Literature summary for 1.11.2.2 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.

Search for more literature for 1.11.2.2

Crystallization (Commentary)

Crystallization (Comment)	Organism
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

Inhibitors	Comment	Organism	Structure
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)

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

Organism

Organism	UniProt	Comment	Textmining
Homo sapiens	P05164	-	-

Source Tissue

Source Tissue	Comment	Organism	Textmining
neutrophil	-	Homo sapiens	-

Substrates and Products (Substrate)

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

Subunits

Subunits	Comment	Organism
homodimer	x-ray crystallography	Homo sapiens

Synonyms

Synonyms	Comment	Organism
MPO	isoform C	Homo sapiens

Cofactor

Cofactor	Comment	Organism	Structure
heme	-	Homo sapiens

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Release 2023.1 (January 2023)