Masna-kiselina peroksigenaza
| Masna-kiselina peroksigenaza | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifikatori | |||||||||
| EC broj | 1.11.2.4 | ||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB | RCSB PDB PDBe PDBj PDBsum | ||||||||
| |||||||||
Masna-kiselina peroksigenaza (EC 1.11.2.4, masno kiselinska hidroksilaza (nespecifična), P450 peroksigenaza, CYP152A1, P450BS, P450SPalfa) je enzim sa sistematskim imenom masna kiselina:hidroperoksid oksidoreduktaza (RH-hidroksilacija).[1][2][3][4][5][6][7][8] Ovaj enzim katalizuje sledeću hemijsku reakciju
- masna kiselina + H2O2 3- ili 2-hidroksi masna kiselina + H2O
Ovaj citosolni hem-tiolatni protein je sekventno homologan sa P450 monooksigenazama. Za njegov rad nisu neophodni NAD(P)H, dioksigen i specifične reduktaze. Enzime ovog tipa formiraju bakterije (e.g. Sphingomonas paucimobilis, Bacillus subtilis).
Reference
- ↑ Matsunaga, I., Yamada, M., Kusunose, E., Nishiuchi, Y., Yano, I. and Ichihara, K. (1996). „Direct involvement of hydrogen peroxide in bacterial α-hydroxylation of fatty acid”. FEBS Lett. 386: 252-254. PMID 8647293.
- ↑ Matsunaga, I., Yamada, M., Kusunose, E., Miki, T. and Ichihara, K. (1998). „Further characterization of hydrogen peroxide-dependent fatty acid α-hydroxylase from Sphingomonas paucimobilis”. J. Biochem. 124: 105-110. PMID 9644252.
- ↑ Matsunaga, I., Ueda, A., Fujiwara, N., Sumimoto, T. and Ichihara, K. (1999). „Characterization of the ybdT gene product of Bacillus subtilis: novel fatty acid β-hydroxylating cytochrome P450”. Lipids 34: 841-846. PMID 10529095.
- ↑ Imai, Y., Matsunaga, I., Kusunose, E. and Ichihara, K. (2000). „Unique heme environment at the putative distal region of hydrogen peroxide-dependent fatty acid α-hydroxylase from Sphingomonas paucimobilis (peroxygenase P450SPα)”. J. Biochem. 128: 189-194. PMID 10920253.
- ↑ Matsunaga, I., Yamada, A., Lee, D.S., Obayashi, E., Fujiwara, N., Kobayashi, K., Ogura, H. and Shiro, Y. (2002). „Enzymatic reaction of hydrogen peroxide-dependent peroxygenase cytochrome P450s: kinetic deuterium isotope effects and analyses by resonance Raman spectroscopy”. Biochemistry 41: 1886-1892. PMID 11827534.
- ↑ Lee, D.S., Yamada, A., Sugimoto, H., Matsunaga, I., Ogura, H., Ichihara, K., Adachi, S., Park, S.Y. and Shiro, Y. (2003). „Substrate recognition and molecular mechanism of fatty acid hydroxylation by cytochrome P450 from Bacillus subtilis. Crystallographic, spectroscopic, and mutational studies”. J. Biol. Chem. 278: 9761-9767. PMID 12519760.
- ↑ Matsunaga, I. and Shiro, Y. (2004). „Peroxide-utilizing biocatalysts: structural and functional diversity of heme-containing enzymes”. Curr. Opin. Chem. Biol. 8: 127-132. PMID 15062772.
- ↑ Shoji, O., Wiese, C., Fujishiro, T., Shirataki, C., Wunsch, B. and Watanabe, Y. (2010). „Aromatic C-H bond hydroxylation by P450 peroxygenases: a facile colorimetric assay for monooxygenation activities of enzymes based on Russig’s blue formation”. J. Biol. Inorg. Chem. 15: 1109-1115. PMID 20490877.
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 Fatty-acid+peroxygenase
- 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
