Biology:Pitrilysin

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Pitrilysin
Identifiers
EC number3.4.24.55
CAS number81611-78-1
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum

Pitrilysin (EC 3.4.24.55, Escherichia coli protease III, protease Pi, proteinase Pi, PTR, Escherichia coli metalloproteinase Pi) is an enzyme.[1][2][3][4][5] This enzyme catalyses the following chemical reaction:

Preferential cleavage of -Tyr16- Leu- and -Phe25- Tyr-bonds of oxidized insulin B chain. Also acts on other substrates of less than 7 kDa such as glucagon

This enzyme is present in bacteria Escherichia coli.

References

  1. "Complete nucleotide sequence of the Escherichia coli ptr gene encoding protease III". Nucleic Acids Research 14 (19): 7695–703. October 1986. doi:10.1093/nar/14.19.7695. PMID 3534791. 
  2. "Human insulin-degrading enzyme shares structural and functional homologies with E. coli protease III". Science 242 (4884): 1415–8. December 1988. doi:10.1126/science.3059494. PMID 3059494. Bibcode1988Sci...242.1415A. 
  3. "An unusual active site identified in a family of zinc metalloendopeptidases". Proceedings of the National Academy of Sciences of the United States of America 89 (9): 3835–9. May 1992. doi:10.1073/pnas.89.9.3835. PMID 1570301. Bibcode1992PNAS...89.3835B. 
  4. "Comparison of the enzymatic and biochemical properties of human insulin-degrading enzyme and Escherichia coli protease III". The Journal of Biological Chemistry 267 (4): 2414–20. February 1992. doi:10.1016/S0021-9258(18)45895-4. PMID 1733942. 
  5. "Characterization of the bacterial metalloendopeptidase pitrilysin by use of a continuous fluorescence assay". The Biochemical Journal 290 ( Pt 2) (2): 601–7. March 1993. doi:10.1042/bj2900601. PMID 7680857. 

External links