin + jodid + H2O2 [tiroglobulin]-3,5-dijodo-L-tirozin + 2H2O
- (4) 2 [tiroglobulin]-3,5-dijodo-L-tirozin + H2O2 [tiroglobulin]-L-tiroksin + [tiroglobulin]-aminoakrilat + 2H2O
- (5) [tiroglobulin]-3-jodo-L-tirozin + [tiroglobulin]-3,5-dijodo-L-tirozin + H2O2 [tiroglobulin]-3,5,3'-trijodo-L-tironin + [tiroglobulin]-aminoakrilat + 2H2O
Tiroidna peroksidaza katalizuje biosintezu tiroidnih hormona L-tiroksina i trijodo-L-tironina.
Reference
- ↑ Cunningham, B.A. and Kirkwood, S. (1961). „Enzyme systems concerned with the synthesis of monoiodotyrosine. III. Ion requirements of the soluble system”. J. Biol. Chem. 236: 485-489. PMID 13718859.
- ↑ Hosoya, T., Kondo, Y. and Ui, N. (1962). „Peroxidase activity in thyroid gland and partial purification of the enzyme”. J. Biochem. (Tokyo) 52: 180-189. PMID 13964156.
- ↑ Coval, M.L. and Taurog, A. (1967). „Purification and iodinating activity of hog thyroid peroxidase”. J. Biol. Chem. 242: 5510-5523. PMID 12325367.
- ↑ Gavaret, J.M., Cahnmann, H.J. and Nunez, J. (1981). „Thyroid hormone synthesis in thyroglobulin. The mechanism of the coupling reaction”. J. Biol. Chem. 256: 9167-9173. PMID 7021557.
- ↑ Ohtaki, S., Nakagawa, H., Nakamura, M. and Yamazaki, I. (1982). „One- and two-electron oxidations of tyrosine, monoiodotyrosine, and diiodotyrosine catalyzed by hog thyroid peroxidase”. J. Biol. Chem. 257: 13398-13403. PMID 7142155.
- ↑ Magnusson, R.P., Taurog, A. and Dorris, M.L. (1984). „Mechanism of iodide-dependent catalatic activity of thyroid peroxidase and lactoperoxidase”. J. Biol. Chem. 259: 197-205. PMID 6706930.
- ↑ Virion, A., Courtin, F., Deme, D., Michot, J.L., Kaniewski, J. and Pommier, J. (1985). „Spectral characteristics and catalytic properties of thyroid peroxidase-H2O2 compounds in the iodination and coupling reactions”. Arch. Biochem. Biophys. 242: 41-47. PMID 2996435.
- ↑ Rawitch, A.B., Pollock, G., Yang, S.X. and Taurog, A. (1992). „Thyroid peroxidase glycosylation: the location and nature of the N-linked oligosaccharide units in porcine thyroid peroxidase”. Arch. Biochem. Biophys. 297: 321-327. PMID 1497352.
- ↑ Sun, W. and Dunford, H.B. (1993). „Kinetics and mechanism of the peroxidase-catalyzed iodination of tyrosine”. Biochemistry 32: 1324-1331. PMID 8448141.
- ↑ Taurog, A., Dorris, M.L. and Doerge, D.R. (1996). „Mechanism of simultaneous iodination and coupling catalyzed by thyroid peroxidase”. Arch. Biochem. Biophys. 330: 24-32. PMID 8651700.
- ↑ Ruf, J. and Carayon, P. (2006). „Structural and functional aspects of thyroid peroxidase”. Arch. Biochem. Biophys. 445: 269-277. PMID 16098474.
Literatura
- Nicholas C. Price, Lewis Stevens (1999). Fundamentals of Enzymology: The Cell and Molecular Biology of Catalytic Proteins (Third izd.). USA: Oxford University Press. ISBN 019850229X.
- Eric J. Toone (2006). Advances in Enzymology and Related Areas of Molecular Biology, Protein Evolution (Volume 75 izd.). Wiley-Interscience. ISBN 0471205036.
- Branden C, Tooze J.. Introduction to Protein Structure. New York, NY: Garland Publishing. ISBN: 0-8153-2305-0.
- Irwin H. Segel. Enzyme Kinetics: Behavior and Analysis of Rapid Equilibrium and Steady-State Enzyme Systems (Book 44 izd.). Wiley Classics Library. ISBN 0471303097.
- Robert A. Copeland (2013). Evaluation of Enzyme Inhibitors in Drug Discovery: A Guide for Medicinal Chemists and Pharmacologists (2nd izd.). Wiley-Interscience. ISBN 111848813X.
- Gerhard Michal, Dietmar Schomburg (2012). Biochemical Pathways: An Atlas of Biochemistry and Molecular Biology (2nd izd.). Wiley. ISBN 0470146842.
Spoljašnje veze
- MeSH Iodide+peroxidase
- p
- r
- u
Aktivno mesto • Alosterna regulacija • Mesto vezivanja • Katalitički perfektan enzim • Koenzim • Kofaktor • Kooperativnost • EC broj • Enzimska kataliza • Inhibicija enzima • Enzimska kinetika • Lajnviver–Burk dijagram • Mihaelis–Mentenova kinetika • Spisak enzima
EC1 Oksidoreduktaze/spisak • EC2 Transferaze/spisak • EC3 Hidrolaze/spisak • EC4 Lijaze/spisak • EC5 Izomeraze/spisak • EC6 Ligaze/spisak
B enzm: 1.1/2/3/4/5/6/7/8/10/11/13/14/15-18, 2.1/2/3/4/5/6/7/8, 2.7.10, 2.7.11-12, 3.1/2/3/4/5/6/7, 3.1.3.48, 3.4.21/22/23/24, 4.1/2/3/4/5/6, 5.1/2/3/4/99, 6.1-3/4/5-6