D00483
type: Enzyme
cath: http://ezcatdb.cbrc.jp/EzCatDB/cath/1.-.-.-
cath: Myeloperoxidase, subunit C
ec: https://purl.uniprot.org/enzyme/1.11.1.7
csa: 1mhl
uniprot: P05164
kegg enzyme: peroxidase
kegg enzyme: myeloperoxidase
kegg enzyme: lactoperoxidase
kegg pathway: Phenylalanine metabolism
kegg pathway: Methane metabolism
kegg pathway: Phenylpropanoid biosynthesis
kegg cofactor: Heme
kegg cofactor: Calcium
kegg substrate: Donor
kegg substrate: H2O2
kegg substrate: Chloride
kegg product: Oxidized donor
kegg product: H2O
kegg product: Hypochlorite
pdb: 1cxpA
pdb: 1cxpB
pdb: 1d2vA
pdb: 1d2vB
pdb: 1d5lA
pdb: 1d5lB
pdb: 1d7wA
pdb: 1d7wB
pdb: 1dnuA
pdb: 1dnuB
pdb: 1dnwA
pdb: 1dnwB
pdb: 1mhlA
pdb: 1mhlB
pdb: 1mypA
pdb: 1mypB
pdb: 1cxpC
pdb: 1cxpD
pdb: 1d2vC
pdb: 1d2vD
pdb: 1d5lC
pdb: 1d5lD
pdb: 1d7wC
pdb: 1d7wD
pdb: 1dnuC
pdb: 1dnuD
pdb: 1dnwC
pdb: 1dnwD
pdb: 1mhlC
pdb: 1mhlD
pdb: 1mypC
pdb: 1mypD
active site residues resources: Site-directed mutagenesis of human myeloperoxidase: further identification of residues involved in catalytic activity and heme interaction.
active site residues resources: 2.3 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.
active site residues resources: http://ezcatdb.cbrc.jp/EzCatDB/reference/D00483#12
active site residues resources: P05164
references: Preliminary crystallographic analysis of human myeloperoxidase.
references: Tetragonal crystals of canine myeloperoxidase suitable for X-ray structural analysis.
references: Crystallization and subunit structure of canine myeloperoxidase.
references: Site-directed mutants of human myeloperoxidase. A topological approach to the heme-binding site.
references: X-ray crystal structure of canine myeloperoxidase at 3 A resolution.
references: Site-directed mutagenesis of human myeloperoxidase: further identification of residues involved in catalytic activity and heme interaction.
references: Peroxidasin: a novel enzyme-matrix protein of Drosophila development.
references: Optical spectrum of myeloperoxidase. Origin of the red shift.
references: Aromatic substrate molecules bind at the distal heme pocket of myeloperoxidase.
references: Structure of the green heme in myeloperoxidase.
references: 2.3 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.
references: http://ezcatdb.cbrc.jp/EzCatDB/reference/D00483#12
references: The primary and higher order structures of sea urchin ovoperoxidase as determined by cDNA cloning and predicted by homology modeling.
references: Spin trapping and protein cross-linking of the lactoperoxidase protein radical.
references: Purification and cloning of the salivary peroxidase/catechol oxidase of the mosquito Anopheles albimanus.
references: Effects of pH and chloride concentration on resonance Raman spectra of human myeloperoxidase and Raman microspectroscopic analysis of enzyme state in azurophilic granules.
references: Enzyme-mediated dialdehyde formation: an alternative pathway for benzo[a]pyrene 7,8-dihydrodiol bioactivation.
references: X-ray crystal structure and characterization of halide-binding sites of human myeloperoxidase at 1.8 A resolution.
references: Impact of missense mutations on biosynthesis of myeloperoxidase.
references: Internalization of proteinase 3 is concomitant with endothelial cell apoptosis and internalization of myeloperoxidase with generation of intracellular oxidants.
references: Mutations affecting the calcium-binding site of myeloperoxidase and lactoperoxidase.
references: Human myeloperoxidase: structure of a cyanide complex and its interaction with bromide and thiocyanate substrates at 1.9 A resolution.
references: A transient kinetic study on the reactivity of recombinant unprocessed monomeric myeloperoxidase.
comment: 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.

