KEGG   ENZYME: 1.11.1.10Help
Entry
EC 1.11.1.10                Enzyme                                 

Name
chloride peroxidase;
chloroperoxidase;
CPO;
vanadium haloperoxidase
Class
Oxidoreductases;
Acting on a peroxide as acceptor;
Peroxidases
BRITE hierarchy
Sysname
chloride:hydrogen-peroxide oxidoreductase
Reaction(IUBMB)
RH + chloride + H2O2 = RCl + 2 H2O [RN:R00052]
Reaction(KEGG)
Substrate
RH [CPD:C01371];
chloride [CPD:C00698];
H2O2 [CPD:C00027]
Product
RCl [CPD:C01334];
H2O [CPD:C00001]
Comment
Brings about the chlorination of a range of organic molecules, forming stable C-Cl bonds. Also oxidizes bromide and iodide. Enzymes of this type are either heme-thiolate proteins, or contain vanadate. A secreted enzyme produced by the ascomycetous fungus Caldariomyces fumago (Leptoxyphium fumago) is an example of the heme-thiolate type. It catalyses the production of hypochlorous acid by transferring one oxygen atom from H2O2 to chloride. At a separate site it catalyses the chlorination of activated aliphatic and aromatic substrates, via HClO and derived chlorine species. In the absence of halides, it shows peroxidase (e.g. phenol oxidation) and peroxygenase activities. The latter inserts oxygen from H2O2 into, for example, styrene (side chain epoxidation) and toluene (benzylic hydroxylation), however, these activities are less pronounced than its activity with halides. Has little activity with non-activated substrates such as aromatic rings, ethers or saturated alkanes. The chlorinating peroxidase produced by ascomycetous fungi (e.g. Curvularia inaequalis) is an example of a vanadium chloroperoxidase, and is related to bromide peroxidase (EC 1.11.1.18). It contains vanadate and oxidizes chloride, bromide and iodide into hypohalous acids. In the absence of halides, it peroxygenates organic sulfides and oxidizes ABTS [2,2'-azinobis(3-ethylbenzthiazoline-6-sulfonic acid)] but no phenols.
History
EC 1.11.1.10 created 1972, modified 2011
Orthology
K00433  non-heme chloroperoxidase
K17990  vanadium chloroperoxidase
Genes
MGR: MGG_02210
PNO: SNOG_09935
BZE: COCCADRAFT_95108
BSC: COCSADRAFT_212376
BOR: COCMIDRAFT_29537
ZTR: MYCGRDRAFT_86416
ENT: Ent638_1149
ENC: ECL_02122
ENO: ECENHK_07930 ECENHK_12485
EEC: EcWSU1_02540(cpo)
ECLX: LI66_10185
KPN: KPN_02451
KPU: KP1_3653
KPP: A79E_1656
KPT: VK055_5070(cpo)
KPE: KPK_1737
KPR: KPR_1654(cpo)
KPJ: N559_1810
KPX: PMK1_04893(cpo)
KPNU: LI86_08850
KVA: Kvar_1628
KOX: KOX_20890
KOE: A225_3037
EAE: EAE_13185
EAR: CCG31335
CKO: CKO_04375
CRO: ROD_06251
EBF: D782_2077
EBI: EbC_16970
XCC: XCC2172(cpo)
XCB: XC_1946
XCP: XCR_2441
XCV: XCV2196
XAX: XACM_2141
XAC: XAC2035(cpo)
XCI: XCAW_01789(mhpC)
SML: Smlt2516 Smlt2882(cpo)
SMZ: SMD_2189 SMD_2519(cpo)
PAE: PA2717(cpo)
PAEV: N297_2799
PAEI: N296_2799
PAU: PA14_29020(cpo)
PAP: PSPA7_3995(cpo)
