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:Institute of Analytical Chemistry,University of Leipzig, Linnestr. 3, D-04103 Leipzig, Germany.
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.
