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Information on EC 1.11.2.4 - fatty-acid peroxygenase
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1.11.2.4 fatty-acid peroxygenaseIUBMB Comments
A cytosolic heme-thiolate protein with sequence homology to P-450 monooxygenases. Unlike the latter, it needs neither NAD(P)H, dioxygen nor specific reductases for function. Enzymes of this type are produced by bacteria (e.g. Sphingomonas paucimobilis, Bacillus subtilis). Catalytic turnover rates are high compared with those of monooxygenation reactions as well as peroxide shunt reactions catalysed by the common P-450s. A model substrate is myristate, but other saturated and unsaturated fatty acids are also hydroxylated. Oxidizes the peroxidase substrate 3,3',5,5'-tetramethylbenzidine (TMB) and peroxygenates aromatic substrates in a fatty-acid-dependent reaction.
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Word Map
- 1.11.2.4
-
peroxygenases
-
oletje
- alkene
-
self-sufficient
- cumene
-
phanerochaete
-
chrysosporium
-
monooxygenation
- paucimobilis
-
peroxygenation
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
Synonyms
p450foxy, cyp152a2, cyp152a1, cyp505, p450 peroxygenase, fatty-acid hydroxylase, p450bsbeta, peroxygenase p450, cyp152b1, cytochrome p450bsbeta, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
CYP505
fatty-acid subterminal hydroxylase
hydrogen peroxide-dependent peroxygenase cytochrome P450
P450foxy
peroxygenase P450
CYP505
bifunctional fusion enzyme, the primary structure of P450foxy can be divided into P450, P450 reductase and their linker domains
CYP505
bifunctional fusion enzyme, the primary structure of P450foxy can be divided into P450, P450 reductase and their linker domains
-
P450foxy
bifunctional fusion enzyme, the primary structure of P450foxy can be divided into P450, P450 reductase and their linker domains
P450foxy
bifunctional fusion enzyme, the primary structure of P450foxy can be divided into P450, P450 reductase and their linker domains
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
fatty acid + H2O2 = 3- or 2-hydroxy fatty acid + H2O
-
-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
monooxygenation
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SYSTEMATIC NAME
IUBMB Comments
fatty acid:hydroperoxide oxidoreductase (RH-hydroxylating)
A cytosolic heme-thiolate protein with sequence homology to P-450 monooxygenases. Unlike the latter, it needs neither NAD(P)H, dioxygen nor specific reductases for function. Enzymes of this type are produced by bacteria (e.g. Sphingomonas paucimobilis, Bacillus subtilis). Catalytic turnover rates are high compared with those of monooxygenation reactions as well as peroxide shunt reactions catalysed by the common P-450s. A model substrate is myristate, but other saturated and unsaturated fatty acids are also hydroxylated. Oxidizes the peroxidase substrate 3,3',5,5'-tetramethylbenzidine (TMB) and peroxygenates aromatic substrates in a fatty-acid-dependent reaction.
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
1-methoxynaphthalene + H2O2
4-methoxy-1-naphthol + H2O
in the presence of heptanoic acid as a decoy molecule
-
-
?
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
-
-
?
lauric acid + H2O2
?
after 2 min of reaction conversion of 0.06 mM lauric acid reaches 55%
-
-
?
myristic acid + H2O2
?
-
-
-
?
myristic acid + H2O2
?
CYP152A1 attacks the beta-carbon as well as the alpha-carbon of myristic acid
-
-
?
myristic acid + H2O2
?
highest activity, after 2 min of reaction conversion of 0.06 mM myristic acid reaches 40%
-
-
?
palmitic acid + H2O2
?
after 2 min of reaction conversion of 0.06 mM palmitic acid reaches 60%
-
-
?
additional information
?
-
a reductase and NAD(P)H are not required for activity
-
-
?
additional information
?
-
P450BSbeta produces alpha- and beta-hydroxylated products at 33 and 67%, respectively
-
-
?
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
-
-
?
additional information
?
-
P450SPalpha produces the alpha-hydroxylated products at 100%
-
-
?
additional information
?
