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Literature summary extracted from

  • Wang, Y.; Liu, K.F.; Yang, Y.; Davis, I.; Liu, A.
    Observing 3-hydroxyanthranilate-3,4-dioxygenase in action through a crystalline lens (2020), Proc. Natl. Acad. Sci. USA, 117, 19720-19730.
    View publication on PubMed

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
1.13.11.6 seven catalytic intermediates are kinetically and structurally resolved in the crystalline state, and each accompanies protein conformational changes at the active site. Among them, a monooxygenated, seven-membered lactone intermediate as a monodentate ligand of the iron center at 1.59 A resolution is captured, which presumably corresponds to a substrate-based radical species observed by EPR using a slurry of small-sized single crystals. Other structural snapshots determined at around 2.0 A resolution include monodentate and subsequently bidentate coordinated substrate, superoxo, alkylperoxo, and two metal-bound enol tautomers of the unstable dioxygenase product Cupriavidus metallidurans

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
1.13.11.6 Iron nonheme iron-based enzyme Cupriavidus metallidurans

Organism

EC Number Organism UniProt Comment Textmining
1.13.11.6 Cupriavidus metallidurans Q1LCS4
-
-
1.13.11.6 Cupriavidus metallidurans ATCC 43123 Q1LCS4
-
-

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
-
 ?
1.13.11.6 3-hydroxyanthranilate + O2
-
 Cupriavidus metallidurans ATCC 43123 2-amino-3-carboxymuconate semialdehyde
-
 ?

Synonyms

EC Number Synonyms Comment Organism
1.13.11.6 HAO
-
 Cupriavidus metallidurans