Myeloperoxidase, subunit C
type: Cath
references: http://www.cathdb.info/version/latest/superfamily/1.10.640.10
catalytic domain: index.html

Phenylalanine metabolism
type: KeggPathway
references: KEGG:MAP00360

Methane metabolism
type: KeggPathway
references: KEGG:MAP00680

Phenylpropanoid biosynthesis
type: KeggPathway
references: KEGG:MAP00940

Heme
type: KeggCofactor
references: KEGG:C00032
compound type: aromatic ring (with nitrogen atoms)
compound type: carboxyl group
compound type: heavy metal
references: CHEBI:17627
references: CHEBI:26355

Calcium
type: KeggCofactor
references: KEGG:C00076
compound type: divalent metal (Ca2+, Mg2+)
references: CHEBI:29108
references: http://pubchem.ncbi.nlm.nih.gov/summary/summary.cgi

Donor
type: KeggSubstrate
references: KEGG:C01351
compound type: others

H2O2
type: KeggSubstrate
references: KEGG:C00027
compound type: others
references: CHEBI:16240
references: http://pubchem.ncbi.nlm.nih.gov/summary/summary.cgi

Chloride
type: KeggSubstrate
references: KEGG:C00115
compound type: halide

Oxidized donor
type: KeggProduct
references: KEGG:C02177
compound type: others

H2O
type: KeggProduct
references: KEGG:C00001
compound type: H2O
references: CHEBI:15377
references: http://pubchem.ncbi.nlm.nih.gov/summary/summary.cgi

Hypochlorite
type: KeggProduct
references: KEGG:C99999
compound type: halide

1cxpA
type: Pdb
references: 1cxp
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1cxp
catalytic residue: GLN 91;HIS 95
cofactor binding residue: ASP 94(Heme);ASP 96(Calcium)

1cxpB
type: Pdb
references: 1cxp
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1cxp
catalytic residue: GLN 91;HIS 95
cofactor binding residue: ASP 94(Heme);ASP 96(Calcium)

1d2vA
type: Pdb
references: 1d2v
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1d2v
catalytic residue: GLN 91;HIS 95
cofactor binding residue: ASP 94(Heme);ASP 96(Calcium)

1d2vB
type: Pdb
references: 1d2v
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1d2v
catalytic residue: GLN 91;HIS 95
cofactor binding residue: ASP 94(Heme);ASP 96(Calcium)

1d5lA
type: Pdb
references: 1d5l
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1d5l
catalytic residue: GLN 91;HIS 95
cofactor binding residue: ASP 94(Heme);ASP 96(Calcium)

1d5lB
type: Pdb
references: 1d5l
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1d5l
catalytic residue: GLN 91;HIS 95
cofactor binding residue: ASP 94(Heme);ASP 96(Calcium)

1d7wA
type: Pdb
references: 1d7w
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1d7w
catalytic residue: GLN 91;HIS 95
cofactor binding residue: ASP 94(Heme);ASP 96(Calcium)

1d7wB
type: Pdb
references: 1d7w
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1d7w
catalytic residue: GLN 91;HIS 95
cofactor binding residue: ASP 94(Heme);ASP 96(Calcium)

1dnuA
type: Pdb
references: 1dnu
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1dnu
catalytic residue: GLN 91;HIS 95
cofactor binding residue: ASP 94(Heme);ASP 96(Calcium)

1dnuB
type: Pdb
references: 1dnu
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1dnu
catalytic residue: GLN 91;HIS 95
cofactor binding residue: ASP 94(Heme);ASP 96(Calcium)

1dnwA
type: Pdb
references: 1dnw
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1dnw
catalytic residue: GLN 91;HIS 95
cofactor binding residue: ASP 94(Heme);ASP 96(Calcium)

