1.11.2.4: fatty-acid peroxygenase
This is an abbreviated version!
For detailed information about fatty-acid peroxygenase, go to the full flat file.
Word Map on EC 1.11.2.4
-
1.11.2.4
-
peroxygenases
-
oletje
-
alkene
-
self-sufficient
-
cumene
-
phanerochaete
-
chrysosporium
-
monooxygenation
-
paucimobilis
-
peroxygenation
- 1.11.2.4
-
peroxygenases
-
oletje
- alkene
-
self-sufficient
- cumene
-
phanerochaete
-
chrysosporium
-
monooxygenation
- paucimobilis
-
peroxygenation
Reaction
Synonyms
alpha-fatty acid hydroxylase, CYP152A1, CYP152A2, CYP152B1, CYP505, cytochrome P450 monooxygenase, cytochrome P450BSbeta, fatty-acid hydroxylase, fatty-acid subterminal hydroxylase, hydrogen peroxide-dependent cytochrome P450BSbeta, hydrogen peroxide-dependent fatty acid alpha-hydroxylase, hydrogen peroxide-dependent peroxygenase cytochrome P450, P450 BM-3 peroxygenase 21B3, P450 peroxygenase, P450BSbeta, P450CLA, P450foxy, P450SPalpha, peroxygenase cytochrome P450, peroxygenase P450, peroxygenase P450SPalpha
ECTree
Advanced search results
Reference
Reference on EC 1.11.2.4 - fatty-acid peroxygenase
for references in articles please use BRENDA:EC1.11.2.4
Please use the Reference Search for a specific query.
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
Lee, D.S.; Yamada, A.; Matsunaga, I.; Ichihara, K.; Adachi, S.; Park, S.Y.; Shiro, Y.
Crystallization and preliminary X-ray diffraction analysis of fatty-acid hydroxylase cytochrome P450BSbeta from Bacillus subtilis
Acta Crystallogr. Sect. D
58
687-689
2002
Bacillus subtilis (O31440), Bacillus subtilis
Matsunaga, I.; Ueda, A.; Sumimoto, T.; Ichihara, K.; Ayata, M.; Ogura, H.
Site-directed mutagenesis of the putative distal helix of peroxygenase cytochrome P450
Arch. Biochem. Biophys.
394
45-53
2001
Bacillus subtilis (O31440)
Girhard, M.; Schuster, S.; Dietrich, M.; Durre, P.; Urlacher, V.B.
Cytochrome P450 monooxygenase from Clostridium acetobutylicum: a new alpha-fatty acid hydroxylase
Biochem. Biophys. Res. Commun.
362
114-119
2007
Clostridium acetobutylicum (Q97DZ0), Clostridium acetobutylicum
Matsunaga, I.; Yamada, A.; Lee, D.S.; Obayashi, E.; Fujiwara, N.; Kobayashi, K.; Ogura, H.; Shiro, Y.
Enzymatic reaction of hydrogen peroxide-dependent peroxygenase cytochrome P450s: kinetic deuterium isotope effects and analyses by resonance Raman spectroscopy
Biochemistry
41
1886-1892
2002
Bacillus subtilis (O31440), Sphingomonas paucimobilis
Salazar, O.; Cirino, P.C.; Arnold, F.H.
Thermostabilization of a cytochrome P450 peroxygenase
ChemBioChem
4
891-893
2003
Priestia megaterium
Matsunaga, I.; Shiro, Y.
Peroxide-utilizing biocatalysts: structural and functional diversity of heme-containing enzymes
Curr. Opin. Chem. Biol.
8
127-132
2004
Sphingomonas paucimobilis, Bacillus subtilis (O31440)
Matsunaga, I.; Sumimoto, T.; Ayata, M.; Ogura, H.
Functional modulation of a peroxygenase cytochrome P450: novel insight into the mechanisms of peroxygenase and peroxidase enzymes
FEBS Lett.
528
90-94
2002
Bacillus subtilis (O31440)
Imai, Y.; Matsunaga, I.; Kusunose, E.; Ichihara, K.
Unique heme environment at the putative distal region of hydrogen peroxide-dependent fatty acid alpha-hydroxylase from Sphingomonas paucimobilis (peroxygenase P450SPalpha)
J. Biochem.
128
189-194
2000
Sphingomonas paucimobilis
Kitazume, T.; Takaya, N.; Nakayama, N.; Shoun, H.
Fusarium oxysporum fatty-acid subterminal hydroxylase (CYP505) is a membrane-bound eukaryotic counterpart of Bacillus megaterium cytochrome P450BM3
J. Biol. Chem.
275
39734-39740
2000
Fusarium oxysporum (Q9Y8G7), Fusarium oxysporum, Fusarium oxysporum MT-811 (Q9Y8G7)
Lee, D.-S.; Yamada, A.; Sugimoto, H.; Matsunaga, I.; Ogura, H.; Ichihara, K.; Adachi, S.-i.; Park, S.-Y.; Shiro, Y.
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
2003
Bacillus subtilis (O31440)
Shoji, O.; Wiese, C.; Fujishiro, T.; Shirataki, C.; Wunsch, B.; Watanabe, Y.
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
2010
Bacillus subtilis (O31440)
html completed