Trypsin

Trypsin
Identifiers
EC no.3.4.21.4
CAS no.9002-07-7
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum
Gene OntologyAmiGO / QuickGO
Search
PMCarticles
PubMedarticles
NCBIproteins
Trypsin
Identifiers
SymbolTrypsin
PfamPF00089
InterProIPR001254
SMARTSM00020
PROSITEPDOC00124
MEROPSS1
SCOP21c2g / SCOPe / SUPFAM
CDDcd00190
Available protein structures:
Pfam  structures / ECOD  
PDBRCSB PDB; PDBe; PDBj
PDBsumstructure summary

Trypsin is an enzyme in the first section of the small intestine that starts the digestion of protein molecules by cutting long chains of amino acids into smaller pieces. It is a serine protease from the PA clan superfamily, found in the digestive system of many vertebrates, where it hydrolyzes proteins.[2][3] Trypsin is formed in the small intestine when its proenzyme form, the trypsinogen produced by the pancreas, is activated. Trypsin cuts peptide chains mainly at the carboxyl side of the amino acids lysine or arginine. It is used for numerous biotechnological processes. The process is commonly referred to as trypsinogen proteolysis or trypsinization, and proteins that have been digested/treated with trypsin are said to have been trypsinized.[4]

Trypsin was discovered in 1876 by Wilhelm Kühne.[5] Although many sources say that Kühne named trypsin from the Ancient Greek word for rubbing, 'tripsis', because the enzyme was first isolated by rubbing the pancreas with glass powder and alcohol, in fact Kühne named trypsin from the Ancient Greek word 'thrýpto' which means 'I break' or 'I break apart'.[6]

  1. ^ PDB: 1UTN​; Leiros HK, Brandsdal BO, Andersen OA, Os V, Leiros I, Helland R, et al. (April 2004). "Trypsin specificity as elucidated by LIE calculations, X-ray structures, and association constant measurements". Protein Science. 13 (4): 1056–70. doi:10.1110/ps.03498604. PMC 2280040. PMID 15044735.
  2. ^ Rawlings ND, Barrett AJ (1994). "[2] Families of serine peptidases". Families of serine peptidases. Methods in Enzymology. Vol. 244. pp. 19–61. doi:10.1016/0076-6879(94)44004-2. ISBN 978-0-12-182145-6. PMC 7133253. PMID 7845208.
  3. ^ The German physiologist Wilhelm Kühne (1837-1900) discovered trypsin in 1876. See: Kühne W (1877). "Über das Trypsin (Enzym des Pankreas)". Verhandlungen des Naturhistorisch-medicinischen Vereins zu Heidelberg. new series. 1 (3): 194–198 – via Google Books.Open access icon
  4. ^ Engelking LR (2015-01-01). "Chapter 7 - Protein Digestion". Textbook of Veterinary Physiological Chemistry (Third ed.). Boston: Academic Press. pp. 39–44. doi:10.1016/B978-0-12-391909-0.50007-4. ISBN 978-0-12-391909-0.
  5. ^ Kühne W (March 6, 1876). "Ueber das Trypsin (Enzym des Pankreas)" [About trypsin (enzyme of the pancreas)]. In Naturhistorisch-medizinischen Verein (ed.). Verhandlungen des Naturhistorisch-medizinischen Vereins zu Heidelberg [Negotiations by the Natural History Medical Association in Heidelberg] (in German). Heidelberg, Germany: Carl Winter's Universitätsbuchhandlung (published 1877). pp. 194–8 – via Archive.org.
  6. ^ Girolami GS (2024). "Origin and Likely Etymology of the Word 'Trypsin'". Bull. Hist. Chem. 49 (1): 59–60.

Developed by StudentB