Literature summary extracted from

Pipirou, Z.; Bottrill, A.R.; Metcalfe, C.M.; Mistry, S.C.; Badyal, S.K.; Rawlings, B.J.; Raven, E.L.
Autocatalytic formation of a covalent link between tryptophan 41 and the heme in ascorbate peroxidase (2007), Biochemistry, 46, 2174-2180.

Localization

EC Number	Localization	Comment	Organism	GeneOntology No.	Textmining
1.11.1.11	cytosol	-	Glycine max	5829	-

Organism

EC Number	Organism	UniProt	Comment	Textmining
1.11.1.11	Glycine max	Q43758	-	-

Purification (Commentary)

EC Number	Purification (Comment)	Organism
1.11.1.11	-	Glycine max

Substrates and Products (Substrate)

EC Number	Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
1.11.1.11	L-ascorbate + H2O2	-	Glycine max	dehydroascorbate + H2O	-	?

Cofactor

EC Number	Cofactor	Comment	Organism	Structure
1.11.1.11	heme	covalent linking of Trp41 to the heme group in ascorbate peroxidase can occur on exposure of the enzyme to peroxide. A reaction mechanism involving formation of a protein radical at Trp41 is implicated to account for this observation	Glycine max

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Release 2023.1 (January 2023)