Literature for peptidase C51.001: D-alanyl-glycyl peptidase (staphylococcal phage phi11-type)

Summary Alignment Tree Sequences Sequence features Distribution Literature Substrates

(Topics flags: S Structure, E Expression, U Therapeutic. To select only the references relevant to a single topic, click the link above. See explanation.)

    2020
  1. Rahimzadeh,G., Gill,P. and Rezai,M.S.
    Cysteine/histidine-dependent amidohydrolase/peptidase (CHAP)-displayed nano phages: antimicrobial function against methicillin-resistant Staphylococcus aureus (MRSA)
    Avicenna J Med Biotechnol12, 85-90. PubMed  Europe PubMed
  2. 2017
  3. Hathaway,H., Ajuebor,J., Stephens,L., Coffey,A., Potter,U., Sutton,J.M. and Jenkins,A.T.
    Thermally triggered release of the bacteriophage endolysin CHAPK and the bacteriocin lysostaphin for the control of methicillin resistant Staphylococcus aureus (MRSA)
    J Control Release245, 108-115. PubMed  Europe PubMed DOI  U
  4. 2016
  5. Filatova,L.Y., Donovan,D.M., Ishnazarova,N.T., Foster-Frey,J.A., Becker,S.C., Pugachev,V.G., Balabushevich,N.G., Dmitrieva,N.F. and Klyachko,N.L.
    A chimeric LysK-lysostaphin fusion enzyme lysing Staphylococcus aureus cells: a study of both kinetics of inactivation and specifics of interaction with anionic polymers
    Appl Biochem Biotechnol180, 544-557. PubMed  Europe PubMed DOI
  6. Hosseini,E.S., Moniri,R., Goli,Y.D. and Kashani,H.H.
    Purification of antibacterial CHAPK protein using a self-cleaving fusion tag and its activity against methicillin-resistant Staphylococcus aureus
    Probiotics Antimicrob Proteins8, 202-210. PubMed  Europe PubMed DOI
  7. Keary,R., Sanz-Gaitero,M., van Raaij,M.J., O'Mahony,J., Fenton,M., McAuliffe,O., Hill,C., Ross,R.P. and Coffey,A.
    Characterization of a bacteriophage-derived murein peptidase for elimination of antibiotic-resistant Staphylococcus aureus
    Curr Protein Pept Sci17, 183-190. PubMed  Europe PubMed DOI  S
  8. 2015
  9. Kashani,H.H. and Moniri,R.
    Expression of recombinant pET22b-LysK-cysteine/histidine-dependent amidohydrolase/peptidase bacteriophage therapeutic protein in Escherichia coli BL21 (DE3)
    Osong Public Health Res Perspect6, 256-260. PubMed  Europe PubMed DOI  E
  10. 2014
  11. Gu,J., Feng,Y., Feng,X., Sun,C., Lei,L., Ding,W., Niu,F., Jiao,L., Yang,M., Li,Y., Liu,X., Song,J., Cui,Z., Han,D., Du,C., Yang,Y., Ouyang,S., Liu,Z.J. and Han,W.
    Structural and biochemical characterization reveals LysGH15 as an unprecedented "EF-hand-like" calcium-binding phage lysin
    PLoS Pathog10, e1004109-e1004109. PubMed  Europe PubMed DOI  S
  12. Sanz-Gaitero,M., Keary,R., Garcia-Doval,C., Coffey,A. and van Raaij,M.J.
    Crystal structure of the lytic CHAP(K) domain of the endolysin LysK from Staphylococcus aureus bacteriophage K
    Virol J11, 133-133. PubMed  Europe PubMed DOI  S
  13. Standish,A.J., Whittall,J.J. and Morona,R.
    Tyrosine phosphorylation enhances activity of pneumococcal autolysin LytA
    Microbiology (Reading, Engl )160, 2745-2754. PubMed  Europe PubMed DOI
  14. 2013
