Literature summary for 7.2.1.3 extracted from

Ganasen, M.; Togashi, H.; Takeda, H.; Asakura, H.; Tosha, T.; Yamashita, K.; Hirata, K.; Nariai, Y.; Urano, T.; Yuan, X.; Hamza, I.; Mauk, A.G.; Shiro, Y.; Sugimotom, H.; Sawai, H.
Structural basis for promotion of duodenal iron absorption by enteric ferric reductase with ascorbate (2018), Commun. Biol., 1, 120 .

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Cloned(Commentary)

Cloned (Comment)	Organism
expression in Escherichia coli	Homo sapiens

Crystallization (Commentary)

Crystallization (Comment)	Organism
enzyme and its complex with ascorbate and Zn2+. Each monomer of the homodimeric protein possesses cytoplasmic and apical heme groups, as well as cytoplasmic and apical ascorbate-binding sites located adjacent to each heme. Zn2+ coordinates to two hydroxyl groups of the apical ascorbate and to a histidine residue. Fe3+ competes with Zn2+ for this binding site	Homo sapiens

Protein Variants

Protein Variants	Comment	Organism
F184A	35% residual activity	Homo sapiens
F58L	less than 50% residual activity	Homo sapiens
H108A	20% residual activity	Homo sapiens
H108Q	25% residual activity	Homo sapiens
Y117A	35% residual activity	Homo sapiens
Y117S	40% residual activity	Homo sapiens
Y131L	less than 50% residual activity	Homo sapiens

Inhibitors

Inhibitors	Comment	Organism	Structure
Zn2+	1 mM, 43% residual activity. Zn2+ coordinates to two hydroxyl groups of the apical ascorbate and to a histidine residue. Fe3+ competes with Zn2+ for this binding site	Homo sapiens

Localization

Localization	Comment	Organism	GeneOntology No.	Textmining
membrane	-	Homo sapiens	16020	-

Organism

Organism	UniProt	Comment	Textmining
Homo sapiens	Q53TN4	-	-

Source Tissue

Source Tissue	Comment	Organism	Textmining

Synonyms

Synonyms	Comment	Organism
cytochrome b reductase 1	-	Homo sapiens

Cofactor

Cofactor	Comment	Organism	Structure
heme	each monomer of the homodimeric protein possesses cytoplasmic and apical heme groups	Homo sapiens

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Release 2023.1 (January 2023)