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ENZYME entry: EC 1.11.2.4

Accepted Name
Fatty-acid peroxygenase.
Alternative Name(s)
CYP152A1.
Fatty acid hydroxylase.
P450 peroxygenase.
P450SP-alpha.
Reaction catalysed
Fatty acid + H(2)O(2) <=> 3- or 2-hydroxy fatty acid + H(2)O
Cofactor(s)
Heme-thiolate.
Comment(s)
  • A cytosolic heme-thiolate protein with sequence homology to P450 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 catalyzed by the common P450s.
  • 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.
Cross-references
PROSITEPDOC00081
BRENDA1.11.2.4
EC2PDB1.11.2.4
ExplorEnz1.11.2.4
PRIAM enzyme-specific profiles1.11.2.4
KEGG Ligand Database for Enzyme Nomenclature1.11.2.4
IUBMB Enzyme Nomenclature1.11.2.4
IntEnz1.11.2.4
MEDLINEFind literature relating to 1.11.2.4
MetaCyc1.11.2.4
UniProtKB/Swiss-Prot
O31440, CYPC_BACSU

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All ENZYME / UniProtKB/Swiss-Prot entries corresponding to 1.11.2.-
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