CATH Classification
Level | CATH Code | Description |
---|---|---|
1 | Mainly Alpha | |
1.10 | Orthogonal Bundle | |
1.10.630 | Cytochrome p450 | |
1.10.630.10 | Cytochrome P450 |
Domain Context
CATH Clusters
Superfamily | Cytochrome P450 |
Functional Family | Fatty-acid peroxygenase |
Enzyme Information
1.11.2.4 |
Fatty-acid peroxygenase.
based on mapping to UniProt O31440
Fatty acid + H(2)O(2) = 3- or 2-hydroxy fatty acid + H(2)O.
-!- 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.
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UniProtKB Entries (1)
O31440 |
CYPC_BACSU
Bacillus subtilis subsp. subtilis str. 168
Fatty-acid peroxygenase
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PDB Structure
PDB | 1IZO |
External Links | |
Method | X-RAY DIFFRACTION |
Organism | Escherichia |
Primary Citation |
Substrate Recognition and Molecular Mechanism of Fatty Acid Hydroxylation by Cytochrome P450 from Bacillus subtilis. CRYSTALLOGRAPHIC, SPECTROSCOPIC, AND MUTATIONAL STUDIES.
J.Biol.Chem.
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