KEGG   ENZYME: 1.11.2.2Help
Entry
EC 1.11.2.2                 Enzyme                                 

Name
myeloperoxidase;
MPO;
verdoperoxidase
Class
Oxidoreductases;
Acting on a peroxide as acceptor;
Peroxygenases
BRITE hierarchy
Sysname
chloride:hydrogen-peroxide oxidoreductase (hypochlorite-forming)
Reaction(IUBMB)
Cl- + H2O2 + H+ = HClO + H2O [RN:R09564]
Reaction(KEGG)
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
Orthology
K10789  
myeloperoxidase
Genes
HSA: 
4353(MPO)
PTR: 
748680(MPO)
PPS: 
GGO: 
PON: 
NLE: 
MCC: 
714246(MPO)
MCF: 
CJC: 
MMU: 
17523(Mpo)
RNO: 
303413(Mpo)
CGE: 
NGI: 
HGL: 
OCU: 
TUP: 
CFA: 
609986(MPO)
AML: 
UMR: 
FCA: 
PTG: 
BTA: 
511206(MPO)
BOM: 
PHD: 
CHX: 
OAS: 
SSC: 
CFR: 
BACU: 
LVE: 
ECB: 
MYB: 
MYD: 
PALE: 
MDO: 
SHR: 
GGA: 
417466(LPO) 417467(MPO)
MGP: 
APLA: 
TGU: 
FAB: 
FPG: 
FCH: 
CLV: 
ASN: 
AMJ: 
PSS: 
CMY: 
ACS: 
PBI: 
XLA: 
394386(mpo) 398084(epx)
XTR: 
OLA: 
XMA: 
LCM: 
NGR: 
 » show all
Taxonomy
Reference
1
  Authors
Agner, K.
  Title
Myeloperoxidase.
  Journal
Adv. Enzymol. 3 (1943) 137-148.
Reference
2  [PMID:176150]
  Authors
Harrison JE, Schultz J
  Title
Studies on the chlorinating activity of myeloperoxidase.
  Journal
J. Biol. Chem. 251 (1976) 1371-4.
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 (1998) 17923-30.
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 (2000) 3025-30.
Reference
5  [PMID:15689384]
  Authors
Klebanoff SJ
  Title
Myeloperoxidase: friend and foe.
  Journal
J. Leukoc. Biol. 77 (2005) 598-625.
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 (2000) 11964-71.
  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 (2001) 11961-6.
Other DBs
ExplorEnz - The Enzyme Database: 
IUBMB Enzyme Nomenclature: 
ExPASy - ENZYME nomenclature database: 
BRENDA, the Enzyme Database: 

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