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: 
PNO: 
ZTR: 
EBI: 
ENT: 
ENC: 
ENO: 
EEC: 
KPN: 
KPU: 
KPM: 
KPE: 
KVA: 
KOX: 
CKO: 
CRO: 
SMW: 
PAO: 
RAH: 
XCC: 
XCC2172(cpo)
XCB: 
XCA: 
XCP: 
XCV: 
XAC: 
XAC2035(cpo)
XCI: 
XAX: 
XAO: 
SML: 
SMT: 
BUJ: 
SMZ: 
PSU: 
FAU: 
PAE: 
PA2717(cpo)
PAU: 
PAP: 
PAG: 
PDK: 
PPU: 
PP_4021(est)
PPG: 
PPW: 
PPUU: 
PSB: 
PFL: 
PFO: 
PFE: 
PEN: 
PSA: 
PBA: 
PDR: 
AVN: 
AVL: 
AVD: 
ACD: 
ACB: 
ABY: 
ABC: 
ABN: 
ABB: 
MAH: 
HCH: 
CSA: 
REU: 
REH: 
CNC: 
RME: 
CTI: 
BPS: 
BPM: 
BPL: 
BPD: 
BPSE: 
BPZ: 
BPQ: 
BPK: 
BVI: 
BUR: 
BCN: 
BCH: 
BCM: 
BCJ: 
BAM: 
BAC: 
BMU: 
BMJ: 
BXE: 
BPH: 
BPY: 
BGL: 
BUG: 
BGE: 
BGF: 
BGD: 
BYI: 
BUK: 
BPX: 
BUO: 
PPK: 
PRB: 
AXY: 
PUT: 
VAP: 
VPE: 
VPD: 
AZO: 
GUR: 
DMA: 
DBA: 
AFW: 
SUR: 
MLO: 
MCI: 
MOP: 
MAM: 
PLA: 
SME: 
SMK: 
SMQ: 
SMX: 
SMI: 
SMEG: 
SMEL: 
SMD: 
RHI: 
ATU: 
ARA: 
AVI: 
AGR: 
RET: 
REC: 
RLE: 
RL2967(cpo) pRL110136(cpo) pRL120450(cpO)
RLT: 
RLG: 
RTR: 
RIR: 
BME: 
BJA: 
BJU: 
BRA: 
BBT: 
BRS: 
AOL: 
RPA: 
RPB: 
RPC: 
RPE: 
RPT: 
OCA: 
BTR: 
XAU: 
AZC: 
SNO: 
MEX: 
MEA: 
MDI: 
MCH: 
MRD: 
MPO: 
MSL: 
HNI: 
RVA: 
CAK: 
CSE: 
PZU: 
BSB: 
AEX: 
HNE: 
NPP: 
SPHM: 
SJP: 
SSY: 
GOX: 
GDI: 
AZL: 
ALI: 
ABS: 
TMO: 
BLD: 
BLi02236(yisY)
BAR: 
BAT: 
BAH: 
BAI: 
BCE: 
BCA: 
BCZ: 
BCR: 
BCB: 
BCU: 
BCG: 
BCQ: 
BCX: 
BTK: 
BTL: 
BTB: 
BWE: 
PJD: 
LLM: 
SAG: 
SAN: 
SAK: 
STC: 
STL: 
STE: 
EFA: 
CTC: 
CBO: 
CBA: 
CBH: 
CBY: 
CBL: 
CBB: 
CBI: 
CBF: 
CKL: 
CKR: 
CCE: 
CLJ: 
AOE: 
CPY: 
CDC: 
CDL: 
DAE: 
SGY: 
TOC: 
MVA: 
MGI: 
MMC: 
MKM: 
MJL: 
MCB: 
MNE: 
RHA: 
RER: 
ROP: 
GOR: 
SCO: 
SCO0465(SCF76.05c)
SMA: 
SGR: 
SCB: 
SSX: 
SFA: 
SHY: 
SHO: 
SDV: 
SALB: 
STRP: 
SFI: 
MTS: 
XCE: 
CFI: 
TFU: 
NDA: 
TCU: 
SRO: 
FRE: 
FAL: 
NML: 
MMAR: 
KRA: 
SEN: 
SVI: 
SESP: 
STP: 
SAQ: 
MAU: 
AMS: 
ACTN: 
AFS: 
CAI: 
ABA: 
GMA: 
TSA: 
TRS: 
SUS: 
GAU: 
RBA: 
PSL: 
SYN: 
SYZ: 
SYNE: 
NOS: 
AVA: 
ACY: 
NKO: 
SHG: 
SLI: 
FAE: 
FJO: 
CCH: 
MAC: 
 » 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.
  Organism
Caldariomyces fumago
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.
  Organism
Caldariomyces fumago
  Sequence
[up:P04963]
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.
  Organism
Ascophyllum nodosum
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.
  Organism
Curvularia inaequalis
  Sequence
[up:P49053]
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: 
IUBMB Enzyme Nomenclature: 
ExPASy - ENZYME nomenclature database: 
BRENDA, the Enzyme Database: 
CAS: 
9055-20-3

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