EzCatDB: D00483
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DB codeD00483
CATH domainDomain 11.-.-.-Catalytic domain
Domain 21.10.640.10 : Myeloperoxidase, subunit CCatalytic domain
E.C.1.11.1.7
CSA1mhl


Enzyme Name
UniProtKBKEGG

P05164
Protein nameMyeloperoxidaseperoxidase
myeloperoxidase
lactoperoxidase
verdoperoxidase
guaiacol peroxidase
thiocyanate peroxidase
eosinophil peroxidase
Japanese radish peroxidase
horseradish peroxidase (HRP)
extensin peroxidase
heme peroxidase
MPO
oxyperoxidase
protoheme peroxidase
pyrocatechol peroxidase
scopoletin peroxidase
SynonymsMPO
EC 1.11.1.7
Contains89 kDa myeloperoxidase
84 kDa myeloperoxidase
Myeloperoxidase light chain
Myeloperoxidase heavy chain
RefSeqNP_000241.1 (Protein)
NM_000250.1 (DNA/RNA sequence)
PfamPF03098 (An_peroxidase)
[Graphical view]

KEGG pathways
MAP codePathways
MAP00360Phenylalanine metabolism
MAP00680Methane metabolism
MAP00940Phenylpropanoid biosynthesis

UniProtKB:Accession NumberP05164
Entry namePERM_HUMAN
ActivityDonor + H(2)O(2) = oxidized donor + 2 H(2)O.,Cl(-) + H(2)O(2) = HOCl + 2 H(2)O.
SubunitTetramer of two light chains and two heavy chains.
Subcellular locationLysosome.
CofactorBinds 1 calcium ion per heterodimer.,Binds 1 heme B (iron-protoporphyrin IX) group covalently per heterodimer.

Compound table: links to PDB-related databases & PoSSuM

CofactorsSubstratesProducts
KEGG-idC00032C00076C01351C00027C00115C02177C00001C99999
CompoundHemeCalciumDonorH2O2ChlorideOxidized donorH2OHypochlorite
Typearomatic ring (with nitrogen atoms),carboxyl group,heavy metaldivalent metal (Ca2+, Mg2+)othersothershalideothersH2Ohalide
ChEBI17627
26355
29108

16240


15377

PubChem
271

784
22326046


962
22247451

                
1cxpAUnboundUnboundUnboundUnboundUnboundUnbound Unbound
1cxpBUnboundUnboundUnboundUnboundUnboundUnbound Unbound
1d2vAUnboundUnboundUnboundUnboundAnalogue:_BR 843Unbound Unbound
1d2vBUnboundUnboundUnboundUnboundAnalogue:_BR 843Unbound Unbound
1d5lAUnboundUnboundAnalogue:CYN 1844UnboundUnboundUnbound Unbound
1d5lBUnboundUnboundAnalogue:CYN 1844UnboundUnboundUnbound Unbound
1d7wAUnboundUnboundAnalogue:CYNUnboundAnalogue:_BR 957Unbound Unbound
1d7wBUnboundUnboundAnalogue:CYNUnboundAnalogue:_BR 957Unbound Unbound
1dnuAUnboundUnboundAnalogue:SCN 5UnboundUnboundUnbound Unbound
1dnuBUnboundUnboundAnalogue:SCN 4UnboundUnboundUnbound Unbound
1dnwAUnboundUnboundAnalogue:CYN 3UnboundUnboundUnbound Unbound
1dnwBUnboundUnboundAnalogue:CYN 4UnboundUnboundUnbound Unbound
1mhlAUnboundUnboundUnboundUnboundUnboundUnbound Unbound
1mhlBUnboundUnboundUnboundUnboundUnboundUnbound Unbound
1mypAUnboundUnboundUnboundUnboundUnboundUnbound Unbound
1mypBUnboundUnboundUnboundUnboundUnboundUnbound Unbound
1cxpCBound:HEMBound:_CAUnboundUnboundUnboundUnbound Unbound
1cxpDBound:HEMBound:_CAUnboundUnboundUnboundUnbound Unbound
1d2vCBound:HEMBound:_CAUnboundUnboundUnboundUnbound Unbound
1d2vDBound:HEMBound:_CAUnboundUnboundUnboundUnbound Unbound
1d5lCBound:HEMBound:_CAUnboundUnboundUnboundUnbound Unbound
1d5lDBound:HEMBound:_CAUnboundUnboundUnboundUnbound Unbound
1d7wCBound:HEMBound:_CAUnboundUnboundUnboundUnbound Unbound
1d7wDBound:HEMBound:_CAUnboundUnboundUnboundUnbound Unbound
1dnuCBound:HEMBound:_CAUnboundUnboundUnboundUnbound Unbound
1dnuDBound:HEMBound:_CAUnboundUnboundUnboundUnbound Unbound
1dnwCBound:HEMBound:_CAUnboundUnboundUnboundUnbound Unbound
1dnwDBound:HEMBound:_CAUnboundUnboundUnboundUnbound Unbound
1mhlCBound:HEMBound:_CAUnboundUnboundUnboundUnbound Unbound
1mhlDBound:HEMBound:_CAUnboundUnboundUnboundUnbound Unbound
1mypCBound:HEMBound:_CAUnboundUnboundUnboundUnbound Unbound
1mypDBound:HEMBound:_CAUnboundUnboundUnboundUnbound Unbound

