Structure of l-aminopeptidase d-ala-esterase/amidase from ochrobactrum anthropi, a prototype for the serine aminopeptidases, reveals a new variant among the ntn hydrolase fold
The L-aminopeptidase D-Ala-esterase/amidase from Ochrobactrum anthropi (DmpA) is an aminopeptidase which catalyses the release of N-terminal residues from peptides substrates. It also shows D-amidasic and D-esterasic activities on D-alanine derivatives. DmpA and other ¦Â-aminopeptidases are able to to cleave synthetic ¦Â-peptides, which consist of backbone-elongated ¦Â-amino acid residues that are not processed by common proteolytic enzymes. ¦Â-peptides are considered promising building blocks for the design of novel peptidomimetics,small protein-like chains to mimic peptides which are useful for drug design, thus these enzymes that cleave and release them are useful for production of peptidominetics.
Defined by 5 residues: TYR:A-146ASN:A-218SER:A-250SER:A-288GLY:A-289