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Literature summary extracted from

  • Fiedler, T.J.; Davey, C.A.; Fenna, R.E.
    X-ray crystal structure and characterization of halide-binding sites of human myeloperoxidase at 1.8 A resolution (2000), J. Biol. Chem., 275, 11964-11971.
    View publication on PubMed

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
1.11.2.2 hanging drop vapor diffusion method, using 50 mM sodium acetate (pH 5.5), 50 mM ammonium sulfate, 2 mM calcium chloride, and 22-25% (w/v) PEG 8k, at 18°C Homo sapiens

Inhibitors

EC Number Inhibitors Comment Organism Structure
1.11.2.2 Br- bromide binding to the halide-binding site responsible for shifts in the Soret band of the absorption spectrum of myeloperoxidase inhibits the enzyme by effectively competing with H2O2 for access to the distal histidine Homo sapiens

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.11.2.2 Cl- + H2O2 + H+ Homo sapiens
-
 HClO + H2O
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
1.11.2.2 Homo sapiens P05164
-
-

Source Tissue

EC Number Source Tissue Comment Organism Textmining
1.11.2.2 neutrophil
-
 Homo sapiens
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.11.2.2 Cl- + H2O2 + H+
-
 Homo sapiens HClO + H2O
-
 ?

Subunits

EC Number Subunits Comment Organism
1.11.2.2 homodimer x-ray crystallography Homo sapiens

Synonyms

EC Number Synonyms Comment Organism
1.11.2.2 MPO isoform C Homo sapiens

Cofactor

EC Number Cofactor Comment Organism Structure
1.11.2.2 heme
-
 Homo sapiens