  15. Fenton,M., Keary,R., McAuliffe,O., Ross,R.P., O'Mahony,J. and Coffey,A.
    Bacteriophage-derived peptidase CHAP(K) eliminates and prevents staphylococcal biofilms
    Int J Microbiol2013, 625341-625341. PubMed  Europe PubMed DOI
  16. Sanz-Gaitero,M., Keary,R., Garcia-Doval,C., Coffey,A. and van Raaij,M.J.
    Crystallization of the CHAP domain of the endolysin from Staphylococcus aureus bacteriophage K
    Acta Crystallogr Sect F Struct Biol Cryst Commun69, 1393-1396. PubMed  Europe PubMed DOI
  17. 2010
  18. Fenton,M., Casey,P.G., Hill,C., Gahan,C.G., Ross,R.P., McAuliffe,O., O'Mahony,J., Maher,F. and Coffey,A.
    The truncated phage lysin CHAP(k) eliminates Staphylococcus aureus in the nares of mice
    Bioeng Bugs1, 404-407. PubMed  Europe PubMed DOI  U
  19. 2009
  20. Becker,S.C., Dong,S., Baker,J.R., Foster-Frey,J., Pritchard,D.G. and Donovan,D.M.
    LysK CHAP endopeptidase domain is required for lysis of live staphylococcal cells
    FEMS Microbiol Lett294, 52-60. PubMed  Europe PubMed DOI
  21. Horgan,M., O'Flynn,G., Garry,J., Cooney,J., Coffey,A., Fitzgerald,G.F., Ross,R.P. and McAuliffe,O.
    Phage lysin LysK can be truncated to its CHAP domain and retain lytic activity against live antibiotic-resistant staphylococci
    Appl Environ Microbiol75, 872-874. PubMed  Europe PubMed DOI
  22. 2008
  23. Becker,S.C., Foster-Frey,J. and Donovan,D.M.
    The phage K lytic enzyme LysK and lysostaphin act synergistically to kill MRSA
    FEMS Microbiol Lett287, 185-191. PubMed  Europe PubMed DOI
  24. 2005
  25. O'Flaherty,S., Coffey,A., Meaney,W., Fitzgerald,G.F. and Ross,R.P.
    The recombinant phage lysin LysK has a broad spectrum of lytic activity against clinically relevant staphylococci, including methicillin-resistant Staphylococcus aureus
    J Bacteriol187, 7161-7164. PubMed  Europe PubMed DOI
  26. 2003
  27. Bateman,A. and Rawlings,N.D.
    The CHAP domain: a large family of amidases including GSP amidase and peptidoglycan hydrolases
    Trends Biochem Sci28, 234-237. PubMed  Europe PubMed DOI
  28. Rigden,D.J., Jedrzejas,M.J. and Galperin,M.Y.
    Amidase domains from bacterial and phage autolysins define a family of gamma-D,L-glutamate-specific amidohydrolases
    Trends Biochem Sci28, 230-234. PubMed  Europe PubMed DOI
  29. 1999
  30. [YEAR:28-5-1999]Navarre,W.W., Ton-That,H., Faull,K.F. and Schneewind,O.
    Multiple enzymatic activities of the murein hydrolase from staphylococcal phage phi11. Identification of a D-alanyl-glycine endopeptidase activity
    J Biol Chem274, 15847-15856. PubMed  Europe PubMed DOI
  31. 1998
  32. [YEAR:30-10-1998]Navarre,W.W., Ton-That,H., Faull,K.F. and Schneewind,O.
    Anchor structure of staphylococcal surface proteins. II. COOH-terminal structure of muramidase and amidase-solubilized surface protein
    J Biol Chem273, 29135-29142. PubMed  Europe PubMed DOI
  33. 1991
  34. Wang,X., Wilkinson,B.J. and Jayaswal,R.K.
    Sequence analysis of a Staphylococcus aureus gene encoding a peptidoglycan hydrolase activity
    Gene102, 105-109. PubMed  Europe PubMed DOI