Pitrilysin

Pitrilysin
Identifiers
EC number 3.4.24.55
CAS number 81611-78-1
Databases
IntEnz IntEnz view
BRENDA BRENDA entry
ExPASy NiceZyme view
KEGG KEGG entry
MetaCyc metabolic pathway
PRIAM profile
PDB structures RCSB 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. ↑ Finch PW, Wilson RE, Brown K, Hickson ID, Emmerson PT (October 1986). "Complete nucleotide sequence of the Escherichia coli ptr gene encoding protease III". Nucleic Acids Research. 14 (19): 7695–703. doi:10.1093/nar/14.19.7695. PMC 311789. PMID 3534791.
  2. ↑ Affholter JA, Fried VA, Roth RA (December 1988). "Human insulin-degrading enzyme shares structural and functional homologies with E. coli protease III". Science. 242 (4884): 1415–8. doi:10.1126/science.3059494. PMID 3059494.
  3. ↑ Becker AB, Roth RA (May 1992). "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. doi:10.1073/pnas.89.9.3835. PMC 525585. PMID 1570301.
  4. ↑ Ding L, Becker AB, Suzuki A, Roth RA (February 1992). "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. PMID 1733942.
  5. ↑ Anastasi A, Knight CG, Barrett AJ (March 1993). "Characterization of the bacterial metalloendopeptidase pitrilysin by use of a continuous fluorescence assay". The Biochemical Journal. 290 ( Pt 2): 601–7. doi:10.1042/bj2900601. PMC 1132317. PMID 7680857.
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