1dnwB
type: Pdb
references: 1dnw
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1dnw
catalytic residue: GLN 91;HIS 95
cofactor binding residue: ASP 94(Heme);ASP 96(Calcium)

1mhlA
type: Pdb
references: 1mhl
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1mhl
catalytic residue: GLN 91;HIS 95
cofactor binding residue: ASP 94(Heme);ASP 96(Calcium)

1mhlB
type: Pdb
references: 1mhl
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1mhl
catalytic residue: GLN 91;HIS 95
cofactor binding residue: ASP 94(Heme);ASP 96(Calcium)

1mypA
type: Pdb
references: 1myp
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1myp
catalytic residue: GLN 91;HIS 95
cofactor binding residue: ASP 94(Heme);ASP 96(Calcium)

1mypB
type: Pdb
references: 1myp
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1myp
catalytic residue: GLN 91;HIS 95
cofactor binding residue: ASP 94(Heme);ASP 96(Calcium)

1cxpC
type: Pdb
references: 1cxp
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1cxp
catalytic residue: ARG 239
cofactor binding residue: GLU 242;MET 243(Heme);HIS 336(Heme iron);THR 168;PHE 170;ASP 172;SER 174(Calcium)
modified residue: CSO 150(Cysteine sulfenic acid)

1cxpD
type: Pdb
references: 1cxp
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1cxp
catalytic residue: ARG 239
cofactor binding residue: GLU 242;MET 243(Heme);HIS 336(Heme iron);THR 168;PHE 170;ASP 172;SER 174(Calcium)
modified residue: CSO 150(Cysteine sulfenic acid)

1d2vC
type: Pdb
references: 1d2v
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1d2v
catalytic residue: ARG 239
cofactor binding residue: GLU 242;MET 243(Heme);HIS 336(Heme iron);THR 168;PHE 170;ASP 172;SER 174(Calcium)
modified residue: CSO 150(Cysteine sulfenic acid)

1d2vD
type: Pdb
references: 1d2v
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1d2v
catalytic residue: ARG 239
cofactor binding residue: GLU 242;MET 243(Heme);HIS 336(Heme iron);THR 168;PHE 170;ASP 172;SER 174(Calcium)
modified residue: CSO 150(Cysteine sulfenic acid)

1d5lC
type: Pdb
references: 1d5l
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1d5l
catalytic residue: ARG 239
cofactor binding residue: GLU 242;MET 243(Heme);HIS 336(Heme iron);THR 168;PHE 170;ASP 172;SER 174(Calcium)
modified residue: CSO 150(Cysteine sulfenic acid)

1d5lD
type: Pdb
references: 1d5l
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1d5l
catalytic residue: ARG 239
cofactor binding residue: GLU 242;MET 243(Heme);HIS 336(Heme iron);THR 168;PHE 170;ASP 172;SER 174(Calcium)
modified residue: CSO 150(Cysteine sulfenic acid)

1d7wC
type: Pdb
references: 1d7w
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1d7w
catalytic residue: ARG 239
cofactor binding residue: GLU 242;MET 243(Heme);HIS 336(Heme iron);THR 168;PHE 170;ASP 172;SER 174(Calcium)
modified residue: CSO 150(Cysteine sulfenic acid)

1d7wD
type: Pdb
references: 1d7w
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1d7w
catalytic residue: ARG 239
cofactor binding residue: GLU 242;MET 243(Heme);HIS 336(Heme iron);THR 168;PHE 170;ASP 172;SER 174(Calcium)
modified residue: CSO 150(Cysteine sulfenic acid)

1dnuC
type: Pdb
references: 1dnu
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1dnu
catalytic residue: ARG 239
cofactor binding residue: GLU 242;MET 243(Heme);HIS 336(Heme iron);THR 168;PHE 170;ASP 172;SER 174(Calcium)
modified residue: CSO 150(Cysteine sulfenic acid)

