Issue 12, 2004
From the journal:

Organic & Biomolecular Chemistry

Determination of the binding specificity of the 12S subunit of the transcarboxylase by saturation transfer difference NMR

Claudia Peikert,a   Karsten Seeger,a   Rakesh Kumar Bhata  and  Stefan Berger*a  

* Corresponding authors

a Institute of Analytical Chemistry, University of Leipzig, Linnéstr. 3, D-04103 Leipzig, Germany
E-mail: stberger@rz.uni-leipzig.de
Fax: +49 341 9711833

Abstract

In this study we present the characterization of the interaction of biotin and methylmalonyl-CoA (MMCoA) with the carboxyltransferase subunit (12S) from the transcarboxylase (TC) from Propionibacterium shermanii. This biotin dependent multienzyme complex catalyses the transfer of carbon dioxide from methylmalonyl-CoA (MMCoA) to pyruvate. The Saturation Transfer Difference NMR (STD) technique was performed to determine the binding epitope from biotin and MMCoA to the 12S subunit. We could show by titrations during STD experiments that biotin and MMCoA bind cooperatively in one binding pocket.

Graphical abstract: Determination of the binding specificity of the 12S subunit of the transcarboxylase by saturation transfer difference NMR

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Article information

DOI
https://doi.org/10.1039/B404238G
Article type
Paper
Submitted
19 Mar 2004
Accepted
27 Apr 2004
First published
20 May 2004

Org. Biomol. Chem., 2004,2, 1777-1781

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Determination of the binding specificity of the 12S subunit of the transcarboxylase by saturation transfer difference NMR

C. Peikert, K. Seeger, R. K. Bhat and S. Berger, Org. Biomol. Chem., 2004, 2, 1777 DOI: 10.1039/B404238G

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