Indolamin 2,3-dioksigenaza

Indolamin 2,3-dioksigenaza
Identifikatori
EC broj 1.13.11.52
CAS broj 9014-51-1
IntEnz IntEnz view
BRENDA BRENDA entry
ExPASy NiceZyme view
KEGG KEGG entry
MetaCyc metabolic pathway
PRIAM profile
PDB RCSB PDB PDBe PDBj PDBsum
Pretraga
PMC articles
PubMed articles
NCBI Protein search

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 ⇌ {\displaystyle \rightleftharpoons } N-formil-D-kinurenin
(2) L-triptofan + O2 ⇌ {\displaystyle \rightleftharpoons } N-formil-L-kinurenin

Ovaj enzim je protohemoprotein. Za njegovo dejstvo je neophodna askorbinska kiselina i metilin plavo.

Reference

  1. ↑ Yamamoto, S. and Hayaishi, O. (1967). „Tryptophan pyrrolase of rabbit intestine. D- and L-tryptophan-cleaving enzyme or enzymes”. J. Biol. Chem. 242: 5260-5266. PMID 6065097. 
  2. ↑ 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. 
  3. ↑ 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. 
  4. ↑ 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. 
  5. ↑ 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. 
  6. ↑ 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. 
  7. ↑ Thomas, S.R. and 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. 
  8. ↑ 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

  • 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 +indoleamine+2,3-dioxygenase
  • p
  • r
  • u
TemeTipovi
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