Information on EC 1.11.2.4 - fatty-acid peroxygenase

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The expected taxonomic range for this enzyme is: Bacteria, Eukaryota

EC NUMBER
COMMENTARY hide
1.11.2.4
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RECOMMENDED NAME
GeneOntology No.
fatty-acid peroxygenase
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
fatty acid + H2O2 = 3- or 2-hydroxy fatty acid + H2O
show the reaction diagram
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
monooxygenation
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.
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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UniProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
CYP152A2 is a rapid hydrogen peroxide scavenging enzyme
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
1-methoxynaphthalene + H2O2
4-methoxy-1-naphthol + H2O
show the reaction diagram
in the presence of heptanoic acid as a decoy molecule
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?
12-4-nitrophenoxycarboxylic acid + H2O2
4-nitrophenolate + ?
show the reaction diagram
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?
2-hydroxylauric acid + H2O2
?
show the reaction diagram
3,5,3',5'-tetramethylbenzidine + H2O2
?
show the reaction diagram
fatty acid + H2O2
?
show the reaction diagram
lauric acid + H2O2
?
show the reaction diagram
myristic acid + cumene hydroperoxide
?
show the reaction diagram
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-
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?
myristic acid + H2O2
2-hydroxy-myristic acid
show the reaction diagram
myristic acid + H2O2
?
show the reaction diagram
palmitic acid + H2O2
?
show the reaction diagram
additional information
?
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NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
3,5,3',5'-tetramethylbenzidine + H2O2
?
show the reaction diagram
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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
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?
fatty acid + H2O2
?
show the reaction diagram
myristic acid + H2O2
?
show the reaction diagram
palmitic acid + H2O2
?
show the reaction diagram
O31440
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?
additional information
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
3,5,3',5'-tetramethylbenzidine
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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
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myristic acid hydroxylation is inhibited by 3,5,3',5'-tetramethylbenzidine oxidation in a 3,5,3',5'-tetramethylbenzidine concentration-dependent manner
additional information
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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 hide
LITERATURE
IMAGE
0.026
3,5,3',5'-tetramethylbenzidine
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pH and temperature not specified in the publication
0.11 - 0.24
cumene hydroperoxide
0.021 - 4.4
H2O2
0.026 - 0.058
myristic acid
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
117900
calculated from amino acid sequence
118000
estimated from SDS-PAGE
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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 20C
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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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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Ni-NTA agarose column chromatography, gel filtration
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Ni-NTA column chromatography
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli
expressed in Escherichia coli BL21 cells
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expressed in Escherichia coli BL21(DE3) cells
expressed in Escherichia coli M15 (pREP4) cells
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expressed in Saccharomyces cerevisiae
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
F878A
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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
A246K
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the mutant shows a large decrease in activity and a roughly 19fold lower affinity for myristic acid than the wild type enzyme
A246S
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the mutation decreases the catalytic activity, but does not affect affinity for myristic acid
A246V
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the mutant shows slightly reduced activity and moderately reduced affinity for myristic acid
F250K
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the mutant shows decreased specific activity compared to the wild type enzyme
F79L
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the specific activity is reduced by half compared to the wild type enzyme
F79L/V170F
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the double mutant exhibits 10% of the activity of the wild type enzyme
I244K
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the mutant shows decreased specific activity compared to the wild type enzyme
I247K
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the mutant shows decreased specific activity compared to the wild type enzyme
L237K
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the mutants shows specific activity similar to the wild type enzyme
L241K
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the mutants shows specific activity similar to the wild type enzyme
L251K
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the mutant shows decreased specific activity compared to the wild type enzyme
P243A
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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
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inactive, the mutant gives an absorption spectrum characteristic of a nitrogenous ligand-bound form of a ferric P450
P243K
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inactive, the mutant gives an absorption spectrum characteristic of a nitrogenous ligand-bound form of a ferric P450
P243S
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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
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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
S248K
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the mutant shows decreased specific activity compared to the wild type enzyme
V245K
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the mutant shows decreased specific activity compared to the wild type enzyme
Y249K
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the mutant shows decreased specific activity compared to the wild type enzyme