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Pitrilysin

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Pitrilysin
Identifiers
EC no.3.4.24.55
CAS no.81611-78-1
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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

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  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. Bibcode:1988Sci...242.1415A. 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. Bibcode:1992PNAS...89.3835B. 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. doi:10.1016/S0021-9258(18)45895-4. 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) (2): 601–7. doi:10.1042/bj2900601. PMC 1132317. PMID 7680857.
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