-
the enzyme never requires a supply of electrons or protons
-
-
?
additional information
?
-
CYP152A2 has a clear preference for hydroxylation at alpha-position
-
-
?
additional information
?
-
-
CYP152A2 has a clear preference for hydroxylation at alpha-position
-
-
?
additional information
?
-
even chain fatty acids with chain length between C10 and C16 are the substrates for P450CLA
-
-
?
additional information
?
-
-
even chain fatty acids with chain length between C10 and C16 are the substrates for P450CLA
-
-
?
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
-
-
?
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
-
-
?
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
-
-
?
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
-
-
?
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
-
-
?
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
-
-
?
additional information
?
-
-
P450BSbeta produces alpha- and beta-hydroxylated products at 33 and 67%, respectively
-
-
?
additional information
?
-
-
P450SPalpha produces the alpha-hydroxylated products at 100%
-
-
?
additional information
?
-
-
the enzyme never requires a supply of electrons or protons
-
-
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
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
-
-
?
myristic acid + H2O2
?
CYP152A1 attacks the beta-carbon as well as the alpha-carbon of myristic acid
-
-
?
additional information
?
-
a reductase and NAD(P)H are not required for activity
-
-
?
additional information
?
-
P450BSbeta produces alpha- and beta-hydroxylated products at 33 and 67%, respectively
-
-
?
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
-
-
?
additional information
?
-
P450SPalpha produces the alpha-hydroxylated products at 100%
-
-
?
additional information
?
-
the enzyme never requires a supply of electrons or protons
-
-
?
additional information
?
-
CYP152A2 has a clear preference for hydroxylation at alpha-position
-
-
?
additional information
?
-
-
CYP152A2 has a clear preference for hydroxylation at alpha-position
-
-
?
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
-
-
?
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
-
-
?
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
-
-
?
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
-
-
?
additional information
?
-
-
P450BSbeta produces alpha- and beta-hydroxylated products at 33 and 67%, respectively
-
-
?
additional information
?
-
-
P450SPalpha produces the alpha-hydroxylated products at 100%
-
-
?
additional information
?
-
-
the enzyme never requires a supply of electrons or protons
-
-
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
3,5,3',5'-tetramethylbenzidine
3,5,3',5'-tetramethylbenzidine as an additional substrate intercepts the hydroxylation of myristic acid
H2O2
although a high concentration of hydrogen peroxide of 0.2 mM is necessary for high activities of the enzyme, it leads to a fast enzyme inactivation within 2-4 min
myristic acid
myristic acid hydroxylation is inhibited by 3,5,3',5'-tetramethylbenzidine oxidation in a 3,5,3',5'-tetramethylbenzidine concentration-dependent manner
additional information
-
the fatty acid alpha-hydroxylase activity of P450SPbeta is not affected when 80% of CO (by volume) is used as the gas phase in the reaction
-
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.026
3,5,3',5'-tetramethylbenzidine
pH and temperature not specified in the publication
0.11
cumene hydroperoxide
mutant enzyme R242A, using myristic acid as cosubstrate, in 0.1 M potassium phosphate buffer (pH 6.7), at 25°C
0.2
cumene hydroperoxide
wild type enzyme, using myristic acid as cosubstrate, in 0.1 M potassium phosphate buffer (pH 6.7), at 25°C
0.24
cumene hydroperoxide
mutant enzyme R242K, using myristic acid as cosubstrate, in 0.1 M potassium phosphate buffer (pH 6.7), at 25°C
0.021
H2O2
wild type enzyme, using myristic acid as cosubstrate, in 0.1 M potassium phosphate buffer (pH 6.7), at 25°C
0.21
H2O2
mutant enzyme R242K, using myristic acid as cosubstrate, in 0.1 M potassium phosphate buffer (pH 6.7), at 25°C
4.4
H2O2
mutant enzyme R242A, using myristic acid as cosubstrate, in 0.1 M potassium phosphate buffer (pH 6.7), at 25°C
0.026
myristic acid
pH and temperature not specified in the publication
0.041
myristic acid
-
pH and temperature not specified in the publication
0.058
myristic acid
pH and temperature not specified in the publication
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
physiological function
CYP152A2 is a rapid hydrogen peroxide scavenging enzyme
Show AA Sequence and Transmembrane Helices (183 entries)
Please use the AA Sequence and Transmembrane Helices Search for a specific query.
