The 5S subunit of transcarboxylase interacts with free biotin as studied by transferred-NOESY and Saturation Transfer Difference NMR.
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.
Bhat
Rakesh Kumar
RK
Institute of Analytical Chemistry, University of Leipzig, Linnéstr. 3, D-04103 Leipzig, Germany.
Berger
Stefan
S
D001426:Bacterial Proteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism; D001665:Binding Sites; D001710:Biotin / Q000737:chemistry / Q000378:metabolism*; D019878:Carboxyl and Carbamoyl Transferases / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D009682:Magnetic Resonance Spectroscopy / Q000379:methods*; D015394:Molecular Structure; D011424:Propionibacterium / Q000201:enzymology; D011485:Protein Binding; D021122:Protein Subunits / Q000737:chemistry / Q000378:metabolism; D011994:Recombinant Proteins / Q000737:chemistry / Q000378:metabolism
D001426:Bacterial Proteins; D021122:Protein Subunits; D011994:Recombinant Proteins; D001710:Biotin; D019878:Carboxyl and Carbamoyl Transferases; C021580:Methylmalonyl-CoA carboxytransferase