1dnuD
type: Pdb
references: 1dnu
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1dnu
catalytic residue: ARG 239
cofactor binding residue: GLU 242;MET 243(Heme);HIS 336(Heme iron);THR 168;PHE 170;ASP 172;SER 174(Calcium)
modified residue: CSO 150(Cysteine sulfenic acid)

1dnwC
type: Pdb
references: 1dnw
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1dnw
catalytic residue: ARG 239
cofactor binding residue: GLU 242;MET 243(Heme);HIS 336(Heme iron);THR 168;PHE 170;ASP 172;SER 174(Calcium)
modified residue: CSO 150(Cysteine sulfenic acid)

1dnwD
type: Pdb
references: 1dnw
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1dnw
catalytic residue: ARG 239
cofactor binding residue: GLU 242;MET 243(Heme);HIS 336(Heme iron);THR 168;PHE 170;ASP 172;SER 174(Calcium)
modified residue: CSO 150(Cysteine sulfenic acid)

1mhlC
type: Pdb
references: 1mhl
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1mhl
catalytic residue: ARG 239
cofactor binding residue: GLU 242;MET 243(Heme);HIS 336(Heme iron);THR 168;PHE 170;ASP 172;SER 174(Calcium)
modified residue: CYS 150(Cysteine sulfenic acid)

1mhlD
type: Pdb
references: 1mhl
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1mhl
catalytic residue: ARG 239
cofactor binding residue: GLU 242;MET 243(Heme);HIS 336(Heme iron);THR 168;PHE 170;ASP 172;SER 174(Calcium)
modified residue: CYS 150(Cysteine sulfenic acid)

1mypC
type: Pdb
references: 1myp
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1myp
catalytic residue: ARG 239
cofactor binding residue: GLU 242;MET 243(Heme);HIS 336(Heme iron);THR 168;PHE 170;ASP 172;SER 174(Calcium)
modified residue: CYS 150(Cysteine sulfenic acid)

1mypD
type: Pdb
references: 1myp
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1myp
catalytic residue: ARG 239
cofactor binding residue: GLU 242;MET 243(Heme);HIS 336(Heme iron);THR 168;PHE 170;ASP 172;SER 174(Calcium)
modified residue: CYS 150(Cysteine sulfenic acid)

Preliminary crystallographic analysis of human myeloperoxidase.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/2832613
journal: J Mol Biol
volume: 199
pages: 395-6
published year: 1988
authors:
  item: Sutton BJ
  item: Little C
  item: Olsen RL
  item: Willassen NP

Tetragonal crystals of canine myeloperoxidase suitable for X-ray structural analysis.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/2559209
journal: J Mol Biol
volume: 210
pages: 681-3
published year: 1989
authors:
  item: Zeng J
  item: Fenna RE

Crystallization and subunit structure of canine myeloperoxidase.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/2824790
journal: J Mol Biol
volume: 196
pages: 919-25
published year: 1987
authors:
  item: Fenna RE

Site-directed mutants of human myeloperoxidase. A topological approach to the heme-binding site.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/1321726
journal: FEBS Lett
volume: 302
pages: 189-91
published year: 1992
authors:
  item: Jacquet A
  item: Deleersnyder V
  item: Garcia-Quintana L
  item: Bollen A
  item: Moguilevsky N

X-ray crystal structure of canine myeloperoxidase at 3 A resolution.
type: BibliographicResource
comment: X-ray crystallography
references: http://www.ncbi.nlm.nih.gov/pubmed/1320128
journal: J Mol Biol
volume: 226
pages: 185-207
published year: 1992
authors:
  item: Zeng J
  item: Fenna RE
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl

Site-directed mutagenesis of human myeloperoxidase: further identification of residues involved in catalytic activity and heme interaction.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/8037771
journal: Biochem Biophys Res Commun
volume: 202
pages: 73-81
published year: 1994
authors:
  item: Jacquet A
  item: Garcia-Quintana L
  item: Deleersnyder V
  item: Fenna R
  item: Bollen A
  item: Moguilevsky N

