Site for the dioxygen ligand that is thought to mediate the formation In the structure is consistent with the previously published V/ K IE data and provides an empty coordination The вЂњend-onвЂќ conformation of oxalate observed О”E162 OxDC variant, in which Glu 162 has been deletedДЇrom the active site loop, reveals the likely mode by which the substrateД¬oordinates the catalytically active Mn ion prior to CвЂ“C bondД¬leavage. Structure of a complex between oxalate and the Co(II)-substituted Increased level of access of the solvent to the active site duringД¬atalysis, implying that the functional role of Glu 162 is Observed oxidase activity of the DASN OxDC variant arises from an Taken together, these results raise the possibility that the Residues does not modulate the chemistry of the enzyme-bound Mn(II) Via the same mechanism as in the wild-type enzyme, even though the

Show that CвЂ“C bond cleavage in the DASN OxDC variant proceeds Of the DASN OxDC variant is associated with only a small fraction Of the reaction stoichiometry as a function of oxalate concentration,ДЄs determined by MIMS, suggests that the increased oxidase activity (MIMS) and isotope effect (IE) measurements. In activity has now been investigated using membrane inlet mass spectrometry

Oxalate oxidase gives a chimeric variant (DASN) that exhibits significantly The cognate residues Asp 161-Ala 162-Ser- 163-Asn 164 of an evolutionarily related, Mn-dependent Previous studies have shown that replacingДЄn active-site loop segment Ser 161-Glu 162-Asn 163-Ser 164 in the N-terminal domain of OxDC with Into formate and carbon dioxide in a remarkable reaction that requires Decarboxylase (OxDC) catalyzes the conversion of oxalate

Oxalate complex ion bonding