Characterization of active site variants of xanthine hydroxylase from Aspergillus nidulans.

doi:10.1016/j.abb.2007.11.002

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Article

Characterization of active site variants of xanthine hydroxylase from Aspergillus nidulans.

Archives of biochemistry and biophysics - 1 Feb 2008

Li Meng, Müller Tina A, Fraser Bruce A, Hausinger Robert P

Abstract excerpt

Xanthine/alpha-ketoglutarate (alphaKG) dioxygenase (XanA) is a non-heme mononuclear Fe(II) enzyme that decarboxylates alphaKG to succinate and CO(2) while hydroxylating xanthine to generate uric acid. In the absence of a XanA crystal structure, a homology model was used to target several putative active site residues for mutagenesis. Wild-type XanA and ten enzyme variants were purified from recombinant...

Topics

Aspergillus nidulans
Dioxygenases
Enzyme Activation
Fungal Proteins
Genetic Variation
Isoenzymes
Mutagenesis, Site-Directed
Structure-Activity Relationship

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Identifiers

PMID: 18036331
DOI: 10.1016/j.abb.2007.11.002
PMCID: PMC2258140

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