Peroxidasin: a novel enzyme-matrix protein of Drosophila development.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/8062820
journal: EMBO J
volume: 13
pages: 3438-47
published year: 1994
authors:
  item: Nelson RE
  item: Fessler LI
  item: Takagi Y
  item: Blumberg B
  item: Keene DR
  item: Olson PF
  item: Parker CG
  item: Fessler JH

Optical spectrum of myeloperoxidase. Origin of the red shift.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/8020506
journal: Eur J Biochem
volume: 222
pages: 677-85
published year: 1994
authors:
  item: Floris R
  item: Kim Y
  item: Babcock GT
  item: Wever R

Aromatic substrate molecules bind at the distal heme pocket of myeloperoxidase.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/8132563
journal: J Biol Chem
volume: 269
pages: 8388-92
published year: 1994
authors:
  item: Hori H
  item: Fenna RE
  item: Kimura S
  item: Ikeda-Saito M

Structure of the green heme in myeloperoxidase.
type: BibliographicResource
comment: X-RAY CRYSTALLOGRAPHY (2.25 ANGSTROMS) OF 167-744
medline id: 95142692
references: http://www.ncbi.nlm.nih.gov/pubmed/7840679
journal: Arch Biochem Biophys
volume: 316
pages: 653-6
published year: 1995
authors:
  item: Fenna R
  item: Zeng J
  item: Davey C
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: P05164

2.3 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.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/8718890
journal: Biochemistry
volume: 35
pages: 10967-73
published year: 1996
authors:
  item: Davey CA
  item: Fenna RE

http://ezcatdb.cbrc.jp/EzCatDB/reference/D00483#12
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/9478947
journal: J Biol Chem
volume: 273
pages: 4997-5005
published year: 1998
authors:
  item: Hazen SL
  item: d'Avignon A
  item: Anderson MM
  item: Hsu FF
  item: Heinecke JW
title: Human 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.

The primary and higher order structures of sea urchin ovoperoxidase as determined by cDNA cloning and predicted by homology modeling.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/10395733
journal: Arch Biochem Biophys
volume: 367
pages: 173-84
published year: 1999
authors:
  item: Nomura K
  item: Hoshino K
  item: Suzuki N

Spin trapping and protein cross-linking of the lactoperoxidase protein radical.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/10585414
journal: J Biol Chem
volume: 274
pages: 35441-8
published year: 1999
authors:
  item: Lardinois OM
  item: Medzihradszky KF
  item: Ortiz de Montellano PR

Purification and cloning of the salivary peroxidase/catechol oxidase of the mosquito Anopheles albimanus.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/10069970
journal: J Exp Biol
volume: 202
pages: 809-16
published year: 1999
authors:
  item: Ribeiro JM
  item: Valenzuela JG

Effects of pH and chloride concentration on resonance Raman spectra of human myeloperoxidase and Raman microspectroscopic analysis of enzyme state in azurophilic granules.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/10805914
journal: Biopolymers
volume: 57
pages: 169-78
published year: 2000
authors:
  item: Araki K
  item: Takeuchi H

Enzyme-mediated dialdehyde formation: an alternative pathway for benzo[a]pyrene 7,8-dihydrodiol bioactivation.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/11087440
journal: Chem Res Toxicol
volume: 13
pages: 1174-80
published year: 2000
authors:
  item: Stansbury KH
  item: Noll DM
  item: Groopman JD
  item: Trush MA

X-ray crystal structure and characterization of halide-binding sites of human myeloperoxidase at 1.8 A resolution.
type: BibliographicResource
comment: X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS) OF 167-744
medline id: 20229799
references: http://www.ncbi.nlm.nih.gov/pubmed/10766826
journal: J Biol Chem
volume: 275
pages: 11964-71
published year: 2000
authors:
  item: Fiedler TJ
  item: Davey CA
  item: Fenna RE
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: P05164

Impact of missense mutations on biosynthesis of myeloperoxidase.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/10994874
journal: Redox Rep
volume: 5
pages: 197-206
published year: 2000
authors:
  item: Nauseef WM
  item: McCormick S
  item: Goedken M

