Literature summary for 1.14.14.B10 extracted from

Ouellet, Y.H.; Ndiaye, C.T.; Gagne, S.M.; Sebilo, A.; Suits, M.D.; Jubinville, E.; Jia, Z.; Ivancich, A.; Couture, M.
An alternative reaction for heme degradation catalyzed by the Escherichia coli O157 H7 ChuS protein Release of hematinic acid, tripyrrole and Fe(III) (2016), J. Inorg. Biochem., 154, 103-113 .

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Natural Substrates/ Products (Substrates)

Natural Substrates	Organism	Comment (Nat. Sub.)	Natural Products	Comment (Nat. Pro.)	Rev.	Reac.
protoporphyrin IX + ascorbate + O2	Escherichia coli	cosubstrate is hydrogen peroxide that is formed in solution in the presence of ascorbate and O2	hematinic acid + a tripyrrole + Fe3+	-	?

Organism

Organism	UniProt	Comment	Textmining
Escherichia coli	Q8X5N8	-	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
additional information	enzyme binds and degrades heme in a reaction that releases carbon monoxide. Initial intermediates of the reaction of ChuS with hydrogen peroxide, i.e. a ferrous keto pi neutral radical and ferric verdoheme, are in common with heme oxygenases, while a further reaction step, involving the cleavage of the porphyrin ring at adjacent meso-carbons, results in the release of hematinic acid, a tripyrrole product and non-heme iron in the ferric oxidation state	Escherichia coli	?	-	?
protoporphyrin IX + ascorbate + O2	cosubstrate is hydrogen peroxide that is formed in solution in the presence of ascorbate and O2	Escherichia coli	hematinic acid + a tripyrrole + Fe3+	-	?

Synonyms

Synonyms	Comment	Organism
ChuS	-	Escherichia coli

Cofactor

Cofactor	Comment	Organism	Structure
heme	spectrum shows bands at 409, 549, and 586 nm	Escherichia coli

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Release 2023.1 (January 2023)