Triptofan 5-monooksigenaza
| Triptofan 5-monooksigenaza | |||||||||
|---|---|---|---|---|---|---|---|---|---|
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| Identifikatori | |||||||||
| EC broj | 1.14.16.4 | ||||||||
| CAS broj | 9037-21-2 | ||||||||
| 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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Triptofan 5-monooksigenaza (EC 1.14.16.4, L-triptofanska hidroksilaza, indolsirćetna kiselina-5-hidroksilaza, triptofanska 5-hidroksilaza, triptofanska hidroksilaza) je enzim sa sistematskim imenom L-triptofan,tetrahidrobiopterin:kiseonik oksidoreduktaza (5-hidroksilacija).[1][2][3][4][5] Ovaj enzim katalizuje sledeću hemijsku reakciju
- L-triptofan + tetrahidrobiopterin + O2 5-hidroksi-L-triptofan + 4a-hidroksitetrahidrobiopterin
Aktivni centar sadrži mononuklearno gvožđe(II). Enzim se aktivira fosforilacijom, koju katalizuje Ca2+-aktivirana proteinska kinaza.
Reference
- ↑ Friedman, P.A., Kappelman, A.H. and Kaufman, S. (1972). „Partial purification and characterization of tryptophan hydroxylase from rabbit hindbrain”. J. Biol. Chem. 247: 4165-4173. PMID 4402511.
- ↑ Hamon, M., Bourgoin, S., Artaud, F. and Glowinski, J. (1979). „The role of intraneuronal 5-HT and of tryptophan hydroxylase activation in the control of 5-HT synthesis in rat brain slices incubated in K+-enriched medium”. J. Neurochem. 33: 1031-1042. PMID 315449.
- ↑ Ichiyama, A., Nakamura, S., Nishizuka, Y. and Hayaishi, O. (1970). „Enzymic studies on the biosynthesis of serotonin in mammalian brain”. J. Biol. Chem. 245: 1699-1709. PMID 5309585.
- ↑ Jequier, E., Robinson, B.S., Lovenberg, W. and Sjoerdsma, A. (1969). „Further studies on tryptophan hydroxylase in rat brainstem and beef pineal”. Biochem. Pharmacol. 18: 1071-1081. PMID 5789774.
- ↑ Wang, L., Erlandsen, H., Haavik, J., Knappskog, P.M. and Stevens, R.C. (2002). „Three-dimensional structure of human tryptophan hydroxylase and its implications for the biosynthesis of the neurotransmitters serotonin and melatonin”. Biochemistry 41: 12569-12574. PMID 12379098.
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 Tryptophan+5-monooxygenase
- 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
