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Catalysis of the hydrolysis of peptide bonds formed between L-amino acids. Catalysis of the hydrolysis of internal, alpha-peptide bonds in a polypeptide chain. Catalysis of the hydrolysis of internal, alpha-peptide bonds in a polypeptide chain by a catalytic mechanism that involves a catalytic triad consisting of a serine nucleophile that is activated by a proton relay involving an acidic residue (e.g. aspartate or glutamate) and a basic residue (usually histidine). Catalysis of the hydrolysis of peptide bonds in a polypeptide chain by a catalytic mechanism that involves a catalytic triad consisting of a serine nucleophile that is activated by a proton relay involving an acidic residue (e.g. aspartate or glutamate) and a basic residue (usually histidine). Catalysis of the hydrolysis of a substrate by a catalytic mechanism that involves a catalytic triad consisting of a serine nucleophile that is activated by a proton relay involving an acidic residue (e.g. aspartate or glutamate) and a basic residue (usually histidine).

View Gene Ontology (GO) Term

GO TERM SUMMARY
Name: serine-type endopeptidase activity
Acc: GO:0004252
Aspect: Molecular Function
Desc: Catalysis of the hydrolysis of internal, alpha-peptide bonds in a polypeptide chain by a catalytic mechanism that involves a catalytic triad consisting of a serine nucleophile that is activated by a proton relay involving an acidic residue (e.g. aspartate or glutamate) and a basic residue (usually histidine).
Synonyms:
  • blood coagulation factor activity
Proteins in PDR annotated with:
   This term: 987 [Search]
   Term or descendants: 987 [Search]


[geneontology.org]
INTERACTIVE GO GRAPH

GO:0004252 - serine-type endopeptidase activity (interactive image map)
YRC Informatics Platform - Version 3.0
Created and Maintained by: Michael Riffle