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
Search PMC articles PubMed articles NCBI proteins

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

External links

• Pitrilysin at the US National Library of Medicine Medical Subject Headings (MeSH)