Probing the Dimeric Structure of Porcine Aminoacylase 1 by Mass Spectrometric and Modeling Procedures

摘要: Aminoacylase 1 is a zinc-binding metalloprotease catalyzing the hydrolysis of Nα-acylated l-amino acids; it presents altered expression levels in different renal and small cell lung carcinomas. A description its redox oligomerization state was achieved by combined biochemical mass spectrometric procedures. topological analysis enzyme structural architecture derived from limited proteolysis selective chemical modification experiments, using broad range proteases reagents. The reaction products techniques identified 26 amino acids as being accessible on molecular surface, defining polypeptide regions exposed structure dimeric protein. nature intermolecular contact zone between monomers investigated cross-linking mapping experiments. cross-linked dimer isolated, peptides were characterized, thus demonstrating spatia...