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Literature summary for 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.
    View publication on PubMed


Inhibitors Comment Organism Structure
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 UniProt Comment Textmining
Cupriavidus metallidurans
recombinantly expressed in Escherichia coli

Purification (Commentary)

Purification (Comment) Organism
Cupriavidus metallidurans

Substrates and Products (Substrate)

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