Catalysis of the hydrolysis of N-terminal amino acid residues from in a polypeptide chain [goid 4177] [pmid 11106490] [evidence IDA]; Catalysis of the hydrolysis of a peptide bond. A peptide bond is a covalent bond formed when the carbon atom from the carboxyl group of one amino acid shares electrons with the nitrogen atom from the amino group of a second amino acid [goid 8233] [evidence IEA]; Catalysis of the hydrolysis of a peptide bond not more than three residues from the N- or C-terminus of a polypeptide chain by a mechanism in which water acts as a nucleophile, one or two metal ions hold the water molecule in place, and charged amino acid side chains are ligands for the metal ions [goid 8235] [evidence IEA]; Interacting selectively with manganese (Mn) ions [goid 30145] [evidence IEA]; Interacting selectively with any metal ion [goid 46872] [evidence IEA]; Catalysis of the hydrolysis of N-terminal amino acid residues from in a polypeptide chain [goid 4177] [evidence IEA]; Catalysis of the hydrolysis of a peptide bond not more than three residues from the N- or C-terminus of a polypeptide chain by a mechanism in which water acts as a nucleophile, one or two metal ions hold the water molecule in place, and charged amino acid side chains are ligands for the metal ions [goid 8235] [evidence IEA]; Catalysis of the hydrolysis of various bonds, e.g. C-O, C-N, C-C, phosphoric anhydride bonds, etc. Hydrolase is the systematic name for any enzyme of EC class 3 [goid 16787] [evidence IEA]; Catalysis of the hydrolysis of N-terminal amino acid residues from in a polypeptide chain [goid 4177] [evidence IEA]; Catalysis of the hydrolysis of a peptide bond not more than three residues from the N- or C-terminus of a polypeptide chain by a mechanism in which water acts as a nucleophile, one or two metal ions hold the water molecule in place, and charged amino acid side chains are ligands for the metal ions [goid 8235] [evidence IEA]; Catalysis of the hydrolysis of N-terminal amino acid residues from in a polypeptide chain [goid 4177] [evidence IEA]; Catalysis of the hydrolysis of a peptide bond not more than three residues from the N- or C-terminus of a polypeptide chain by a mechanism in which water acts as a nucleophile, one or two metal ions hold the water molecule in place, and charged amino acid side chains are ligands for the metal ions [goid 8235] [evidence IEA]; Catalysis of the hydrolysis of various bonds, e.g. C-O, C-N, C-C, phosphoric anhydride bonds, etc. Hydrolase is the systematic name for any enzyme of EC class 3 [goid 16787] [evidence IEA]; Catalysis of the hydrolysis of N-terminal amino acid residues from in a polypeptide chain [goid 4177] [evidence IEA]; Catalysis of the hydrolysis of a peptide bond not more than three residues from the N- or C-terminus of a polypeptide chain by a mechanism in which water acts as a nucleophile, one or two metal ions hold the water molecule in place, and charged amino acid side chains are ligands for the metal ions [goid 8235] [evidence IEA]; Catalysis of the hydrolysis of N-terminal amino acid residues from in a polypeptide chain [goid 4177] [evidence IEA]; Catalysis of the hydrolysis of a peptide bond not more than three residues from the N- or C-terminus of a polypeptide chain by a mechanism in which water acts as a nucleophile, one or two metal ions hold the water molecule in place, and charged amino acid side chains are ligands for the metal ions [goid 8235] [evidence IEA]; Catalysis of the hydrolysis of N-terminal amino acid residues from in a polypeptide chain [goid 4177] [evidence IEA]; Catalysis of the hydrolysis of a peptide bond not more than three residues from the N- or C-terminus of a polypeptide chain by a mechanism in which water acts as a nucleophile, one or two metal ions hold the water molecule in place, and charged amino acid side chains are ligands for the metal ions [goid 8235] [evidence IEA]; Catalysis of the hydrolysis of various bonds, e.g. C-O, C-N, C-C, phosphoric anhydride bonds, etc. Hydrolase is the systematic name for any enzyme of EC class 3 [goid 16787] [evidence IEA]