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Literature summary extracted from

  • Silvaggi, N.R.; Josephine, H.R.; Kuzin, A.P.; Nagarajan, R.; Pratt, R.F.; Kelly, J.A.
    Crystal structures of complexes between the R61 DD-peptidase and peptidoglycan-mimetic beta-lactams: a non-covalent complex with a "perfect penicillin" (2005), J. Mol. Biol., 345, 521-533.
    View publication on PubMed

Application

EC Number Application Comment Organism
3.4.16.4 medicine clinical defense against bacterial infections, DD-peptidases are the killing targets of beta-lactams Streptomyces sp. R61

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
3.4.16.4 by hanging-drop, vapor-diffusion method, to 1.5 A resolution, X-ray structure of non-covalent and covalent complexes of beta-lactams with DD-peptidase Streptomyces sp. R61

Inhibitors

EC Number Inhibitors Comment Organism Structure
3.4.16.4 benzylpenicillin classical non-specific beta-lactam Streptomyces sp. R61
3.4.16.4 cephalosporin with glycyl-L-alpha-amino-epsilon-pimelyl side-chain, this beta lactam might be a better antibiotic than a non-specific counterpart Streptomyces sp. R61
3.4.16.4 cephalosporin C classical non-specific beta-lactam Streptomyces sp. R61
3.4.16.4 penicillin having the glycyl-L-alpha-amino-epsilon-pimelyl side-chain of Streptomyces strain R61 peptidoglycan, this beta lactam might be the perfect antibiotic as compared to a non-specific counterpart Streptomyces sp. R61

Organism

EC Number Organism UniProt Comment Textmining
3.4.16.4 Streptomyces sp. R61 P15555
-
-

Synonyms

EC Number Synonyms Comment Organism
3.4.16.4 D-alanyl-D-alanine-transpeptidase
-
 Streptomyces sp. R61
3.4.16.4 DD-peptidase
-
 Streptomyces sp. R61