Literature summary for 1.11.1.12 extracted from

Scheerer, P.; Borchert, A.; Krauss, N.; Wessner, H.; Gerth, C.; Hoehne, W.; Kuhn, H.
Structural basis for catalytic activity and enzyme polymerization of phospholipid hydroperoxide glutathione peroxidase-4 (GPx4) (2007), Biochemistry, 46, 9041-9049.

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Cloned(Commentary)

Cloned (Comment)	Organism
expression of mutant enzyme U46C in Escherichia coli	Homo sapiens

Crystallization (Commentary)

Crystallization (Comment)	Organism
sparse matrix crystallization method, crystal structure of the catalytically active U46C mutant of human GPx4 to 1.55 A resolution	Homo sapiens

Localization

Localization	Comment	Organism	GeneOntology No.	Textmining
cytosol	-	Homo sapiens	5829	-

Organism

Organism	UniProt	Comment	Textmining
Homo sapiens	P36969	-	-

Subunits

Subunits	Comment	Organism
More	like the wild-type enzyme, the U46C mutant exhibits a strong tendency toward protein polymerization, which was prevented by reductants	Homo sapiens

Synonyms

Synonyms	Comment	Organism
GPx4	-	Homo sapiens
phospholipid hydroperoxide glutathione peroxidase-4	-	Homo sapiens

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Release 2023.1 (January 2023)