Article
Characterization of Glu350 as a critical residue involved in the N-terminal amine binding site of aminopeptidase N (EC 3.4.11.2): insights into its mechanism of action.
Biochemistry - 13 Jan 1998
Luciani N, Marie-Claire C, Ruffet E, Beaumont A, Roques B P, Fournié-Zaluski M C
Abstract excerpt
The molecular components ensuring the strict exopeptidase action of aminopeptidase N (APN) and related zinc aminopeptidases of the M1 family have not yet been clearly established. The specific recognition of the N-terminal amino acid of the substrates by the enzymes has been proposed to involve either the complexation of the free amino group by the catalytic zinc ion or an interaction with an anionic binding...
Topics
- Amino Acid Sequence
- Animals
- Binding Sites
- CD13 Antigens
- COS Cells
- Exopeptidases
- Glutamic Acid
- Models, Chemical
- Molecular Sequence Data
- Mutagenesis, Site-Directed
- Mutation
- Peptide Hydrolases
- Protease Inhibitors
- Protein Binding