Active-site residues
resource
Swiss-prot;P05164 & literature [5], [10], [11]
pdbCatalytic residuesCofactor-binding residuesModified residues
           
1cxpAGLN 91;HIS 95
ASP 94(Heme);ASP 96(Calcium)
 
1cxpBGLN 91;HIS 95
ASP 94(Heme);ASP 96(Calcium)
 
1d2vAGLN 91;HIS 95
ASP 94(Heme);ASP 96(Calcium)
 
1d2vBGLN 91;HIS 95
ASP 94(Heme);ASP 96(Calcium)
 
1d5lAGLN 91;HIS 95
ASP 94(Heme);ASP 96(Calcium)
 
1d5lBGLN 91;HIS 95
ASP 94(Heme);ASP 96(Calcium)
 
1d7wAGLN 91;HIS 95
ASP 94(Heme);ASP 96(Calcium)
 
1d7wBGLN 91;HIS 95
ASP 94(Heme);ASP 96(Calcium)
 
1dnuAGLN 91;HIS 95
ASP 94(Heme);ASP 96(Calcium)
 
1dnuBGLN 91;HIS 95
ASP 94(Heme);ASP 96(Calcium)
 
1dnwAGLN 91;HIS 95
ASP 94(Heme);ASP 96(Calcium)
 
1dnwBGLN 91;HIS 95
ASP 94(Heme);ASP 96(Calcium)
 
1mhlAGLN 91;HIS 95
ASP 94(Heme);ASP 96(Calcium)
 
1mhlBGLN 91;HIS 95
ASP 94(Heme);ASP 96(Calcium)
 
1mypAGLN 91;HIS 95
ASP 94(Heme);ASP 96(Calcium)
 
1mypBGLN 91;HIS 95
ASP 94(Heme);ASP 96(Calcium)
 
