Literature summary for 1.13.11.6 extracted from

Chakraborty, B.; Paine, T.
Aromatic ring cleavage of 2-amino-4-tert-butylphenol by a nonheme iron(II) complex: functional model of 2-aminophenol dioxygenases (2013), Angew. Chem. Int. Ed. Engl., 52, 920-924.

Search for more literature for 1.13.11.6

Metals/Ions

Metals/Ions	Comment	Organism	Structure
Fe2+	required, the active site of HAD contains an iron(II) center that is coordinated by the 2-His-1-Glu facial triad	Pseudomonas oleovorans

Natural Substrates/ Products (Substrates)

Natural Substrates	Organism	Comment (Nat. Sub.)	Natural Products	Comment (Nat. Pro.)	Rev.	Reac.
3-hydroxyanthranilate + O2	Pseudomonas oleovorans	-	2-amino-3-carboxymuconate semialdehyde	-	?

Organism

Organism	UniProt	Comment	Textmining
Pseudomonas oleovorans	-	-	-

Reaction

Reaction	Comment	Organism	Reaction ID
3-hydroxyanthranilate + O2 = 2-amino-3-carboxymuconate semialdehyde	reaction mechanism, overview	Pseudomonas oleovorans	a

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
3-hydroxyanthranilate + O2	-	Pseudomonas oleovorans	2-amino-3-carboxymuconate semialdehyde	-	?

Synonyms

Synonyms	Comment	Organism
HAD	-	Pseudomonas oleovorans

General Information

General Information	Comment	Organism
evolution	HAD belongs to the class of nonheme iron(II) enzymes and shares functional similarity with extradiol-cleaving catechol dioxygenases	Pseudomonas oleovorans
additional information	oxidative CC bond cleavage of 2-amino-4-tert-butylphenolate on complex nonheme iron(II) complex, [(6-Me3-TPA)FeII(4-tBu-HAP)](ClO4) is mimicking the enzyme function. The iron(II)-aminophenolate complex reacts with molecular oxygen in acetonitrile under ambient conditions, overview	Pseudomonas oleovorans
physiological function	the enzyme catalyzes the degradation of 3-hydroxyanthranilate to quinolinate in the presence of dioxygen	Pseudomonas oleovorans

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Release 2023.1 (January 2023)