PAG: PLES_23871(cpo)
PAF: PAM18_2255(cpo)
PNC: NCGM2_3745(cpo)
PAEB: NCGM1900_3778(cpo)
PAEM: U769_11570
PAEL: T223_12155
PAEU: BN889_07075(cpo)
PAEG: AI22_21900
PAEC: M802_2796
PAEO: M801_2665
PRE: PCA10_34310(est)
PPU: PP_4021(cpo)
PSB: Psyr_4478
PFL: PFL_3458(cpo)
PFC: PflA506_3576(cpo)
PEN: PSEEN2814(cpo) PSEEN5395
PSA: PST_0170
PSZ: PSTAB_0233(fold)
PSTT: CH92_10190
ACB: A1S_1833
ABY: ABAYE1730(dch)
ABN: AB57_2170
ABB: ABBFA_001620(cpo)
MAH: MEALZ_2527(cpo)
HCH: HCH_03053
CSA: Csal_0764
REH: H16_A2213(h16_A2213) H16_B1410(h16_B1410) H16_B1427(h16_B1427) H16_B1943(h16_B1943)
CNC: CNE_2c02760(thcF) CNE_2c19030(cpo)
RME: Rmet_5312(cpo)
BPS: BPSS0444(cpo)
BPM: BURPS1710b_A1992(cpo)
BPL: BURPS1106A_A0603(cpoF)
BPSE: BDL_3672(cpo)
BPSM: BBQ_5750(cpo)
BPSU: BBN_3846(cpo)
BPSD: BBX_5509(cpo)
BPZ: BP1026B_II0496(cpo)
BPK: BBK_5651(cpo)
BPSH: DR55_4907(cpo)
BPSA: BBU_5601(cpo)
BPSO: X996_4657(cpo)
BUT: X994_4175
BVE: AK36_5141(cpo)
BCEW: DM40_5024(cpo) DM40_5272(cpo)
BCEO: I35_7691
BMU: Bmul_1700
BMJ: BMULJ_01542(cpo)
BCED: DM42_7217(cpo) DM42_7232(cpo)
BDL: AK34_5281(cpo)
BCON: NL30_31150
BGO: BM43_1184(cpo)
BUK: MYA_5744
PPNO: DA70_12945
PPNM: LV28_17750
PPUL: RO07_11945
PSPU: NA29_07970
PAPI: SG18_12280
AXY: AXYL_00446(cpo)
PUT: PT7_0850
VPD: VAPA_1c21800(cpo)
JAG: GJA_5363(cpo)
AZO: azo0490
GUR: Gura_3450
DMA: DMR_10710
DBA: Dbac_1162
SMI: BN406_02327(cpo) BN406_04115(cpo1) BN406_04738(cpo3) BN406_06603(cpo3)
RHI: NGR_b15830(cpo1) NGR_b15880(cpo2) NGR_c25070
SFD: USDA257_c49370(cpo2)
EAD: OV14_3277
ATU: Atu3463(cpoF) Atu3493 Atu4778(cpo) Atu5065(prxC) Atu5389
ARA: Arad_8698
AVI: Avi_5112
RLE: RL2967(cpo1) pRL110136(cpo2) pRL120450(cpO)
RIR: BN877_II0479(cpoF)
BME: BMEI0733
BJA: blr1251
BRS: S23_65410
RPA: RPA2105
OCA: OCAR_6762
BTR: BT_1151
XAU: Xaut_1276
MEX: Mext_3628
MCH: Mchl_3920
MPO: Mpop_3910
MSL: Msil_3584
RVA: Rvan_2221
CAK: Caul_0299
PZU: PHZ_c2785
HNE: HNE_3365
SPHM: G432_05745
SJP: SJA_C1-25290(cpo)
SSY: SLG_10660
GDI: GDI0081(cpo)
AZL: AZL_b04970(cpo) AZL_c02950(cpo)
ALI: AZOLI_2360(cpo1)
ABS: AZOBR_p170033(cpo)
TMO: TMO_3352
BLD: BLi02236(yisY)
BAR: GBAA_5030
BAT: BAS4670
BAI: BAA_5042
BANT: A16_50250
BANR: A16R_50920
BANS: BAPAT_4825
BANV: DJ46_3688
BCE: BC4774
BCQ: BCQ_4591
BCX: BCA_4906
BNC: BCN_4690
BCF: bcf_23970
BCER: BCK_11265
BTL: BALH_4349
BTT: HD73_5087
BTHI: BTK_25095
BTG: BTB_c49340(yisY2)
BTI: BTG_24955
BTW: BF38_537
BWW: bwei_0114
LLM: llmg_1737(cpo)
SAG: SAG2132
SAN: gbs2091
SAK: SAK_2071
STC: str1257
STL: stu1257
STE: STER_1236
EFA: EF1028
CTC: CTC_01150
CBO: CBO0840
CBA: CLB_0880
CBH: CLC_0894
CBY: CLM_0988
CBL: CLK_0246
CBB: CLD_3723
CBF: CLI_0921
CBM: CBF_0892
CKL: CKL_0764
CKR: CKR_0686
CPAS: Clopa_1155
CSQ: CSCA_0728
AOE: Clos_1937
CCE: Ccel_2497
CPY: Cphy_1659
DAE: Dtox_1575
SGY: Sgly_3187
TOC: Toce_1661
MMC: Mmcs_1286
MKM: Mkms_1303
