Structure of human aspartyl aminopeptidase complexed with substrate analogue: insight into catalytic mechanism, substrate specificity and M18 peptidase family.
Chaikuad, A., Pilka, E.S., Riso, A.D., Delft, F.V., Kavanagh, K.L., Venien-Bryan, C., Oppermann, U., Yue, W.W.(2012) BMC Struct Biol 12: 14-14
- PubMed: 22720794 
- DOI: https://doi.org/10.1186/1472-6807-12-14
- Primary Citation of Related Structures:  
4DYO - PubMed Abstract: 
Aspartyl aminopeptidase (DNPEP), with specificity towards an acidic amino acid at the N-terminus, is the only mammalian member among the poorly understood M18 peptidases. DNPEP has implicated roles in protein and peptide metabolism, as well as the renin-angiotensin system in blood pressure regulation. Despite previous enzyme and substrate characterization, structural details of DNPEP regarding ligand recognition and catalytic mechanism remain to be delineated.
Organizational Affiliation: 
Structural Genomics Consortium, Old Road Research Campus Building, Oxford OX3 7DQ, UK.