Evidence for the proximity of a cysteine and a lysine residue in the active site of 6-phosphogluconate dehydrogenase from Candida utilis.
The environment of a cysteine residue in the active site of 6-phosphogluconate dehydrogenase from Candida utilis was investigated by means of N-(3-pyrene) maleimide. The reaction between enzyme and inhibitor results in the modification of one cysteine residue per enzyme subunit, and in the complete inactivation of the enzyme. In a second step, the epsilon-amino group of a lysine residue causes an intramolecular aminolysis of the bound inhibitor. These results indicate that a lysine and a cysteine residues are close in the three-dimensional structure of the active site of 6-phosphogluconate dehydrogenase.
D000595:Amino Acid Sequence; D001665:Binding Sites; D002175:Candida / Q000201:enzymology*; D003545:Cysteine / Q000032:analysis*; D007700:Kinetics; D008239:Lysine / Q000032:analysis*; D010734:Phosphogluconate Dehydrogenase / Q000378:metabolism*; D013050:Spectrometry, Fluorescence
D010734:Phosphogluconate Dehydrogenase; D008239:Lysine; D003545:Cysteine