Enzyme classes:
General information:
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EC 3.4 Peptidases - hydrolases that hydrolyse peptide bonds
EC 3.4 subclass definition The EC 3.4 subclass contains peptidases - hydrolases that hydrolyse peptide bonds. Further classification is based on the type of peptide bond and polypeptide sequence around peptide bond. Further classification of EC 3.4 subclass This classification is based on type of ether bond. - EC 3.4.1 - α-Amino-Acyl-Peptide Hydrolases, obsolete, reclassified now as EC 3.4.11
- EC 3.4.2 - Peptidyl-Amino-Acid Hydrolases, obsolete, reclassified now as EC 3.4.17
- EC 3.4.3 - Dipeptide Hydrolases, obsolete, reclassified now as EC 3.4.13
- EC 3.4.4 - Peptidyl Peptide Hydrolases, obsolete, reclassified now as EC 3.4.14, EC 3.4.21, EC 3.4.22, EC 3.4.23 and EC 3.4.24
- EC 3.4.11 - Aminopeptidases - catalyze the cleavage of one amino acid residue from the N-terminus of protein or peptide.
- EC 3.4.12 - Acylamino-Acid Hydrolases or Peptidylamino-Acid Hydrolases, obsolete, reclassified now as EC 3.4.16, EC 3.4.17 and EC 3.4.19
- EC 3.4.13 - Dipeptidases - catalyze the cleavage of two amino acid peptide.
- EC 3.4.14 - Dipeptidyl- and tripeptidyl-peptidases - catalyze the cleavage of N-terminal two- or tri-peptide from a polypeptide chain.
- EC 3.4.15 - Peptidyl-dipeptidases - catalyze the cleavage of C-terminal two-peptide from a polypeptide chain.
- EC 3.4.16 - Serine-type carboxypeptidases - catalyze the cleavage of C-terminal amino acid residue from a polypeptide chain.
- EC 3.4.17 - Metallocarboxypeptidases - catalyze the cleavage of C-terminal amino acid residue from a polypeptide chain.
- EC 3.4.18 - Cysteine-type carboxypeptidases - catalyze the cleavage of C-terminal amino acid residue from a polypeptide chain.
- EC 3.4.19 - Omega peptidases - catalyze the cleavage of substituted, cyclized or linked by isopeptide bonds terminal amino acid residue from a polypeptide chain.
- EC 3.4.21 - Serine endopeptidases - catalyze the internal cleavage in polypeptide chains
- EC 3.4.22 - Cysteine endopeptidases - catalyze the internal cleavage in polypeptide chains
- EC 3.4.23 - Aspartic endopeptidases - catalyze the internal cleavage in polypeptide chains
- EC 3.4.24 - Metalloendopeptidases - catalyze the internal cleavage in polypeptide chains
- EC 3.4.25 - Threonine endopeptidases - catalyze the internal cleavage in polypeptide chains
- EC 3.4.99 - Endopeptidases with unknown mechanisms - catalyze the internal cleavage in polypeptide chains
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