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
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1.11.2.4
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peroxygenases
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oletje
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alkene
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self-sufficient
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cumene
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phanerochaete
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chrysosporium
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monooxygenation
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paucimobilis
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peroxygenation
- 1.11.2.4
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peroxygenases
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oletje
- alkene
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self-sufficient
- cumene
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phanerochaete
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chrysosporium
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monooxygenation
- paucimobilis
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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
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1.11.2.4 fatty-acid peroxygenaseAdvanced search results
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Natural Substrates Products on EC 1.11.2.4 - fatty-acid peroxygenase
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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
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?
myristic acid + H2O2
?
CYP152A1 attacks the beta-carbon as well as the alpha-carbon of myristic acid
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?
additional information
?
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a reductase and NAD(P)H are not required for activity
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-
?
additional information
?
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P450BSbeta produces alpha- and beta-hydroxylated products at 33 and 67%, respectively
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-
?
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
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-
?
additional information
?
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P450SPalpha produces the alpha-hydroxylated products at 100%
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?
additional information
?
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the enzyme never requires a supply of electrons or protons
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?
additional information
?
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CYP152A2 has a clear preference for hydroxylation at alpha-position
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?
additional information
?
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CYP152A2 has a clear preference for hydroxylation at alpha-position
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?
additional information
?
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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
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-
?
additional information
?
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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
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-
?
additional information
?
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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
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-
?
additional information
?
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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
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?
additional information
?
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P450BSbeta produces alpha- and beta-hydroxylated products at 33 and 67%, respectively
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-
?
additional information
?
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P450SPalpha produces the alpha-hydroxylated products at 100%
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-
?
additional information
?
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the enzyme never requires a supply of electrons or protons
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-
?
