Determination of oxalyl-coenzyme A decarboxylase activity in Oxalobacter formigenes and Lactobacillus acidophilus by capillary electrophoresis

Bendazzoli, Claudia; Turroni, Silvia; Gotti, Roberto; Olmo, Stefano; Brigidi, Patrizia; Cavrini, Vanni

doi:10.1016/j.jchromb.2007.04.027

Cited by 5 publications

(1 citation statement)

References 24 publications

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“…Previous kinetic studies on ODCs were performed either discontinuously by monitoring the decarboxylation of oxalyl CoA to formyl CoA by HPLC and capillary electrophoresis, respectively [17,18], or continuously by using two auxiliary enzymes, formate dehydrogenase and formyl CoA transferase [2]. Here, a kinetic assay was established to directly monitor changes in the UV absorbance of the substrate oxalyl CoA during catalysis.…”

Section: Resultsmentioning

confidence: 99%

New insights into structure–function relationships of oxalyl CoA decarboxylase from Escherichia coli

et al. 2010

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DatabaseStructural data for holo-EcODC (ThDP-EcODC) in the absence of additional ligands and in complex with either ADP or acetyl CoA have been submitted to the Protein Data Bank under the accession numbers 2q27, 2q28 and 2q29, respectively. The gene yfdU from Escherichia coli encodes a putative oxalyl coenzyme A decarboxylase, a thiamine diphosphate-dependent enzyme that is potentially involved in the degradation of oxalate. The enzyme has been purified to homogeneity. The kinetic constants for conversion of the substrate oxalyl coenzyme A by the enzyme in the absence and presence of the inhibitor coenzyme A, as well as in the absence and presence of the activator adenosine 5¢-diphosphate, were determined using a novel continuous optical assay. The effects of these ligands on the solution and crystal structure of the enzyme were studied using small-angle X-ray scattering and X-ray crystal diffraction. Analyses of the obtained crystal structures of the enzyme in complex with the cofactor thiamine diphosphate, the activator adenosine 5¢-diphosphate and the inhibitor acetyl coenzyme A, as well as the corresponding solution scattering patterns, allow comparison of the oligomer structures of the enzyme complexes under various experimental conditions, and provide insights into the architecture of substrate and effector binding sites. Abbreviations EcODC, oxalyl CoA decarboxylase from Escherichia coli; OfODC, oxalyl CoA decarboxylase from Oxalobacter formigenes; PADP, 3¢-phosphoadenosine 5¢-diphosphate; ThDP, thiamine diphosphate.

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Section: Resultsmentioning

confidence: 99%

New insights into structure–function relationships of oxalyl CoA decarboxylase from Escherichia coli

et al. 2010

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Advances in-capillary electrophoretic enzyme assays

Scriba

2010

Journal of Pharmaceutical and Biomedical Analysis

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New insights into structure-function relationships of oxalyl CoA decarboxylase from Escherichia coli

et al. 2010

View full text Add to dashboard Cite

The gene yfdU from Escherichia coli encodes a putative oxalyl coenzyme A decarboxylase, a thiamine diphosphate-dependent enzyme that is potentially involved in the degradation of oxalate. The enzyme has been purified to homogeneity. The kinetic constants for conversion of the substrate oxalyl coenzyme A by the enzyme in the absence and presence of the inhibitor coenzyme A, as well as in the absence and presence of the activator adenosine 5'-diphosphate, were determined using a novel continuous optical assay. The effects of these ligands on the solution and crystal structure of the enzyme were studied using small-angle X-ray scattering and X-ray crystal diffraction. Analyses of the obtained crystal structures of the enzyme in complex with the cofactor thiamine diphosphate, the activator adenosine 5'-diphosphate and the inhibitor acetyl coenzyme A, as well as the corresponding solution scattering patterns, allow comparison of the oligomer structures of the enzyme complexes under various experimental conditions, and provide insights into the architecture of substrate and effector binding sites.

show abstract

Determination of oxalyl-coenzyme A decarboxylase activity in Oxalobacter formigenes and Lactobacillus acidophilus by capillary electrophoresis

Cited by 5 publications

References 24 publications

New insights into structure–function relationships of oxalyl CoA decarboxylase from Escherichia coli

New insights into structure–function relationships of oxalyl CoA decarboxylase from Escherichia coli

Advances in-capillary electrophoretic enzyme assays

New insights into structure-function relationships of oxalyl CoA decarboxylase from Escherichia coli

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