Pitrilysin

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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

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[edit]

  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. 

External links[edit]