Abstract:
:Oxalate oxidase (E.C. 1.2.3.4) catalyzes the oxygen-dependent oxidation of oxalate to carbon dioxide in a reaction that is coupled with the formation of hydrogen peroxide. Although there is currently no structural information available for oxalate oxidase from Ceriporiopsis subvermispora (CsOxOx), sequence data and homology modeling indicate that it is the first manganese-containing bicupin enzyme identified that catalyzes this reaction. Interestingly, CsOxOx shares greatest sequence homology with bicupin microbial oxalate decarboxylases (OxDC). We show that CsOxOx activity directly correlates with Mn content and other metals do not appear to be able to support catalysis. EPR spectra indicate that the Mn is present as Mn(II), and are consistent with the coordination environment expected from homology modeling with known X-ray crystal structures of OxDC from Bacillus subtilis. EPR spin-trapping experiments support the existence of an oxalate-derived radical species formed during turnover. Acetate and a number of other small molecule carboxylic acids are competitive inhibitors for oxalate in the CsOxOx catalyzed reaction. The pH dependence of this reaction suggests that the dominant contribution to catalysis comes from the monoprotonated form of oxalate binding to a form of the enzyme in which an active site carboxylic acid residue must be unprotonated.
journal_name
Arch Biochem Biophysjournal_title
Archives of biochemistry and biophysicsauthors
Moussatche P,Angerhofer A,Imaram W,Hoffer E,Uberto K,Brooks C,Bruce C,Sledge D,Richards NG,Moomaw EWdoi
10.1016/j.abb.2011.02.022subject
Has Abstractpub_date
2011-05-01 00:00:00pages
100-7issue
1eissn
0003-9861issn
1096-0384pii
S0003-9861(11)00086-5journal_volume
509pub_type
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