KEGG   ENZYME: 1.11.2.2
Entry
EC 1.11.2.2                 Enzyme                                 

Name
myeloperoxidase;
MPO;
verdoperoxidase
Class
Oxidoreductases;
Acting on a peroxide as acceptor;
Peroxygenases
Sysname
chloride:hydrogen-peroxide oxidoreductase (hypochlorite-forming)
Reaction(IUBMB)
Cl- + H2O2 + H+ = HClO + H2O [RN:R09564]
Reaction(KEGG)
R09564;
(other) R11906
Substrate
Cl- [CPD:C00698];
H2O2 [CPD:C00027];
H+ [CPD:C00080]
Product
HClO [CPD:C19697];
H2O [CPD:C00001]
Comment
Contains calcium and covalently bound heme (proximal ligand histidine). It is present in phagosomes of neutrophils and monocytes, where the hypochlorite produced is strongly bactericidal. It differs from EC 1.11.1.10 chloride peroxidase in its preference for formation of hypochlorite over the chlorination of organic substrates under physiological conditions (pH 5-8). Hypochlorite in turn forms a number of antimicrobial products (Cl2, chloramines, hydroxyl radical, singlet oxygen). MPO also oxidizes bromide, iodide and thiocyanate. In the absence of halides, it oxidizes phenols and has a moderate peroxygenase activity toward styrene.
History
EC 1.11.2.2 created 2011
Pathway
ec00983  Drug metabolism - other enzymes
Orthology
K10789  myeloperoxidase
Genes
HSA: 4353(MPO)
PTR: 748680(MPO)
PPS: 100992079(MPO)
GGO: 101135280(MPO)
PON: 100461693(MPO)
NLE: 100606582(MPO)
MCC: 714246(MPO)
MCF: 102130410(MPO)
CSAB: 103242854(MPO)
RRO: 104669826(MPO)
RBB: 108521655(MPO)
CJC: 100408045(MPO)
SBQ: 101046117(MPO)
MMU: 17523(Mpo)
MCAL: 110305648(Mpo)
MPAH: 110331385(Mpo)
RNO: 303413(Mpo)
MUN: 110566146(Mpo)
CGE: 100752227(Mpo) 100757792
NGI: 103741805(Mpo)
HGL: 101707361(Mpo)
OCU: 100340692(MPO)
TUP: 102501858(MPO)
CFA: 609986(MPO)
VVP: 112918144(MPO)
AML: 100472895(MPO)
UMR: 103667463(MPO)
UAH: 113268870(MPO)
ORO: 101380182(MPO)
ELK: 111151617
FCA: 100142673(MPO)
PTG: 102973033(MPO)
PPAD: 109247205(MPO)
AJU: 106989943(MPO)
BTA: 511206(MPO)
BOM: 102286491(MPO)
BIU: 109573426(MPO)
BBUB: 102404921(MPO)
CHX: 102185772(MPO)
OAS: 101123053(MPO)
SSC: 100517120(MPO)
CFR: 102510136(MPO)
CDK: 105097806(MPO)
BACU: 103004965(MPO)
LVE: 103083642(MPO)
OOR: 101290133(MPO)
DLE: 111163673(MPO)
PCAD: 102982078(MPO)
ECB: 100070920(MPO)
EPZ: 103546343(MPO)
EAI: 106822013(MPO)
MYB: 102240978(MPO)
MYD: 102756726(MPO)
MNA: 107535307(MPO)
HAI: 109379730(MPO)
DRO: 112316355(MPO)
PALE: 102883356(MPO)
RAY: 107499177(MPO)
MJV: 108397175(MPO)
LAV: 100662013(MPO)
TMU: 101340378
MDO: 100012330(MPO) 100022606
SHR: 100918289
PCW: 110212135
OAA: 100078069(MPO)
GGA: 417466(LPO) 417467(MPO)
MGP: 100547955(LPO)
NMEL: 110407540(EPX) 110407753
ACYG: 106041022 106041024(MPO)
TGU: 116809130
LSR: 110475906
GFR: 102037835(MPO)
FAB: 101820562(MPO)
CCW: 104695782
ETL: 114063781
FPG: 101914513(EPX) 101914689(MPO)
FCH: 102052208
EGZ: 104131757 104131758(MPO)
NNI: 104012465(LPO)
ACUN: 113487144 113487180(MPO)
AAM: 106496096 106496104(MPO)
AMJ: 102559230(LPO)
PBI: 103062626 103062866(LPO)
PMUR: 107288571(MPO)
TSR: 106549249(MPO) 106553876(LPO)
PMUA: 114585840
GJA: 107112485
XLA: 373710(mpo.S) 394386(mpo.L) 398084(epx.L)
XTR: 100490938(mpo) 100496213(epx)
SRX: 107713297
SANH: 107688477
SGH: 107569391
SASA: 100380666(perm)
OTW: 112231092
SALP: 111964113
LCM: 102347787 102348047(MPO)
 » show all
Reference
1
  Authors
Agner, K.
  Title
Myeloperoxidase.
  Journal
Adv Enzymol 3:137-148 (1943)
Reference
2  [PMID:176150]
  Authors
Harrison JE, Schultz J
  Title
Studies on the chlorinating activity of myeloperoxidase.
  Journal
J Biol Chem 251:1371-4 (1976)
Reference
3  [PMID:9922160]
  Authors
Furtmuller PG, Burner U, Obinger C
  Title
Reaction of myeloperoxidase compound I with chloride, bromide, iodide, and thiocyanate.
  Journal
Biochemistry 37:17923-30 (1998)
DOI:10.1021/bi9818772
Reference
4  [PMID:10652281]
  Authors
Tuynman A, Spelberg JL, Kooter IM, Schoemaker HE, Wever R
  Title
Enantioselective epoxidation and carbon-carbon bond cleavage catalyzed by Coprinus cinereus peroxidase and myeloperoxidase.
  Journal
J Biol Chem 275:3025-30 (2000)
DOI:10.1074/jbc.275.5.3025
Reference
5  [PMID:15689384]
  Authors
Klebanoff SJ
  Title
Myeloperoxidase: friend and foe.
  Journal
J Leukoc Biol 77:598-625 (2005)
DOI:10.1189/jlb.1204697
Reference
6  [PMID:10766826]
  Authors
Fiedler TJ, Davey CA, Fenna RE
  Title
X-ray crystal structure and characterization of halide-binding sites of human myeloperoxidase at 1.8 A resolution.
  Journal
J Biol Chem 275:11964-71 (2000)
DOI:10.1074/jbc.275.16.11964
  Sequence
[hsa:4353]
Reference
7  [PMID:11593004]
  Authors
Gaut JP, Yeh GC, Tran HD, Byun J, Henderson JP, Richter GM, Brennan ML, Lusis AJ, Belaaouaj A, Hotchkiss RS, Heinecke JW
  Title
Neutrophils employ the myeloperoxidase system to generate antimicrobial brominating and chlorinating oxidants during sepsis.
  Journal
Proc Natl Acad Sci U S A 98:11961-6 (2001)
DOI:10.1073/pnas.211190298
Other DBs
ExplorEnz - The Enzyme Database: 1.11.2.2
IUBMB Enzyme Nomenclature: 1.11.2.2
ExPASy - ENZYME nomenclature database: 1.11.2.2
BRENDA, the Enzyme Database: 1.11.2.2
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