Structure-Based Dissection of the Active Site Chemistry of Leukotriene A4 Hydrolase: Implications for M1 Aminopeptidases and Inhibitor Design
M1 aminopeptidases comprise a large family of biologically important zinc enzymes. We show that peptide turnover by the M1 prototype, leukotriene A4 hydrolase/ aminopeptidase, involves a shift in substrate position associated with exchange of zinc coordinating groups,while maintaining the overall coordination geometry. The transition state is stabilized by residues conserved among M1 members and in […] Read full post »
Published on September 22, 2008
