Interaction of yeast 3-phosphoglycerate kinase with negatively charged carriers.
The aim of this study was to investigate the possibility of an interaction of yeast 3-phosphoglycerate kinase with negatively charged carriers such as polyanionic agents or a polarized electrode. Various polyanions were found to promote enzyme aggregation as judged by ultracentrifugation measurements and chemical modification. The data obtained suggest that these interactions are mediated through the N-terminal domain of the protein. However, the most striking property of 3-phosphoglycerate kinase described here is concerned with its significant dipolar moment as evidenced by electrocapillary measurements, which allows an orientation of the macromolecule in an electric field. Further, the enzyme could be absorbed by a negatively charged surface, first by hydrophobic links and then oriented perpendicularly to the surface. Therefore, the intrinsic properties of yeast 3-phosphoglycerate kinase agree with the formation of an enzyme-membrane complex and afford the ability for a specific orientation of the molecule at the lipid bilayer surface or in the cytoplasm.
D002809:Chondroitin Sulfates / Q000494:pharmacology; D004228:Dithionitrobenzoic Acid / Q000494:pharmacology*; D004355:Drug Stability; D009579:Nitrobenzoates / Q000494:pharmacology*; D009994:Osmolar Concentration; D010735:Phosphoglycerate Kinase / Q000378:metabolism*; D011099:Polyglutamic Acid / Q000494:pharmacology; D011122:Polyphosphates / Q000494:pharmacology; D011145:Polyvinyls / Q000494:pharmacology; D012441:Saccharomyces cerevisiae / Q000201:enzymology*; D013329:Structure-Activity Relationship
D009579:Nitrobenzoates; D011122:Polyphosphates; D011145:Polyvinyls; C019050:polyvinyl sulfate; D011099:Polyglutamic Acid; D002809:Chondroitin Sulfates; D004228:Dithionitrobenzoic Acid; D010735:Phosphoglycerate Kinase