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Serine protease
Class of enzymes / From Wikipedia, the free encyclopedia
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Serine proteases (or serine endopeptidases) are enzymes that cleave peptide bonds in proteins. Serine serves as the nucleophilic amino acid at the (enzyme's) active site.[1] They are found ubiquitously in both eukaryotes and prokaryotes. Serine proteases fall into two broad categories based on their structure: chymotrypsin-like (trypsin-like) or subtilisin-like.[2]
Quick Facts Identifiers, EC no. ...
Serine protease | |||||||||
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![]() Crystal structure of bovine chymotrypsin. The catalytic residues are shown as yellow sticks. Rendered from PDB 1CBW. | |||||||||
Identifiers | |||||||||
EC no. | 3.4.21.- | ||||||||
Databases | |||||||||
IntEnz | IntEnz view | ||||||||
BRENDA | BRENDA entry | ||||||||
ExPASy | NiceZyme view | ||||||||
KEGG | KEGG entry | ||||||||
MetaCyc | metabolic pathway | ||||||||
PRIAM | profile | ||||||||
PDB structures | RCSB PDB PDBe PDBsum | ||||||||
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