1cxpCARG 239
GLU 242;MET 243(Heme);HIS 336(Heme iron);THR 168;PHE 170;ASP 172;SER 174(Calcium)
CSO 150(Cysteine sulfenic acid)
1cxpDARG 239
GLU 242;MET 243(Heme);HIS 336(Heme iron);THR 168;PHE 170;ASP 172;SER 174(Calcium)
CSO 150(Cysteine sulfenic acid)
1d2vCARG 239
GLU 242;MET 243(Heme);HIS 336(Heme iron);THR 168;PHE 170;ASP 172;SER 174(Calcium)
CSO 150(Cysteine sulfenic acid)
1d2vDARG 239
GLU 242;MET 243(Heme);HIS 336(Heme iron);THR 168;PHE 170;ASP 172;SER 174(Calcium)
CSO 150(Cysteine sulfenic acid)
1d5lCARG 239
GLU 242;MET 243(Heme);HIS 336(Heme iron);THR 168;PHE 170;ASP 172;SER 174(Calcium)
CSO 150(Cysteine sulfenic acid)
1d5lDARG 239
GLU 242;MET 243(Heme);HIS 336(Heme iron);THR 168;PHE 170;ASP 172;SER 174(Calcium)
CSO 150(Cysteine sulfenic acid)
1d7wCARG 239
GLU 242;MET 243(Heme);HIS 336(Heme iron);THR 168;PHE 170;ASP 172;SER 174(Calcium)
CSO 150(Cysteine sulfenic acid)
1d7wDARG 239
GLU 242;MET 243(Heme);HIS 336(Heme iron);THR 168;PHE 170;ASP 172;SER 174(Calcium)
CSO 150(Cysteine sulfenic acid)
1dnuCARG 239
GLU 242;MET 243(Heme);HIS 336(Heme iron);THR 168;PHE 170;ASP 172;SER 174(Calcium)
CSO 150(Cysteine sulfenic acid)
1dnuDARG 239
GLU 242;MET 243(Heme);HIS 336(Heme iron);THR 168;PHE 170;ASP 172;SER 174(Calcium)
CSO 150(Cysteine sulfenic acid)
1dnwCARG 239
GLU 242;MET 243(Heme);HIS 336(Heme iron);THR 168;PHE 170;ASP 172;SER 174(Calcium)
CSO 150(Cysteine sulfenic acid)
1dnwDARG 239
GLU 242;MET 243(Heme);HIS 336(Heme iron);THR 168;PHE 170;ASP 172;SER 174(Calcium)
CSO 150(Cysteine sulfenic acid)
1mhlCARG 239
GLU 242;MET 243(Heme);HIS 336(Heme iron);THR 168;PHE 170;ASP 172;SER 174(Calcium)
CYS 150(Cysteine sulfenic acid)
1mhlDARG 239
GLU 242;MET 243(Heme);HIS 336(Heme iron);THR 168;PHE 170;ASP 172;SER 174(Calcium)
CYS 150(Cysteine sulfenic acid)
1mypCARG 239
GLU 242;MET 243(Heme);HIS 336(Heme iron);THR 168;PHE 170;ASP 172;SER 174(Calcium)
CYS 150(Cysteine sulfenic acid)
1mypDARG 239
GLU 242;MET 243(Heme);HIS 336(Heme iron);THR 168;PHE 170;ASP 172;SER 174(Calcium)
CYS 150(Cysteine sulfenic acid)

References for Catalytic Mechanism
ReferencesSectionsNo. of steps in catalysis
[5]

[6]

[10]Fig.3
[11]p.10970-10973
[12]SCHEME IV, p.5004
[17]Scheme 1, p.1178
[18]p.11964
[22]


