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EC number
CAS number 81611-78-1
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Pitrilysin (EC, 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.


  1. ^ Finch, P.W.; Wilson, R.E.; Brown, K.; Hickson, I.D.; Emmerson, P.T. (1986). "Complete nucleotide sequence of the Escherichia coli ptr gene encoding protease III". Nucleic Acids Res. 14: 7695–7703. PMC 311789Freely accessible. PMID 3534791. doi:10.1093/nar/14.19.7695. 
  2. ^ Affholter, J.A.; Fried, V.A.; Roth, R.A. (1988). "Human insulin-degrading enzyme shares structural and functional homologies with E. coli protease III". Science. 242: 1415–1418. PMID 3059494. doi:10.1126/science.3059494. 
  3. ^ Becker, A.B.; Roth, R.A. (1992). "An unusual active site identified in a family of zinc metalloendopeptidases". Proc. Natl. Acad. Sci. USA. 89 (9): 3835–3839. PMC 525585Freely accessible. PMID 1570301. doi:10.1073/pnas.89.9.3835. 
  4. ^ Ding, L.; Becker, A.B.; Suzuki, A.; Roth, R.A. (1992). "Comparison of the enzymatic and biochemical properties of human insulin-degrading enzyme and Escherichia coli protease III". J. Biol. Chem. 267 (4): 2414–2420. PMID 1733942. 
  5. ^ Anastasi, A.; Knight, C.G.; Barrett, A.J. (1993). "Characterization of the bacterial metalloendopeptidase pitrilysin by use of a continuous fluorescence assay". Biochem. J. 290: 601–607. PMC 1132317Freely accessible. PMID 7680857. doi:10.1042/bj2900601. 

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