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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

Tobias Werther, Agnes Zimmer, Georg Wille, Ralph Golbik, Manfred S Weiss, Stephan König

FEBS J. 2010 Jun;277(12):2628-40.

PMID: 20553497

Abstract:

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.

Chemicals Related in the Paper:

Catalog Number	Product Name	Structure	CAS Number	Price
AS271844	Acetyl norfentanyl-13C6 oxalate solution			Price

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