The Enzyme Database

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Accepted name: pitrilysin
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 insulin and glucagon
Other name(s): Escherichia coli protease III; protease Pi; proteinase Pi; PTR; Escherichia coli metalloproteinase Pi
Comments: From the periplasmic space of Escherichia coli. Inhibited by EDTA and 1,10-phenanthroline; not thiol-dependent. Type example of peptidase family M16
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, MEROPS, PDB, CAS registry number: 81611-78-1
1.  Finch, P.W., Wilson, R.E., Brown, K., Hickson, I.D. and Emmerson, P.T. Complete nucleotide sequence of the Escherichia coli ptr gene encoding protease III. Nucleic Acids Res. 14 (1986) 7695–7703. [DOI] [PMID: 3534791]
2.  Affholter, J.A., Fried, V.A. and Roth, R.A. Human insulin-degrading enzyme shares structural and functional homologies with E. coli protease III. Science 242 (1988) 1415–1418. [DOI] [PMID: 3059494]
3.  Becker, A.B. and Roth, R.A. An unusual active site identified in a family of zinc metalloendopeptidases. Proc. Natl. Acad. Sci. USA 89 (1992) 3835–3839. [DOI] [PMID: 1570301]
4.  Ding, L., Becker, A.B., Suzuki, A. and Roth, R.A. Comparison of the enzymatic and biochemical properties of human insulin-degrading enzyme and Escherichia coli protease III. J. Biol. Chem. 267 (1992) 2414–2420. [PMID: 1733942]
5.  Anastasi, A., Knight, C.G. and Barrett, A.J. Characterization of the bacterial metalloendopeptidase pitrilysin by use of a continuous fluorescence assay. Biochem. J. 290 (1993) 601–607. [PMID: 7680857]
[EC created 1992 as EC, transferred 1993 to EC (EC created 1992, incorporated 1993)]

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