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Information on EC 1.11.2.4 - fatty-acid peroxygenase and Organism(s) Fusarium oxysporum and UniProt Accession Q9Y8G7

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EC Tree
     1 Oxidoreductases
         1.11 Acting on a peroxide as acceptor
             1.11.2 Peroxygenases
                1.11.2.4 fatty-acid peroxygenase
IUBMB 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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Fusarium oxysporum
UNIPROT: Q9Y8G7
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Word Map
The taxonomic range for the selected organisms is: Fusarium oxysporum
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
Synonyms
p450foxy, cyp152a2, cyp152a1, cyp505, p450 peroxygenase, fatty-acid hydroxylase, p450bsbeta, peroxygenase p450, p450cla, cyp152b1, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
CYP505
bifunctional fusion enzyme, the primary structure of P450foxy can be divided into P450, P450 reductase and their linker domains
fatty-acid subterminal hydroxylase
-
P450foxy
bifunctional fusion enzyme, the primary structure of P450foxy can be divided into P450, P450 reductase and their linker domains
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.
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
myristic acid + H2O2
?
show the reaction diagram
-
-
-
?
additional information
?
-
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
myristic acid + H2O2
?
show the reaction diagram
-
-
-
?
additional information
?
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
UniProt
Manually annotated by BRENDA team
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
C505_FUSOX
1066
0
117926
Swiss-Prot
-
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
117900
calculated from amino acid sequence
118000
estimated from SDS-PAGE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Saccharomyces cerevisiae
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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)
Manually annotated by BRENDA team