KEGG   ENZYME: 1.11.2.4Help
Entry
EC 1.11.2.4                 Enzyme                                 

Name
fatty-acid peroxygenase;
fatty acid hydroxylase (ambiguous);
P450 peroxygenase;
CYP152A1;
P450BS;
P450SPalpha
Class
Oxidoreductases;
Acting on a peroxide as acceptor;
Peroxygenases
BRITE hierarchy
Sysname
fatty acid:hydroperoxide oxidoreductase (RH-hydroxylating)
Reaction(IUBMB)
fatty acid + H2O2 = 3- or 2-hydroxy fatty acid + H2O [RN:R09740 R09741]
Reaction(KEGG)
Substrate
fatty acid [CPD:C00162];
H2O2 [CPD:C00027]
Product
3-hydroxy fatty acid [CPD:C19861];
2-hydroxy fatty acid [CPD:C19860];
H2O [CPD:C00001]
Comment
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 catalysed 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.
History
EC 1.11.2.4 created 2011
Orthology
K15629  
fatty-acid peroxygenase
Genes
XCC: 
XCC1993(cypC)
XCB: 
XCA: 
XCP: 
PSA: 
PSZ: 
PSR: 
PSTU: 
PSTT: 
AMAA: 
AMAD: 
AMAI: 
MEJ: 
RTA: 
RGE: 
RGE_22720(cypC)
MFA: 
DAF: 
MES: 
MET: 
MPO: 
HNI: 
RSP: 
RSP_2378(cypC)
RSH: 
RSQ: 
RSK: 
SAL: 
ABS: 
TMO: 
BSU: 
BSU02100(cypC)
BSR: 
BSL: 
BSH: 
BSY: 
BSUT: 
BSUL: 
BSS: 
BST: 
BSO: 
BSN: 
BSQ: 
BSX: 
C663_0198(cypC)
BSP: 
BAO: 
BAMF_1180(cypC)
BAY: 
BYA: 
BAMP: 
BAML: 
BAMA: 
RBAU_1067(cypC)
BAMN: 
BASU_1046(cypC)
BAMB: 
BAMT: 
BAZ: 
BQL: 
LL3_01185(cypC)
BXH: 
BQY: 
MUS_1146(cypC)
BAMC: 
BAMY: 
BAE: 
BHA: 
BCL: 
ABC3040(cypC)
BPF: 
BAG: 
BJS: 
BIF: 
BMET: 
BMP: 
OIH: 
HHD: 
TAP: 
VIR: 
SSD: 
SDT: 
MCL: 
EAT: 
SIV: 
SSIL_0949(cypC)
EFC: 
EFAU: 
EFU: 
EFM: 
EFT: 
EHR: 
EMU: 
THL: 
CAC: 
CAE: 
SMB_G3367(cypC)
CAY: 
CBO: 
CBO1038(cypC)
CBA: 
CBH: 
CBY: 
CBL: 
CBB: 
CBI: 
CBF: 
CBM: 
CBJ: 
CPAS: 
CLT: 
CLE: 
CPY: 
CSH: 
CEF: 
CHN: 
CMD: 
CDO: 
SCB: 
SSX: 
SGU: 
MTS: 
ART: 
KRH: 
KSE: 
DNI: 
PBO: 
PRA: 
GOB: 
BSD: 
MMAR: 
SESP: 
MAU: 
MIL: 
VMA: 
AMS: 
ASE: 
ACPL_3968(cypC)
ACTN: 
L083_1361(cypC)
AFS: 
SNA: 
RRD: 
SCS: 
ZPR: 
DMR: 
 » show all
Taxonomy
Reference
1  [PMID:8647293]
  Authors
Matsunaga I, Yamada M, Kusunose E, Nishiuchi Y, Yano I, Ichihara K
  Title
Direct involvement of hydrogen peroxide in bacterial alpha-hydroxylation of fatty acid.
  Journal
FEBS. Lett. 386 (1996) 252-4.
Reference
2  [PMID:9644252]
  Authors
Matsunaga I, Yamada M, Kusunose E, Miki T, Ichihara K
  Title
Further characterization of hydrogen peroxide-dependent fatty acid alpha-hydroxylase from Sphingomonas paucimobilis.
  Journal
J. Biochem. 124 (1998) 105-10.
Reference
3  [PMID:10529095]
  Authors
Matsunaga I, Ueda A, Fujiwara N, Sumimoto T, Ichihara K
  Title
Characterization of the ybdT gene product of Bacillus subtilis: novel fatty acid  beta-hydroxylating cytochrome P450.
  Journal
Lipids. 34 (1999) 841-6.
  Sequence
[bsu:BSU02100]
Reference
4  [PMID:10920253]
  Authors
Imai Y, Matsunaga I, Kusunose E, Ichihara K
  Title
Unique heme environment at the putative distal region of hydrogen peroxide-dependent fatty acid alpha-hydroxylase from Sphingomonas paucimobilis (peroxygenase P450(SPalpha).
  Journal
J. Biochem. 128 (2000) 189-94.
Reference
5  [PMID:11827534]
  Authors
Matsunaga I, Yamada A, Lee DS, Obayashi E, Fujiwara N, Kobayashi K, Ogura H, Shiro Y
  Title
Enzymatic reaction of hydrogen peroxide-dependent peroxygenase cytochrome P450s:  kinetic deuterium isotope effects and analyses by resonance Raman spectroscopy.
  Journal
Biochemistry. 41 (2002) 1886-92.
Reference
6  [PMID:12519760]
  Authors
Lee DS, Yamada A, Sugimoto H, Matsunaga I, Ogura H, Ichihara K, Adachi S, Park SY, Shiro Y
  Title
Substrate recognition and molecular mechanism of fatty acid hydroxylation by cytochrome P450 from Bacillus subtilis. Crystallographic, spectroscopic, and mutational studies.
  Journal
J. Biol. Chem. 278 (2003) 9761-7.
  Sequence
[bsu:BSU02100]
Reference
7  [PMID:15062772]
  Authors
Matsunaga I, Shiro Y
  Title
Peroxide-utilizing biocatalysts: structural and functional diversity of heme-containing enzymes.
  Journal
Curr. Opin. Chem. Biol. 8 (2004) 127-32.
Reference
8  [PMID:20490877]
  Authors
Shoji O, Wiese C, Fujishiro T, Shirataki C, Wunsch B, Watanabe Y
  Title
Aromatic C-H bond hydroxylation by P450 peroxygenases: a facile colorimetric assay for monooxygenation activities of enzymes based on Russig's blue formation.
  Journal
J. Biol. Inorg. Chem. 15 (2010) 1109-15.
Other DBs
ExplorEnz - The Enzyme Database: 
IUBMB Enzyme Nomenclature: 
ExPASy - ENZYME nomenclature database: 
BRENDA, the Enzyme Database: 

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