Tirozin 3-monooksigenaza
| Tirozin 3-monooksigenaza | |||||||||
|---|---|---|---|---|---|---|---|---|---|
 | |||||||||
| Identifikatori | |||||||||
| EC broj | 1.14.16.2 | ||||||||
| CAS broj | 9036-22-0 | ||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB | RCSB PDB PDBe PDBj PDBsum | ||||||||
| |||||||||
Tirozin 3-monooksigenaza (EC 1.14.16.2, L-tirozinska hidroksilaza, tirozinska 3-hidroksilaza, tirozinska hidroksilaza) je enzim sa sistematskim imenom L-tirozin,tetrahidrobiopterin:kiseonik oksidoreduktaza (3-hidroksilacija).[1][2][3][4][5] Ovaj enzim katalizuje sledeću hemijsku reakciju
- L-tirozin + tetrahidrobiopterin + O2 L-dopa + 4a-hidroksitetrahidrobiopterin
Aktivni centar sadrži mononuklearno gvožđe(II). Ovaj enzim se aktivira fosforilacijom.
Reference
- ↑ El Mestikawy, S., Glowinski, J. and Hamon, M. (1983). „Tyrosine hydroxylase activation in depolarized dopaminergic terminals -involvement of Ca2+-dependent phosphorylation”. Nature (Lond.) 302: 830-832. PMID 6133218.
- ↑ Ikeda, M., Levitt, M. and Udenfriend, S. (1967). „Phenylalanine as substrate and inhibitor of tyrosine hydroxylase”. Arch. Biochem. Biophys. 120: 420-427. PMID 6033458.
- ↑ Nagatsu, T., Levitt, M. and Udenfriend, S. (1964). „Tyrosine hydroxylase. The initial step in norepinephrine biosynthesis”. J. Biol. Chem. 239: 2910-2917. PMID 14216443.
- ↑ Pigeon, D., Drissi-Daoudi, R., Gros, F. and Thibault, J. (1986). „Copurification of tyrosine hydroxylase from rat pheochromocytoma by protein kinase”. C. R. Acad. Sci. III 302: 435-438. PMID 2872947.
- ↑ Goodwill, K.E., Sabatier, C., Marks, C., Raag, R., Fitzpatrick, P.F. and Stevens, R.C. (1997). „Crystal structure of tyrosine hydroxylase at 2.3 Å and its implications for inherited neurodegenerative diseases”. Nat. Struct. Biol. 4: 578-585. PMID 9228951.
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 Tyrosine+3-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
