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

Rakesh   Kumar   Bhat; Stefan      Berger

doi:10.2174/092986608784966886

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.

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

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Protein & Peptide Letters

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

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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.

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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