Fatty-acid peroxygenase
Fatty-acid peroxygenase | |||||||||
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Identifiers | |||||||||
EC number | 1.11.2.4 | ||||||||
Databases | |||||||||
IntEnz | IntEnz view | ||||||||
BRENDA | BRENDA entry | ||||||||
ExPASy | NiceZyme view | ||||||||
KEGG | KEGG entry | ||||||||
MetaCyc | metabolic pathway | ||||||||
PRIAM | profile | ||||||||
PDB structures | RCSB PDB PDBe PDBsum | ||||||||
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Fatty-acid peroxygenase (EC 1.11.2.4, fatty acid hydroxylase (ambiguous), P450 peroxygenase, CYP152A1, P450BS, P450SPalpha) is an enzyme with systematic name fatty acid:hydroperoxide oxidoreductase (RH-hydroxylating).[1][2][3][4][5][6][7][8] This enzyme catalyses the following chemical reaction
- fatty acid + H2O2 3- or 2-hydroxy fatty acid + H2O
Fatty-acid peroxygenase is a cytosolic heme-thiolate protein.
References
- ↑ Matsunaga, I.; Yamada, M.; Kusunose, E.; Nishiuchi, Y.; Yano, I.; Ichihara, K. (1996). "Direct involvement of hydrogen peroxide in bacterial α-hydroxylation of fatty acid". FEBS Lett. 386 (2-3): 252–254. doi:10.1016/0014-5793(96)00451-6. PMID 8647293.
- ↑ Matsunaga, I.; Yamada, M.; Kusunose, E.; Miki, T.; Ichihara, K. (1998). "Further characterization of hydrogen peroxide-dependent fatty acid α-hydroxylase from Sphingomonas paucimobilis". J. Biochem. 124 (1): 105–110. doi:10.1093/oxfordjournals.jbchem.a022068. PMID 9644252.
- ↑ Matsunaga, I.; Ueda, A.; Fujiwara, N.; Sumimoto, T.; Ichihara, K. (1999). "Characterization of the ybdT gene product of Bacillus subtilis: novel fatty acid β-hydroxylating cytochrome P450". Lipids. 34 (8): 841–846. doi:10.1007/s11745-999-0431-3. PMID 10529095.
- ↑ Imai, Y.; Matsunaga, I.; Kusunose, E.; 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 (2): 189–194. doi:10.1093/oxfordjournals.jbchem.a022740. PMID 10920253.
- ↑ Matsunaga, I.; Yamada, A.; Lee, D.S.; Obayashi, E.; Fujiwara, N.; Kobayashi, K.; Ogura, H.; Shiro, Y. (2002). "Enzymatic reaction of hydrogen peroxide-dependent peroxygenase cytochrome P450s: kinetic deuterium isotope effects and analyses by resonance Raman spectroscopy". Biochemistry. 41 (6): 1886–1892. doi:10.1021/bi011883p. PMID 11827534.
- ↑ Lee, D.S.; Yamada, A.; Sugimoto, H.; Matsunaga, I.; Ogura, H.; Ichihara, K.; Adachi, S.; Park, S.Y.; 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 (11): 9761–9767. doi:10.1074/jbc.M211575200. PMID 12519760.
- ↑ Matsunaga, I.; Shiro, Y. (2004). "Peroxide-utilizing biocatalysts: structural and functional diversity of heme-containing enzymes". Curr. Opin. Chem. Biol. 8 (2): 127–132. doi:10.1016/j.cbpa.2004.01.001. PMID 15062772.
- ↑ Shoji, O.; Wiese, C.; Fujishiro, T.; Shirataki, C.; Wunsch, B.; 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 (7): 1109–1115. doi:10.1007/s00775-010-0671-9. PMID 20490877.
External links
- Fatty-acid peroxygenase at the US National Library of Medicine Medical Subject Headings (MeSH)
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