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:C05102];
H2O [CPD:C00001]
Comment
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.
History
EC 1.11.2.4 created 2011
Orthology
K15629  fatty-acid peroxygenase
Genes
XCC: XCC1993(cypC)
XCB: XC_2191
XCA: xcc-b100_2293(cypC)
XCP: XCR_2273
PSA: PST_3282
PSZ: PSTAB_3329
PSR: PSTAA_3445
PSTU: UIB01_16925 UIB01_17410
PSTT: CH92_16810
PPSL: BJP27_00755
AMAD: I636_15975
AMAI: I635_16630
CGD: CR3_3130
RTA: Rta_37620
RGE: RGE_22720(cypC)
MFA: Mfla_1442
MES: Meso_4213
RHT: NT26_p10171(cypC)
MPO: Mpop_1292
MET: M446_4307
MMED: Mame_04450(cypC)
RSP: RSP_2378(cypC)
CID: P73_4344
MALG: MALG_04698
SAL: Sala_2556
ABS: AZOBR_p440090(cypC)
TMO: TMO_b0157
BSU: BSU02100(cypC)
BSR: I33_0247
BSL: A7A1_3272
BSH: BSU6051_02100(cypC)
BSUT: BSUB_00258(cypC)
BSUL: BSUA_00258(cypC)
BSUS: Q433_01315
BSS: BSUW23_01075(cypC)
BST: GYO_0400
BSO: BSNT_06509(cypC)
BSQ: B657_02100(cypC)
BSX: C663_0198(cypC)
BAY: RBAM_011070(cypC)
BYA: BANAU_1013(cypC)
BAMP: B938_05360
BAML: BAM5036_1007(cypC)
BAMA: RBAU_1067(cypC)
BAMN: BASU_1046(cypC)
BAMB: BAPNAU_2689(cypC)
BAMT: AJ82_06225
BAMY: V529_10520(cypC)
BMP: NG74_01117(cypC)
BAO: BAMF_1180(cypC)
BAZ: BAMTA208_05145(cypC)
BQL: LL3_01185(cypC)
BXH: BAXH7_01079(cypC)
BQY: MUS_1146(cypC)
BAMC: U471_11010
BHA: BH1757
BCL: ABC3040(cypC)
BPF: BpOF4_07440(faaH)
BMEG: BG04_5610
BAG: Bcoa_2050
BCOA: BF29_1516(cypC)
BJS: MY9_0209
BMET: BMMGA3_06595(cypC) BMMGA3_16880(cypC2)
BACB: OY17_08235
BACO: OXB_3532
BACY: QF06_00005
BACL: BS34A_02650(cypC)
BALM: BsLM_0214
BEO: BEH_25845
OIH: OB3101
HHD: HBHAL_1734(cypC)
SDT: SPSE_1582
SAGQ: EP23_02095
MCL: MCCL_0804
MCAK: MCCS_10350(cypC)
SIV: SSIL_0949(cypC)
JEO: JMA_11630
EFU: HMPREF0351_12437(cypX)
EFM: M7W_2456
EHR: EHR_06745
EMU: EMQU_2599
THL: TEH_14060
CARC: NY10_1909
JDA: BW727_101921(cypC)
CAC: CA_C3330
CAE: SMB_G3367(cypC)
CAY: CEA_G3333
CBO: CBO1038(cypC)
CBA: CLB_1078
CBH: CLC_1090
CBY: CLM_1194
CBL: CLK_0485
CBB: CLD_3520
CBI: CLJ_B1087
CBF: CLI_1129
CBM: CBF_1100
CPAS: Clopa_0939
CPAT: CLPA_c32420(cypC)
CPAE: CPAST_c32420(cypC)
CLT: CM240_0328(cypC)
CLD: CLSPO_c10440(cypC)
CPY: Cphy_2911
HSD: SD1D_1756(cypC)
CEF: CE2459
SCB: SCAB_80661(cypC)
STRM: M444_05205
SPRI: SPRI_6884
STRD: NI25_35225
SLX: SLAV_38290(cypC)
MTS: MTES_1735
KRH: KRH_21570
ACIJ: JS278_00530(cypC)
GOB: Gobs_3819
MMAR: MODMU_4242(cypC)
SESP: BN6_53090
MIL: ML5_3421
ASE: ACPL_3968(cypC)
ACTN: L083_1361(cypC)
AFS: AFR_28365
ACTS: ACWT_3839
SNA: Snas_5322
ZPR: ZPR_3345
 » 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 386:252-4 (1996)
DOI:10.1016/0014-5793(96)00451-6
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 124:105-10 (1998)
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 34:841-6 (1999)
DOI:10.1007/s11745-999-0431-3
  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 128:189-94 (2000)
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 41:1886-92 (2002)
DOI:10.1021/bi011883p
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 278:9761-7 (2003)
DOI:10.1074/jbc.M211575200
  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 8:127-32 (2004)
DOI:10.1016/j.cbpa.2004.01.001
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 15:1109-15 (2010)
DOI:10.1007/s00775-010-0671-9
Other DBs
ExplorEnz - The Enzyme Database: 1.11.2.4
IUBMB Enzyme Nomenclature: 1.11.2.4
ExPASy - ENZYME nomenclature database: 1.11.2.4
BRENDA, the Enzyme Database: 1.11.2.4

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