The 5S Subunit of Transcarboxylase Interacts with Free Biotin as Studied by Transferred-NOESY and Saturation Transfer Difference NMR

Title: The 5S Subunit of Transcarboxylase Interacts with Free Biotin as Studied by Transferred-NOESY and Saturation Transfer Difference NMR

Volume: 15 Issue: 6

Author(s): Rakesh Kumar Bhat and Stefan Berger

Affiliation:

Keywords: methylmalonyl CoA, Propionibacterium shermanii, NMR titration, STD amplification factor, Biotin Protons

Abstract: The 5S subunit of transcarboxylase was expressed and purified. Recent methods of NMR spectroscopy as transferred NOESY, INPHARMA and Saturation Transfer Difference (STD) NMR were used to investigate ligand binding of free biotin to the 5S protein. The binding epitope for biotin is very similar to that obtained at the 12S subunit of transcarboxylase, however no common binding site for pyruvate and biotin exists.

Cite this article as:

Bhat Kumar Rakesh and Berger Stefan, The 5S Subunit of Transcarboxylase Interacts with Free Biotin as Studied by Transferred-NOESY and Saturation Transfer Difference NMR, Protein & Peptide Letters 2008; 15 (6) . https://dx.doi.org/10.2174/092986608784966886

DOI https://dx.doi.org/10.2174/092986608784966886	Print ISSN 0929-8665
Publisher Name Bentham Science Publisher	Online ISSN 1875-5305