Effect of red cell membrane binding on the catalytic activity of glyceraldehyde-3-phosphate dehydrogenase.
Band 3, the anion transport protein of the human erythrocyte, provides the site of association of certain glycolytic enzymes with the membrane. We have now demonstrated that glyceraldehyde-3-P dehydrogenase is inhibited, reversibly and completely, when membrane bound. The inhibition was competitive with respect to NAD+ and arsenate, but was noncompetitive with glyceraldehyde-3-P. Peptide fragments containing the NH2-terminal 23 residues of band 3 also inhibited the enzyme and displaced it from ghosts. Thus, the red cell membrane binding site for glyceraldehyde-3-P dehydrogenase is the same as that for aldolase, the polyanionic NH2-terminal region of the band 3 polypeptide.
D001457:Anion Exchange Protein 1, Erythrocyte; D000838:Anions; D001798:Blood Proteins / Q000378:metabolism*; D004910:Erythrocyte Membrane / Q000378:metabolism*; D004912:Erythrocytes / Q000378:metabolism*; D005987:Glyceraldehyde-3-Phosphate Dehydrogenases / Q000097:blood*; D006801:Humans; D007700:Kinetics; D009994:Osmolar Concentration; D011485:Protein Binding
D001457:Anion Exchange Protein 1, Erythrocyte; D000838:Anions; D001798:Blood Proteins; D005987:Glyceraldehyde-3-Phosphate Dehydrogenases