Pitrilysin - Misplaced Pages

Pitrilysin (EC 3.4.24.55, Escherichia coli protease III, protease Pi, proteinase Pi, PTR, Escherichia coli metalloproteinase Pi) is an enzyme. This enzyme catalyses the following chemical reaction:

Preferential cleavage of -Tyr- Leu- and -Phe- 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

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.
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.
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.
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.
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.

External links

Pitrilysin at the U.S. National Library of Medicine Medical Subject Headings (MeSH)

v t e Proteases: metalloendopeptidases (EC 3.4.24)
ADAM proteins	Alpha secretases ADAM9 ADAM10 ADAM17 ADAM19 ADAM2 ADAM7 ADAM8 ADAM11 ADAM12 ADAM15 ADAM18 ADAM22 ADAM23 ADAM28 ADAM33 ADAMTS1 ADAMTS2 ADAMTS3 ADAMTS4 ADAMTS5 ADAMTS8 ADAMTS9 ADAMTS10 ADAMTS12 ADAMTS13
Matrix metalloproteinases	Collagenases MMP1 MMP8 Gelatinases MMP2 MMP9 MMP3 MMP7 MMP10 MMP11 MMP12 MMP13 MMP14 MMP15 MMP16 MMP17 MMP19 MMP20 MMP21 MMP23A MMP23B MMP24 MMP25 MMP26 MMP27 MMP28
Other	Neprilysin Procollagen peptidase Thermolysin Pregnancy-associated plasma protein A Bone morphogenetic protein 1 Lysostaphin Insulin-degrading enzyme ZMPSTE24

v t e Enzymes
Activity	Active site Binding site Catalytic triad Oxyanion hole Enzyme promiscuity Diffusion-limited enzyme Cofactor Enzyme catalysis
Regulation	Allosteric regulation Cooperativity Enzyme inhibitor Enzyme activator
Classification	EC number Enzyme superfamily Enzyme family List of enzymes
Kinetics	Enzyme kinetics Eadie–Hofstee diagram Hanes–Woolf plot Lineweaver–Burk plot Michaelis–Menten kinetics
Types	EC1 Oxidoreductases (list) EC2 Transferases (list) EC3 Hydrolases (list) EC4 Lyases (list) EC5 Isomerases (list) EC6 Ligases (list) EC7 Translocases (list)

Portal:

Biology

Category:

EC 3.4.24