Literature for peptidase M15.021: Ply500 L-Ala-D-Glu peptidase

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

2012
1. Payne,K.M. and Hatfull,G.F.
   Mycobacteriophage endolysins: diverse and modular enzymes with multiple catalytic activities
   PLoS ONE7, e34052-e34052. PubMed  Europe PubMed DOI  V
2008
2. Korndorfer,I.P., Kanitz,A., Danzer,J., Zimmer,M., Loessner,M.J. and Skerra,A.
   Structural analysis of the L-alanoyl-D-glutamate endopeptidase domain of Listeria bacteriophage endolysin Ply500 reveals a new member of the LAS peptidase family
   Acta Crystallogr D Biol Crystallogr64, 644-650. PubMed  Europe PubMed DOI  S
2006
3. Korndorfer,I.P., Danzer,J., Schmelcher,M., Zimmer,M., Skerra,A. and Loessner,M.J.
   The crystal structure of the bacteriophage PSA endolysin reveals a unique fold responsible for specific recognition of Listeria cell walls
   J Mol Biol364, 678-689. PubMed  Europe PubMed DOI  S
1995
4. Loessner,M.J., Wendlinger,G. and Scherer,S.
   Heterogeneous endolysins in Listeria monocytogenes bacteriophages: a new class of enzymes and evidence for conserved holin genes within the siphoviral lysis cassettes
   Mol Microbiol16, 1231-1241. PubMed  Europe PubMed DOI