Internalization of proteinase 3 is concomitant with endothelial cell apoptosis and internalization of myeloperoxidase with generation of intracellular oxidants.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/11159195
journal: Am J Pathol
volume: 158
pages: 581-92
published year: 2001
authors:
  item: Yang JJ
  item: Preston GA
  item: Pendergraft WF
  item: Segelmark M
  item: Heeringa P
  item: Hogan SL
  item: Jennette JC
  item: Falk RJ

Mutations affecting the calcium-binding site of myeloperoxidase and lactoperoxidase.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/11237766
journal: Biochem Biophys Res Commun
volume: 281
pages: 1024-9
published year: 2001
authors:
  item: Shin K
  item: Hayasawa H
  item: Lonnerdal B

Human myeloperoxidase: structure of a cyanide complex and its interaction with bromide and thiocyanate substrates at 1.9 A resolution.
type: BibliographicResource
comment: X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) OF 167-744
medline id: 21562373
references: http://www.ncbi.nlm.nih.gov/pubmed/11705390
journal: Biochemistry
volume: 40
pages: 13990-7
published year: 2001
authors:
  item: Blair-Johnson M
  item: Fiedler T
  item: Fenna R
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: P05164

A transient kinetic study on the reactivity of recombinant unprocessed monomeric myeloperoxidase.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/11513872
journal: FEBS Lett
volume: 503
pages: 147-50
published year: 2001
authors:
  item: Furtmuller PG
  item: Jantschko W
  item: Regelsberger G
  item: Jakopitsch C
  item: Moguilevsky N
  item: Obinger C

verdoperoxidase
type: KeggEnzyme

guaiacol peroxidase
type: KeggEnzyme

thiocyanate peroxidase
type: KeggEnzyme

eosinophil peroxidase
type: KeggEnzyme

Japanese radish peroxidase
type: KeggEnzyme

horseradish peroxidase (HRP)
type: KeggEnzyme

extensin peroxidase
type: KeggEnzyme

heme peroxidase
type: KeggEnzyme

MPO
type: KeggEnzyme

oxyperoxidase
type: KeggEnzyme

protoheme peroxidase
type: KeggEnzyme

pyrocatechol peroxidase
type: KeggEnzyme

scopoletin peroxidase
type: KeggEnzyme

Analogue
compound: Donor
pdb: 1d5lA
ligand het code: CYN_1844

Analogue
compound: Donor
pdb: 1d5lB
ligand het code: CYN_1844

Analogue
compound: Donor
pdb: 1d7wA
ligand het code: CYN

Analogue
compound: Donor
pdb: 1d7wB
ligand het code: CYN

Analogue
compound: Donor
pdb: 1dnuA
ligand het code: SCN_5

Analogue
compound: Donor
pdb: 1dnuB
ligand het code: SCN_4

Analogue
compound: Donor
pdb: 1dnwA
ligand het code: CYN_3

Analogue
compound: Donor
pdb: 1dnwB
ligand het code: CYN_4

Analogue
compound: Chloride
pdb: 1d2vA
ligand het code: _BR_843

Analogue
compound: Chloride
pdb: 1d2vB
ligand het code: _BR_843

Analogue
compound: Chloride
pdb: 1d7wA
ligand het code: _BR_957

Analogue
compound: Chloride
pdb: 1d7wB
ligand het code: _BR_957

ReferenceForCatalyticMechanism
reference index: 5

ReferenceForCatalyticMechanism
reference index: 6

ReferenceForCatalyticMechanism
reference index: 10
reference section: Fig.3

ReferenceForCatalyticMechanism
reference index: 11
reference section: p.10970-10973

ReferenceForCatalyticMechanism
reference index: 12
reference section: SCHEME IV, p.5004

ReferenceForCatalyticMechanism
reference index: 17
reference section: Scheme 1, p.1178

ReferenceForCatalyticMechanism
reference index: 18
reference section: p.11964

ReferenceForCatalyticMechanism
reference index: 22