EC 3.4.24.55 - Pitrilysin

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IntEnz Enzyme Nomenclature
EC 3.4.24.55

Names

Accepted name:
pitrilysin
Other names:
Escherichia coli metalloproteinase Pi
Escherichia coli protease III
PTR
protease Pi
proteinase Pi
Systematic name:

Reaction

Cofactor

Comments:

From the periplasmic space of Escherichia coli. Inhibited by EDTA and 1,10-phenanthroline; not thiol-dependent. Formerly EC 3.4.99.44. Type example of peptidase family M16.

Links to other databases

Enzymes and pathways: NC-IUBMB , BRENDA , ExplorEnz , ENZYME@ExPASy , KEGG , MetaCyc , MEROPS , UniPathway
Protein domains and families: PROSITE:PDOC00130
Structural data: CSA , EC2PDB
Gene Ontology: GO:0008975
CAS Registry Number: 81611-78-1
UniProtKB/Swiss-Prot:

References

  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: 7695-7703 (1986). [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: 1415-1418 (1988). [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: 3835-3839 (1992). [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: 2414-2420 (1992). [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: 601-607 (1993). [PMID: 7680857]

[EC 3.4.24.55 created 1992 as EC 3.4.99.44, transferred 1993 to EC 3.4.24.55 (EC 3.4.99.45 created 1992, incorporated 1993)]