Masna-kiselina peroksigenaza — разлика између измена
Садржај обрисан Садржај додат
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Верзија на датум 26. јануар 2013. у 06:55
Masna-kiselina peroksigenaza | |||||||||
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Identifikatori | |||||||||
EC broj | 1.11.2.4 | ||||||||
Baze podataka | |||||||||
IntEnz | IntEnz pregled | ||||||||
BRENDA | BRENDA pristup | ||||||||
ExPASy | NiceZyme pregled | ||||||||
KEGG | KEGG pristup | ||||||||
MetaCyc | metabolički put | ||||||||
PRIAM | profil | ||||||||
Strukture PBP | RCSB PDB PDBe PDBj PDBsum | ||||||||
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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.
Spoljašnje vezе
- Fatty-acid+peroxygenase на US National Library of Medicine Medical Subject Headings (MeSH)