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

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

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

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

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

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)

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

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.

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
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
journal: J Mol Biol
volume: 226
pages: 185-207
published year: 1992
authors:
  item: Zeng J
  item: Fenna RE

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
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: P05164
journal: Arch Biochem Biophys
volume: 316
pages: 653-6
published year: 1995
authors:
  item: Fenna R
  item: Zeng J
  item: Davey C

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
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: P05164
journal: J Biol Chem
volume: 275
pages: 11964-71
published year: 2000
authors:
  item: Fiedler TJ
  item: Davey CA
  item: Fenna RE

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
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: P05164
journal: Biochemistry
volume: 40
pages: 13990-7
published year: 2001
authors:
  item: Blair-Johnson M
  item: Fiedler T
  item: Fenna R

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