title: Chemical modification of lysine residues in bacterial formate dehydrogenase.
abstract: Specific modification of 4.4 lysine residues per molecule of formate dehydrogenase, from the methylotrophic bacterium Achromobacter parvulus I by pyridoxal, results in complete inactivation of the enzyme. The concentration effect of the modifying agent and substrates on the inactivation of formate dehydrogenase has been studied. Coenzymes do not protect the enzyme from inactivation. Complete maintenance of enzyme activity was achieved in the presence of saturating concentrations of the formate and upon formation of the ternary complex, enzyme-NAD-azide. Formate specifically protects two lysine residues per dimer molecule of the enzyme from modification. The presence of one essential lysine residue in the substrate-binding region of the enzyme active site is assumed.
mesh_terms: D000421:Alcaligenes / Q000201:enzymology*; D000445:Aldehyde Oxidoreductases / Q000378:metabolism*; D000596:Amino Acids / Q000032:analysis; D005560:Formate Dehydrogenases / Q000378:metabolism*; D007700:Kinetics; D008239:Lysine; D011730:Pyridoxal / Q000494:pharmacology; D013056:Spectrophotometry, Ultraviolet
chemical_list: D000596:Amino Acids; D011730:Pyridoxal; D005560:Formate Dehydrogenases; D000445:Aldehyde Oxidoreductases; D008239:Lysine