references
[1]
PubMed ID2824790
JournalJ Mol Biol
Year1987
Volume196
Pages919-25
AuthorsFenna RE
TitleCrystallization and subunit structure of canine myeloperoxidase.
[2]
PubMed ID2832613
JournalJ Mol Biol
Year1988
Volume199
Pages395-6
AuthorsSutton BJ, Little C, Olsen RL, Willassen NP
TitlePreliminary crystallographic analysis of human myeloperoxidase.
[3]
PubMed ID2559209
JournalJ Mol Biol
Year1989
Volume210
Pages681-3
AuthorsZeng J, Fenna RE
TitleTetragonal crystals of canine myeloperoxidase suitable for X-ray structural analysis.
[4]
PubMed ID1321726
JournalFEBS Lett
Year1992
Volume302
Pages189-91
AuthorsJacquet A, Deleersnyder V, Garcia-Quintana L, Bollen A, Moguilevsky N
TitleSite-directed mutants of human myeloperoxidase. A topological approach to the heme-binding site.
[5]
CommentsX-ray crystallography
PubMed ID1320128
JournalJ Mol Biol
Year1992
Volume226
Pages185-207
AuthorsZeng J, Fenna RE
TitleX-ray crystal structure of canine myeloperoxidase at 3 A resolution.
Related PDB1myp
[6]
PubMed ID8037771
JournalBiochem Biophys Res Commun
Year1994
Volume202
Pages73-81
AuthorsJacquet A, Garcia-Quintana L, Deleersnyder V, Fenna R, Bollen A, Moguilevsky N
TitleSite-directed mutagenesis of human myeloperoxidase: further identification of residues involved in catalytic activity and heme interaction.
[7]
PubMed ID8062820
JournalEMBO J
Year1994
Volume13
Pages3438-47
AuthorsNelson RE, Fessler LI, Takagi Y, Blumberg B, Keene DR, Olson PF, Parker CG, Fessler JH
TitlePeroxidasin: a novel enzyme-matrix protein of Drosophila development.
[8]
PubMed ID8020506
JournalEur J Biochem
Year1994
Volume222
Pages677-85
AuthorsFloris R, Kim Y, Babcock GT, Wever R
TitleOptical spectrum of myeloperoxidase. Origin of the red shift.
[9]
PubMed ID8132563
JournalJ Biol Chem
Year1994
Volume269
Pages8388-92
AuthorsHori H, Fenna RE, Kimura S, Ikeda-Saito M
TitleAromatic substrate molecules bind at the distal heme pocket of myeloperoxidase.
[10]
CommentsX-RAY CRYSTALLOGRAPHY (2.25 ANGSTROMS) OF 167-744
Medline ID95142692
PubMed ID7840679
JournalArch Biochem Biophys
Year1995
Volume316
Pages653-6
AuthorsFenna R, Zeng J, Davey C
TitleStructure of the green heme in myeloperoxidase.
Related PDB1mhl
Related UniProtKBP05164
[11]
PubMed ID8718890
JournalBiochemistry
Year1996
Volume35
Pages10967-73
AuthorsDavey CA, Fenna RE
Title2.3 A resolution X-ray crystal structure of the bisubstrate analogue inhibitor salicylhydroxamic acid bound to human myeloperoxidase: a model for a prereaction complex with hydrogen peroxide.
[12]
PubMed ID9478947
JournalJ Biol Chem
Year1998
Volume273
Pages4997-5005
AuthorsHazen SL, d'Avignon A, Anderson MM, Hsu FF, Heinecke JW
TitleHuman neutrophils employ the myeloperoxidase-hydrogen peroxide-chloride system to oxidize alpha-amino acids to a family of reactive aldehydes. Mechanistic studies identifying labile intermediates along the reaction pathway.
[13]
PubMed ID10395733
JournalArch Biochem Biophys
Year1999
Volume367
Pages173-84
AuthorsNomura K, Hoshino K, Suzuki N
TitleThe primary and higher order structures of sea urchin ovoperoxidase as determined by cDNA cloning and predicted by homology modeling.
[14]
PubMed ID10585414
JournalJ Biol Chem
Year1999
Volume274
Pages35441-8
AuthorsLardinois OM, Medzihradszky KF, Ortiz de Montellano PR
TitleSpin trapping and protein cross-linking of the lactoperoxidase protein radical.
[15]
PubMed ID10069970
JournalJ Exp Biol
Year1999
Volume202
Pages809-16
AuthorsRibeiro JM, Valenzuela JG
TitlePurification and cloning of the salivary peroxidase/catechol oxidase of the mosquito Anopheles albimanus.
[16]
PubMed ID10805914
JournalBiopolymers
Year2000
Volume57
Pages169-78
AuthorsAraki K, Takeuchi H
TitleEffects of pH and chloride concentration on resonance Raman spectra of human myeloperoxidase and Raman microspectroscopic analysis of enzyme state in azurophilic granules.
[17]
PubMed ID11087440
JournalChem Res Toxicol
Year2000
Volume13
Pages1174-80
AuthorsStansbury KH, Noll DM, Groopman JD, Trush MA
TitleEnzyme-mediated dialdehyde formation: an alternative pathway for benzo[a]pyrene 7,8-dihydrodiol bioactivation.
[18]
CommentsX-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS) OF 167-744
Medline ID20229799
PubMed ID10766826
JournalJ Biol Chem
Year2000
Volume275
Pages11964-71
AuthorsFiedler TJ, Davey CA, Fenna RE
TitleX-ray crystal structure and characterization of halide-binding sites of human myeloperoxidase at 1.8 A resolution.
Related PDB1cxp,1d2v
Related UniProtKBP05164
[19]
PubMed ID10994874
JournalRedox Rep
Year2000
Volume5
Pages197-206
AuthorsNauseef WM, McCormick S, Goedken M
TitleImpact of missense mutations on biosynthesis of myeloperoxidase.
[20]
PubMed ID11159195
JournalAm J Pathol
Year2001
Volume158
Pages581-92
AuthorsYang JJ, Preston GA, Pendergraft WF, Segelmark M, Heeringa P, Hogan SL, Jennette JC, Falk RJ
TitleInternalization of proteinase 3 is concomitant with endothelial cell apoptosis and internalization of myeloperoxidase with generation of intracellular oxidants.
[21]
PubMed ID11237766
JournalBiochem Biophys Res Commun
Year2001
Volume281
Pages1024-9
AuthorsShin K, Hayasawa H, Lonnerdal B
TitleMutations affecting the calcium-binding site of myeloperoxidase and lactoperoxidase.
[22]
CommentsX-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) OF 167-744
Medline ID21562373
PubMed ID11705390
JournalBiochemistry
Year2001
Volume40
Pages13990-7
AuthorsBlair-Johnson M, Fiedler T, Fenna R
TitleHuman myeloperoxidase: structure of a cyanide complex and its interaction with bromide and thiocyanate substrates at 1.9 A resolution.
Related PDB1d5l,1d7w,1dnu,1dnw
Related UniProtKBP05164
[23]
PubMed ID11513872
JournalFEBS Lett
Year2001
Volume503
Pages147-50
AuthorsFurtmuller PG, Jantschko W, Regelsberger G, Jakopitsch C, Moguilevsky N, Obinger C
TitleA transient kinetic study on the reactivity of recombinant unprocessed monomeric myeloperoxidase.

