Triptofan 2,3-dioksigenaza
| Triptofan 2,3-dioksigenaza | |||||||||
|---|---|---|---|---|---|---|---|---|---|
 | |||||||||
| Identifikatori | |||||||||
| EC broj | 1.13.11.11 | ||||||||
| 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 | ||||||||
| |||||||||
Triptofan 2,3-dioksigenaza (EC 1.13.11.11, triptofanska pirolaza (nespecifična), triptofanska oksigenaza, triptaminska 2,3-dioksigenaza, triptofanska peroksidaza, indolaminska 2,3-dioksigenaza (nespecifična), indolaminska 2,3-dioksigenaza (nespecifična), L-triptofan pirolaza, TDO, L-triptofanska 2,3-dioksigenaza) je enzim sa sistematskim imenom L-triptofan:kiseonik 2,3-oksidoreduktaza (deciklizacija).[1][2][3][4][5] Ovaj enzim katalizuje sledeću hemijsku reakciju
- L-triptofan + O2 N-formil-L-kinurenin
Ovaj enzim je protohemoprotein. Kod sisara, enzim je lociran u jetri.
Reference
[уреди | уреди извор]- ^ Uchida, K., Shimizu, T., Makino, R., Sakaguchi, K., Iizuka, T., Ishimura, Y., Nozawa, T. and Hatano, M. (1983). „Magnetic and natural circular dichroism of L-tryptophan 2,3-dioxygenases and indoleamine 2,3-dioxygenase. I. Spectra of ferric and ferrous high spin forms”. J. Biol. Chem. 258: 2519—2525. PMID 6600455.
- ^ Ren, S., Liu, H., Licad, E. and Correia, M.A. (1996). „Expression of rat liver tryptophan 2,3-dioxygenase in Escherichia coli: structural and functional characterization of the purified enzyme”. Arch. Biochem. Biophys. 333: 96—102. PMID 8806758.
- ^ Leeds, J.M., Brown, P.J., McGeehan, G.M., Brown, F.K. and Wiseman, J.S. (1993). „Isotope effects and alternative substrate reactivities for tryptophan 2,3-dioxygenase”. J. Biol. Chem. 268: 17781—17786. PMID 8349662.
- ^ 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.
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.
- William P. Jencks (1987). Catalysis in Chemistry and Enzymology. Dover Publications. ISBN 0486654605.
Spoljašnje veze
[уреди | уреди извор]- Tryptophan+2,3-dioxygenase на US National Library of Medicine Medical Subject Headings (MeSH)
