Literature summary for 1.13.11.53 extracted from

Ivan, D.A.; Gremillion, A.J.; Sanchez, A.; Sanchez, S.; Lynch, V.M.; Toledo, S.A.
The first structural model for the resting state of the active site of nickel acireductone dioxygenase (Ni-ARD) (2018), Inorg. Chem. Commun., 89, 37-40 .

No PubMed abstract available

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Natural Substrates/ Products (Substrates)

Natural Substrates	Organism	Comment (Nat. Sub.)	Natural Products	Comment (Nat. Pro.)	Rev.	Reac.
1,2-dihydroxy-5-(methylsulfanyl)pent-1-en-3-one + O2	Mus musculus	-	4-(methylsulfanyl)-2-oxobutanoate + formate	-	?

Organism

Organism	UniProt	Comment	Textmining
Mus musculus	Q99JT9	-	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
1,2-dihydroxy-5-(methylsulfanyl)pent-1-en-3-one + O2	-	Mus musculus	4-(methylsulfanyl)-2-oxobutanoate + formate	-	?
additional information	the nickel complex [NiII(OPhN4(6-H-DPEN)(H2O))] is a structural analogue for the resting state of the active site of the nickel oxygenase nickel acireductone dioxyegenase and capable of carbon-carbon bond cleavage of a ketone presumably via dioxygenase type chemistry in line with the reactivity of the enzyme	Mus musculus	?	-	-

Synonyms

Synonyms	Comment	Organism
Ni-ARD	-	Mus musculus
nickel acireductone dioxyegenase	-	Mus musculus

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Release 2023.1 (January 2023)