MJL: Mjls_1315
MVA: Mvan_1567
MGI: Mflv_3146
RER: RER_36450
ROP: ROP_11130
GOR: KTR9_4642
SCO: SCO0465(SCF76.05c)
SGR: SGR_1103
SCB: SCAB_4601(cpo)
SFA: Sfla_0959
SDV: BN159_0372(cpo1)
SALB: XNR_4009
STRP: F750_5890
MTS: MTES_1614
XCE: Xcel_2040
CFI: Celf_2625
TFU: Tfu_1653
NDA: Ndas_2407
TCU: Tcur_0159
SRO: Sros_5197
FAL: FRAAL2804(cpo)
NML: Namu_1046
MMAR: MODMU_3277(cpo)
KRA: Krad_0455
SEN: SACE_3365(cpo)
SESP: BN6_55950(cpo)
SAQ: Sare_4822
AFS: AFR_11670
CAI: Caci_2084
SYZ: MYO_2810
RBA: RB3694
PSL: Psta_0376
SUS: Acid_3478
GAU: GAU_3315
SLI: Slin_3914
FAE: FAES_3445
FJO: Fjoh_4179
CCH: Cag_1627
MAC: MA_0993
 » show all
Taxonomy
Reference
1  [PMID:5949836]
  Authors
Morris DR, Hager LP.
  Title
Chloroperoxidase. I. Isolation and properties of the crystalline glycoprotein.
  Journal
J. Biol. Chem. 241 (1966) 1763-8.
Reference
2  [PMID:1056179]
  Authors
Hager LP, Hollenberg PF, Rand-Meir T, Chiang R, Doubek D.
  Title
Chemistry of peroxidase intermediates.
  Journal
Ann. N. Y. Acad. Sci. 244 (1975) 80-93.
Reference
3  [PMID:17777960]
  Authors
Theiler R, Cook JC, Hager LP, Siuda JF
  Title
Halohydrocarbon synthesis by bromoperoxidase.
  Journal
Science. 202 (1978) 1094-6.
Reference
4  [PMID:8747463]
  Authors
Sundaramoorthy M, Terner J, Poulos TL
  Title
The crystal structure of chloroperoxidase: a heme peroxidase--cytochrome P450 functional hybrid.
  Journal
Structure. 3 (1995) 1367-77.
Reference
5  [PMID:11670813]
  Authors
ten Brink HB, Tuynman A, Dekker HL, Hemrika W, Izumi Y, Oshiro T, Schoemaker HE, Wever R
  Title
Enantioselective Sulfoxidation Catalyzed by Vanadium Haloperoxidases.
  Journal
Inorg. Chem. 37 (1998) 6780-6784.
Reference
6  [PMID:10885468]
  Authors
ten Brink HB, Dekker HL, Schoemaker HE, Wever R
  Title
Oxidation reactions catalyzed by vanadium chloroperoxidase from Curvularia inaequalis.
  Journal
J. Inorg. Biochem. 80 (2000) 91-8.
  Sequence
Reference
7  [PMID:16870515]
  Authors
Murali Manoj K
  Title
Chlorinations catalyzed by chloroperoxidase occur via diffusible intermediate(s)  and the reaction components play multiple roles in the overall process.
  Journal
Biochim. Biophys. Acta. 1764 (2006) 1325-39.
Reference
8  [PMID:16790441]
  Authors
Kuhnel K, Blankenfeldt W, Terner J, Schlichting I
  Title
Crystal structures of chloroperoxidase with its bound substrates and complexed with formate, acetate, and nitrate.
  Journal
J. Biol. Chem. 281 (2006) 23990-8.
Reference
9  [PMID:18220360]
  Authors
Manoj KM, Hager LP
  Title
Chloroperoxidase, a janus enzyme.
  Journal
Biochemistry. 47 (2008) 2997-3003.
Other DBs
ExplorEnz - The Enzyme Database: 1.11.1.10
IUBMB Enzyme Nomenclature: 1.11.1.10
ExPASy - ENZYME nomenclature database: 1.11.1.10
BRENDA, the Enzyme Database: 1.11.1.10
CAS: 9055-20-3

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