1.11.2.4	1-methoxynaphthalene + H2O2	in the presence of heptanoic acid as a decoy molecule	Bacillus subtilis	4-methoxy-1-naphthol + H2O	-	?	413822	
1.11.2.4	12-4-nitrophenoxycarboxylic acid + H2O2	-	Priestia megaterium	4-nitrophenolate + ?	-	?	413850	
1.11.2.4	2-hydroxylauric acid + H2O2	-	Sphingomonas paucimobilis	?	-	?	413948	
1.11.2.4	2-hydroxylauric acid + H2O2	-	Bacillus subtilis	?	-	?	413948	
1.11.2.4	3,5,3',5'-tetramethylbenzidine + H2O2	-	Sphingomonas paucimobilis	?	-	?	413198	
1.11.2.4	3,5,3',5'-tetramethylbenzidine + H2O2	-	Bacillus subtilis	?	-	?	413198	
1.11.2.4	3,5,3',5'-tetramethylbenzidine + H2O2	a myristic acid-dependent reaction, when deuterated myristic acid is used as a substrate to decrease hydroxylation activity, the rate of 3,5,3',5'-tetramethylbenzidine oxidation increases	Bacillus subtilis	?	-	?	413198	
1.11.2.4	fatty acid + H2O2	-	Sphingomonas paucimobilis	?	-	?	413381	
1.11.2.4	fatty acid + H2O2	-	Bacillus subtilis	?	-	?	413381	
1.11.2.4	lauric acid + H2O2	-	Sphingomonas paucimobilis	?	-	?	414797	
1.11.2.4	lauric acid + H2O2	after 2 min of reaction conversion of 0.06 mM lauric acid reaches 55%	Clostridium acetobutylicum	?	-	?	414797	
1.11.2.4	additional information	a reductase and NAD(P)H are not required for activity	Bacillus subtilis	?	-	?	89	
1.11.2.4	additional information	CYP152A2 has a clear preference for hydroxylation at alpha-position	Clostridium acetobutylicum	?	-	?	89	
1.11.2.4	additional information	P450 BM-3 peroxygenase 21B3 is a laboratory-evolved variant of the P450 BM-3 heme domain which functions as an H2O2-driven hydroxylase (peroxygenase) and does not require NADPH, O2 , or the reductase	Priestia megaterium	?	-	?	89	
1.11.2.4	additional information	P450BSbeta produces alpha- and beta-hydroxylated products at 33 and 67%, respectively	Sphingomonas paucimobilis	?	-	?	89	
1.11.2.4	additional information	P450BSbeta produces alpha- and beta-hydroxylated products at 33 and 67%, respectively	Bacillus subtilis	?	-	?	89	
1.11.2.4	additional information	P450BSbeta produces both the beta-OH (60%) and the alpha-OH (40%) fatty acids. Ferredoxin, ferredoxin reductase, and P450 reductase systems do not appear to function in P450BSbeta reactions. P450BSbeta does not require any electrons and protons for catalytic activity, because it utilizes H2O2 as an oxidant instead of O2/2e-/2H+. This enzyme requires neither a reductase nor a proton delivery system	Bacillus subtilis	?	-	?	89	
1.11.2.4	additional information	P450SPalpha produces the alpha-hydroxylated products at 100%	Sphingomonas paucimobilis	?	-	?	89	
1.11.2.4	additional information	P450SPalpha produces the alpha-hydroxylated products at 100%	Bacillus subtilis	?	-	?	89	
1.11.2.4	additional information	the enzyme catalyzes the subterminal (omega-1 to omega-3) hydroxylation of fatty acids. The enzyme can complete its function without the aid of other proteinaceous components such as NADPH-cytochrome P450 oxidoreductase	Fusarium oxysporum	?	-	?	89	
1.11.2.4	additional information	the enzyme never requires a supply of electrons or protons	Sphingomonas paucimobilis	?	-	?	89	
1.11.2.4	additional information	the enzyme never requires a supply of electrons or protons	Bacillus subtilis	?	-	?	89	
1.11.2.4	additional information	even chain fatty acids with chain length between C10 and C16 are the substrates for P450CLA	Clostridium acetobutylicum	?	-	?	89	
1.11.2.4	additional information	the initial activities of P450CLA in reconstitution systems based on the use of oxygen and NADPH are either much lower than those measured with H2O2 or not measurable at all, no conversion is detected for caprylic acid and stearic acid	Clostridium acetobutylicum	?	-	?	89	
1.11.2.4	additional information	the enzyme catalyzes the subterminal (omega-1 to omega-3) hydroxylation of fatty acids. The enzyme can complete its function without the aid of other proteinaceous components such as NADPH-cytochrome P450 oxidoreductase	Fusarium oxysporum MT-811	?	-	?	89	
1.11.2.4	myristic acid + cumene hydroperoxide	-	Bacillus subtilis	?	-	?	414885	
1.11.2.4	myristic acid + H2O2	-	Sphingomonas paucimobilis	?	-	?	413466	
1.11.2.4	myristic acid + H2O2	-	Fusarium oxysporum	?	-	?	413466	
1.11.2.4	myristic acid + H2O2	-	Bacillus subtilis	?	-	?	413466	
1.11.2.4	myristic acid + H2O2	-	Clostridium acetobutylicum	?	-	?	413466	
1.11.2.4	myristic acid + H2O2	CYP152A1 attacks the beta-carbon as well as the alpha-carbon of myristic acid	Bacillus subtilis	?	-	?	413466	
1.11.2.4	myristic acid + H2O2	highest activity, after 2 min of reaction conversion of 0.06 mM myristic acid reaches 40%	Clostridium acetobutylicum	?	-	?	413466	
1.11.2.4	myristic acid + H2O2	-	Fusarium oxysporum MT-811	?	-	?	413466	
1.11.2.4	myristic acid + H2O2	-	Sphingomonas paucimobilis	2-hydroxy-myristic acid	-	?	414886	
1.11.2.4	myristic acid + H2O2	-	Bacillus subtilis	2-hydroxy-myristic acid	-	?	414886	
1.11.2.4	palmitic acid + H2O2	-	Bacillus subtilis	?	-	?	413521	
1.11.2.4	palmitic acid + H2O2	after 2 min of reaction conversion of 0.06 mM palmitic acid reaches 60%	Clostridium acetobutylicum	?	-	?	413521