Indolamin 2,3-dioksigenaza
Изглед
Indolamin 2,3-dioksigenaza | |||||||||
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Identifikatori | |||||||||
EC broj | 1.13.11.52 | ||||||||
CAS broj | 9014-51-1 | ||||||||
Baze podataka | |||||||||
IntEnz | IntEnz pregled | ||||||||
BRENDA | BRENDA pristup | ||||||||
ExPASy | NiceZyme pregled | ||||||||
KEGG | KEGG pristup | ||||||||
MetaCyc | metabolički put | ||||||||
PRIAM | profil | ||||||||
Strukture PBP | RCSB PDB PDBe PDBj PDBsum | ||||||||
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Indolamin 2,3-dioksigenaza (EC 1.13.11.52, IDO (nespecifična), triptofanska pirolaza (nespecifična)) je enzim sa sistematskim imenom D-triptofan:kiseonik 2,3-oksidoreduktaza (deciklizacija).[1][2][3][4][5][6][7][8] Ovaj enzim katalizuje sledeću hemijsku reakciju
- (1) D-triptofan + O2 N-formil-D-kinurenin
- (2) L-triptofan + O2 N-formil-L-kinurenin
Ovaj enzim je protohemoprotein. Za njegovo dejstvo je neophodna askorbinska kiselina i metilin plavo.
Reference
[уреди | уреди извор]- ^ Yamamoto, S. & Hayaishi, O. (1967). „Tryptophan pyrrolase of rabbit intestine. D- and L-tryptophan-cleaving enzyme or enzymes”. J. Biol. Chem. 242: 5260—5266. PMID 6065097.
- ^ Yasui, H., Takai, K., Yoshida, R. and Hayaishi, O. (1986). „Interferon enhances tryptophan metabolism by inducing pulmonary indoleamine 2,3-dioxygenase: its possible occurrence in cancer patients”. Proc. Natl. Acad. Sci. USA. 83: 6622—6626. PMID 2428037.
- ^ Takikawa, O., Yoshida, R., Kido, R. and Hayaishi, O. (1986). „Tryptophan degradation in mice initiated by indoleamine 2,3-dioxygenase”. J. Biol. Chem. 261: 3648—3653. PMID 2419335.
- ^ Hirata, F., Ohnishi, T. and Hayaishi, O. (1977). „Indoleamine 2,3-dioxygenase. Characterization and properties of enzyme. O2- complex”. J. Biol. Chem. 252: 4637—4642. PMID 194886.
- ^ Dang, Y., Dale, W.E. and Brown, O.R. (2000). „Comparative effects of oxygen on indoleamine 2,3-dioxygenase and tryptophan 2,3-dioxygenase of the kynurenine pathway”. Free Radic. Biol. Med. 28: 615—624. PMID 10719243.
- ^ Littlejohn, T.K., Takikawa, O., Truscott, R.J. and Walker, M.J. (2003). „Asp274 and His346 are essential for heme binding and catalytic function of human indoleamine 2,3-dioxygenase”. J. Biol. Chem. 278: 29525—29531. PMID 12766158.
- ^ Thomas, S.R. & Stocker, R. (1999). „Redox reactions related to indoleamine 2,3-dioxygenase and tryptophan metabolism along the kynurenine pathway”. Redox Rep. 4: 199—220. PMID 10731095.
- ^ Sono, M. (1990). „Spectroscopic and equilibrium studies of ligand and organic substrate binding to indolamine 2,3-dioxygenase”. Biochemistry. 29: 1451—1460. PMID 2334706.
Literatura
[уреди | уреди извор]- Nicholas C. Price; Lewis Stevens (1999). Fundamentals of Enzymology: The Cell and Molecular Biology of Catalytic Proteins (Third изд.). USA: Oxford University Press. ISBN 019850229X.
- Eric J. Toone (2006). Advances in Enzymology and Related Areas of Molecular Biology, Protein Evolution (Volume 75 изд.). 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 изд.). Wiley Classics Library. ISBN 0471303097.
Spoljašnje veze
[уреди | уреди извор]- +indoleamine+2,3-dioxygenase на US National Library of Medicine Medical Subject Headings (MeSH)