Literature summary extracted from

Colabroy, K.L.; Zhai, H.; Li, T.; Ge, Y.; Zhang, Y.; Liu, A.; Ealick, S.E.; McLafferty, F.W.; Begley, T.P.
The mechanism of inactivation of 3-hydroxyanthranilate-3,4-dioxygenase by 4-chloro-3-hydroxyanthranilate (2005), Biochemistry, 44, 7623-7631.

Inhibitors

EC Number	Inhibitors	Comment	Organism	Structure
1.13.11.6	4-Chloro-3-hydroxyanthranilate	the inactivation results in the consumption of 2 equivalents of oxygen and the production of superoxide. The inhibitor stimulates the oxidation of the active site Fe(II) to the catalytically inactive Fe(III) oxidation state. The inactivated enzyme can be reactivated by treatment with DTT and FeI(II). The nhibitor does not form an adduct with the enzyme. Four conserved cysteines are oxidized to two disulfides (Cys125-Cys128 and Cys162-Cys165) during the inactivation reaction. These results are consistent with a mechanism in which the enzyme, complexed to the inhibitor and O2, generates superoxide which subsequently dissociates, leaving the inhibitor and the oxidized iron center at the active site	Cupriavidus metallidurans

Organism

EC Number	Organism	UniProt	Comment	Textmining
1.13.11.6	Cupriavidus metallidurans	-	recombinantly expressed in Escherichia coli	-

Purification (Commentary)

EC Number	Purification (Comment)	Organism
1.13.11.6	-	Cupriavidus metallidurans

Substrates and Products (Substrate)

EC Number	Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
1.13.11.6	3-hydroxyanthranilate + O2	-	Cupriavidus metallidurans	2-amino-3-carboxymuconate semialdehyde	the enzymatic product subsequently cyclizes to quinolinate	?

Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.

Release 2023.1 (January 2023)