Literature summary for 7.2.1.3 extracted from

Lu, P.; Ma, D.; Yan, C.; Gong, X.; Du, M.; Shi, Y.
Structure and mechanism of a eukaryotic transmembrane ascorbate-dependent oxidoreductase (2014), Proc. Natl. Acad. Sci. USA, 111, 1813-1818.

Search for more literature for 7.2.1.3

Cloned(Commentary)

Cloned (Comment)	Organism
expressed in Escherichia coli	Arabidopsis thaliana

Crystallization (Commentary)

Crystallization (Comment)	Organism
high-resolution crystal structures of cytochrome b561 from Arabidopsis thaliana in both substrate-free and substrate-bound states is reported. Cyt b561 forms a homodimer, with each protomer consisting of six transmembrane helices and two heme groups	Arabidopsis thaliana

Protein Variants

Protein Variants	Comment	Organism
F105W/H106E	mutations on the noncytoplasmic side only still allows the oxidized Cyt b561 to be reduced by ascorbate	Arabidopsis thaliana
K81A/R150A	mutations on the cytoplasmic side only still allows the oxidized Cyt b561 to be reduced by ascorbate	Arabidopsis thaliana
K81A/R150A/F105W/H106E	mutant carrying ascorbate-binding mutations on both cytoplasmic and noncytoplasmic sides, completely loses its ability to be reduced by ascorbate	Arabidopsis thaliana
Y115W	mutations on the noncytoplasmic side only still allows the oxidized Cyt b561 to be reduced by ascorbate	Arabidopsis thaliana
Y140W	mutations on the cytoplasmic side only still allows the oxidized Cyt b561 to be reduced by ascorbate	Arabidopsis thaliana

Organism

Organism	UniProt	Comment	Textmining
Arabidopsis thaliana	Q9SWS1	-	-

Purification (Commentary)

Purification (Comment)	Organism
purified by affinity chromatography and gel filtration	Arabidopsis thaliana

Subunits

Subunits	Comment	Organism
homodimer	-	Arabidopsis thaliana

Synonyms

Synonyms	Comment	Organism
Cyt b561	-	Arabidopsis thaliana
cytochrome b561	-	Arabidopsis thaliana

General Information

General Information	Comment	Organism
metabolism	oxidized Cyt b561 is reduced by ascorbate	Arabidopsis thaliana

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Release 2023.1 (January 2023)