comments
This enzyme is composed of light chain (chain A or B in PDB) and heavy chain (chain C or D in PDB).
Although this enzyme binds a calcium ion, it is not directly involved in catalysis.

createdupdated
2005-04-042009-02-26


Copyright: Nozomi Nagano, JST & CBRC-AIST
Funded by PRESTO/Japan Science and Technology Corporation (JST) (December 2001 - November 2004)
Funded by Grant-in-Aid for Publication of Scientific Research Results/Japan Society for the Promotion of Science (JSPS) (April 2005 - March 2006)
Funded by Grant-in-Aid for Scientific Research (B)/Japan Society for the Promotion of Science (JSPS) (April 2005 - March 2008)
Funded by BIRD/Japan Science and Technology Corporation (JST) (September 2005 - September 2008)
Funded by BIRD/Japan Science and Technology Corporation (JST) (October 2007 - September 2010)
Funded by Grant-in-Aid for Publication of Scientific Research Results/Japan Society for the Promotion of Science (JSPS) (April 2011 - March 2012)
Funded by Grant-in-Aid for Publication of Scientific Research Results/Japan Society for the Promotion of Science (JSPS) (April 2012 - March 2013)
Supported by the commission for the Development of Artificial Gene Synthesis Technology for Creating Innovative Biomaterial from the Ministry of Economy, Trade and Industry (METI) (October 2012 - )
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