Literature summary for 1.16.3.1 extracted from

Toussaint, L.; Cuypers, M.G.; Bertrand, L.; Hue, L.; Romao, C.V.; Saraiva, L.M.; Teixeira, M.; Meyer-Klaucke, W.; Feiters, M.C.; Crichton, R.R.
Comparative Fe and Zn K-edge X-ray absorption spectroscopic study of the ferroxidase centres of human H-chain ferritin and bacterioferritin from Desulfovibrio desulfuricans (2009), J. Biol. Inorg. Chem., 14, 35-49.

Search for more literature for 1.16.3.1

Cloned(Commentary)

Cloned (Comment)	Organism
-	Homo sapiens
overexpressed via plasmid in Escherichia coli strain BL21-Gold (DE3)	Desulfovibrio desulfuricans

Protein Variants

Protein Variants	Comment	Organism
K86Q	equivalent to wild-type	Homo sapiens
K86Q/E107D	reduced reduction activity	Homo sapiens
K86Q/E27D	in X-ray absorption same properties as wild-type, but reduced reduction activity	Homo sapiens
K86Q/E27D/E107D	no reduction activity	Homo sapiens

Inhibitors

Inhibitors	Comment	Organism	Structure
Zn2+	2 M Zn2+ occupies the ferroxidase center as redox-invariant analogue of Fe2+	Homo sapiens

Organism

Organism	UniProt	Comment	Textmining
Desulfovibrio desulfuricans	Q93PP9	-	-
Homo sapiens	-	-	-

Purification (Commentary)

Purification (Comment)	Organism
-	Homo sapiens
-	Desulfovibrio desulfuricans

Synonyms

Synonyms	Comment	Organism
bacterioferritin	-	Desulfovibrio desulfuricans
DdBfr	Desulfovibrio desulfuricans bacterioferritin	Desulfovibrio desulfuricans
HuHF	-	Homo sapiens
human H-chain ferritin	-	Homo sapiens
rHuHF	recombinant human H-chain ferritin	Homo sapiens

Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.

Release 2023.1 (January 2023)