Nuclear-magnetic-resonance study of the active-site structure of yeast phosphoglycerate kinase.
The enzyme 3-phosphoglycerate kinase from yeast has been studied by observation of the proton nuclear magnetic resonance spectrum at 270 MHz using Fourier transform techniques. Difference spectroscopy was used to enhance the resolution and to identify specific ligand binding effects and conformational changes. Perturbations involving single protons of amino-acid residues could thus be detected despite the relatively high molecular weight of the protein (47000), particularly in the aromatic (6-9 ppm) and methylene (2-3 ppm) regions of the spectrum.
D000244:Adenosine Diphosphate; D000255:Adenosine Triphosphate; D001665:Binding Sites; D006863:Hydrogen-Ion Concentration; D007811:Lanthanum; D008274:Magnesium; D009682:Magnetic Resonance Spectroscopy; D008345:Manganese; D010735:Phosphoglycerate Kinase; D011485:Protein Binding; D011487:Protein Conformation; D012441:Saccharomyces cerevisiae / Q000201:enzymology*
D008345:Manganese; D000244:Adenosine Diphosphate; D007811:Lanthanum; D000255:Adenosine Triphosphate; D010735:Phosphoglycerate Kinase; D008274:Magnesium