Role of lysine residues in the binding of glyceraldehyde-3-phosphate dehydrogenase to human erythrocyte membranes.
Glyceraldehyde-3-phosphate dehydrogenase (EC 1.2.1.12) binds reversibly to human erythrocyte membranes. Several specific amino acid residues involved in the enzyme-membrane contact region have already been identified. These include tyrosine 46 and threonine 150. Covalent modification of lysines 212 and 191 with pyridoxal phosphate results in a decreased affinity of the enzyme for erythrocyte membranes if the enzyme-linked pyridoxal phosphate is not reduced prior to binding. Reduction of the pyridoxal phosphate-lysine complex completely inhibits the binding of the enzyme to erythrocyte membranes. These results suggest a role for lysines 212 and 191 in the interaction of glyceraldehyde-3-phosphate with human erythrocyte membranes.
D000818:Animals; D001894:Borohydrides / Q000378:metabolism; D004910:Erythrocyte Membrane / Q000378:metabolism*; D005987:Glyceraldehyde-3-Phosphate Dehydrogenases / Q000097:blood*; D006801:Humans; D008239:Lysine / Q000378:metabolism*; D011732:Pyridoxal Phosphate / Q000378:metabolism; D011817:Rabbits; D013552:Swine
D001894:Borohydrides; D011732:Pyridoxal Phosphate; C025364:sodium borohydride; D005987:Glyceraldehyde-3-Phosphate Dehydrogenases; D008239:Lysine