Please use the AA Sequence and Transmembrane Helices Search for a specific query.
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
48000
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
ferric P450BSbeta in the substrate-bound form, sitting drop vapor diffusion method, using 10% (w/v) polyethylene glycol 3350 and 50 mM MES at pH 6.8, at 20°C
sitting drop vapor diffusion method, using 10% (w/v) PEG 4000 and 50 mM MES (pH 6.8) or 10% (w/v) PEG 4000, 0.15 mM magnesium acetate and 50 mM MES (pH 6.5) in the presence of 2 mM myristic acid
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
A246K
the mutant shows a large decrease in activity and a roughly 19fold lower affinity for myristic acid than the wild type enzyme
A246S
the mutation decreases the catalytic activity, but does not affect affinity for myristic acid
A246V
the mutant shows slightly reduced activity and moderately reduced affinity for myristic acid
F250K
the mutant shows decreased specific activity compared to the wild type enzyme
F79L
the specific activity is reduced by half compared to the wild type enzyme
F79L/V170F
the double mutant exhibits 10% of the activity of the wild type enzyme
I244K
the mutant shows decreased specific activity compared to the wild type enzyme
I247K
the mutant shows decreased specific activity compared to the wild type enzyme
L237K
the mutants shows specific activity similar to the wild type enzyme
L241K
the mutants shows specific activity similar to the wild type enzyme
L251K
the mutant shows decreased specific activity compared to the wild type enzyme
P243A
the mutant shows decreased specific activity compared to the wild type enzyme and gives an absorption spectrum that is not characteristic of a nitrogenous ligand-bound form of a ferric P450
P243H
inactive, the mutant gives an absorption spectrum characteristic of a nitrogenous ligand-bound form of a ferric P450
P243K
inactive, the mutant gives an absorption spectrum characteristic of a nitrogenous ligand-bound form of a ferric P450
P243S
the mutant shows decreased specific activity compared to the wild type enzyme and gives an absorption spectrum that is not characteristic of a nitrogenous ligand-bound form of a ferric P450
R242A
the mutant shows about a 5fold lower affinity than the wild type for myristic acid, if cumene hydroperoxide is used instead of H2o2, however, the Km value is not affected much by this substitution
R242K
S248K
the mutant shows decreased specific activity compared to the wild type enzyme
V170F
V245K
the mutant shows decreased specific activity compared to the wild type enzyme
Y249K
the mutant shows decreased specific activity compared to the wild type enzyme
F878A
-
P450 BM-3 heme domain containing the single amino acid substitution F87A is significantly more active than wild type heme domain in reactions driven by H2O2
R242K
the mutant enzyme bound with deuterated myristic acid shows greatly increased rate of 3,5,3',5'-tetramethylbenzidine oxidation
R242K
the mutant shows a large decrease in activity for myristic acid and H2O2, if cumene hydroperoxide is used instead of H2o2, however, the Km value is not affected much by this substitution
V170F
the hydroxylation activity of V170F for myristic acid is about one third of that of the wild type, but its catalytic activities for aromatic hydroxylation in the presence of octanoic acid or nonanoic acid are comparable to the catalytic activity of the wild type with pentanoic acid
V170F
the mutant exhibits 30% of the activity of the wild type enzyme
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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
brenda
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)
brenda
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
brenda
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
Sphingomonas paucimobilis, Bacillus subtilis (O31440)
brenda
Salazar, O.; Cirino, P.C.; Arnold, F.H.
Thermostabilization of a cytochrome P450 peroxygenase
ChemBioChem
4
891-893
2003
Priestia megaterium
brenda
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)
brenda
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)
brenda
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
brenda
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)
brenda
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)
brenda
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 Russigs blue formation
J. Biol. Inorg. Chem.
15
1109-1115
2010
Bacillus subtilis (O31440)
brenda
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