HIS 234;HIS 236;GLU 241;HIS 275(Iron-2 binding)
HIS 62;HIS 64;GLU 69;HIS 103(Iron-1 binding)
Crystal structure of human homogentisate dioxygenase.
Germin is a manganese containing homohexamer with oxalate oxidase and superoxide dismutase activities.
X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) IN COMPLEX WITH DIETHYLDITHIOCARBAMATE AND KOJIC ACID.
Functional analysis of the copper-dependent quercetin 2,3-dioxygenase. 1. Ligand-induced coordination changes probed by X-ray crystallography: inhibition, ordering effect, and mechanistic insights.
Functional analysis of the copper-dependent quercetin 2,3-dioxygenase. 2. X-ray absorption studies of native enzyme and anaerobic complexes with the substrates quercetin and myricetin.
X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS) IN COMPLEX WITH KAEMPFEROL AND QUERCETIN.
Anaerobic enzyme.substrate structures provide insight into the reaction mechanism of the copper-dependent quercetin 2,3-dioxygenase.
X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS), MUTAGENESIS OF GLU-73.
Crystal structure of the copper-containing quercetin 2,3-dioxygenase from Aspergillus japonicus.
Bacillus subtilis YxaG is a novel Fe-containing quercetin 2,3-dioxygenase.
The crystal structure of a quercetin 2,3-dioxygenase from Bacillus subtilis suggests modulation of enzyme activity by a change in the metal ion at the active site(s).
Kinetic and spectroscopic studies on the quercetin 2,3-dioxygenase from Bacillus subtilis.
Model systems for the CO-releasing flavonol 2,4-dioxygenase enzyme
This enzyme from Bacillus is homologous to the counterpart enzyme from Aspergillus (fungi) (D00842 in EzCatDB), although it has been thought to use iron as a native cofactor unlike the homologous enzyme, which adopts copper as a cofactor (see [6]). However, according to the literature [7], [8] and [9], this enzyme may use manganese or copper as a cofactor. Thus, Cu2+, and Mn2+ were included as cofactor in this entry. Moreover, this enzyme is homologous to Oxalate oxidase 1 (EC=1.2.3.4, S00145 in EzCatDB) and homogentisate 1,2-dioxygenase (HGO), according to the literature [1] and [2]. This enzyme is composed of two similar domains with catalytic sites. However, it is not clear whether both the sites are used as catalytic site or only either of the site is used.