Triptofan N-monooksigenaza
| Triptofan N-monooksigenaza | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifikatori | |||||||||
| EC broj | 1.14.13.125 | ||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB | RCSB PDB PDBe PDBj PDBsum | ||||||||
| |||||||||
Triptofan N-monooksigenaza (EC 1.14.13.125, triptofanska N-hidroksilaza, CYP79B1, CYP79B2, CYP79B3) je enzim sa sistematskim imenom L-triptofan,NADPH:kiseonik oksidoreduktaza (N-hidroksilacija).[1][2][3][4] Ovaj enzim katalizuje sledeću hemijsku reakciju
- L-triptofan + 2 O2 + 2 NADPH + 2 H+ (E)-indol-3-ilacetaldoksim + 2 NADP+ + CO2 + 3H2O (sveukupna reakcija)
- (1a) L-triptofan + O2 + NADPH + H+ N-hidroksi-L-triptofan + NADP+ +H2O
- (1b) N-hidroksi-L-triptofan + O2 + NADPH + H+ N,N-dihidroksi-L-triptofan + NADP+ +H2O
- (1c) N,N-dihidroksi-L-triptofan (E)-indol-3-ilacetaldoksim + CO2 +H2O
Ovaj enzim je hem-tiolatni protein (P-450). On katalizuje dve sukcesivne N-hidroksilacije L-triptofana.
Reference
- ↑ Mikkelsen, M.D., Hansen, C.H., Wittstock, U. and Halkier, B.A. (2000). „Cytochrome P450 CYP79B2 from Arabidopsis catalyzes the conversion of tryptophan to indole-3-acetaldoxime, a precursor of indole glucosinolates and indole-3-acetic acid”. J. Biol. Chem. 275: 33712-33717. PMID 10922360.
- ↑ Hull, A.K., Vij, R. and Celenza, J.L. (2000). „Arabidopsis cytochrome P450s that catalyze the first step of tryptophan-dependent indole-3-acetic acid biosynthesis”. Proc. Natl. Acad. Sci. USA 97: 2379-2384. PMID 10681464.
- ↑ Zhao, Y., Hull, A.K., Gupta, N.R., Goss, K.A., Alonso, J., Ecker, J.R., Normanly, J., Chory, J. and Celenza, J.L. (2002). „Trp-dependent auxin biosynthesis in Arabidopsis: involvement of cytochrome P450s CYP79B2 and CYP79B3”. Genes Dev. 16: 3100-3112. PMID 12464638.
- ↑ Naur, P., Hansen, C.H., Bak, S., Hansen, B.G., Jensen, N.B., Nielsen, H.L. and Halkier, B.A. (2003). „CYP79B1 from Sinapis alba converts tryptophan to indole-3-acetaldoxime”. Arch. Biochem. Biophys. 409: 235-241. PMID 12464264.
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+N-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
