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Literature summary extracted from

  • Morlot, C.; Pernot, L.; Le Gouellec, A.; Di Guilmi, A.M.; Vernet, T.; Dideberg, O.; Dessen, A.
    Crystal structure of a peptidoglycan synthesis regulatory factor (PBP3) from Streptococcus pneumoniae (2005), J. Biol. Chem., 280, 15984-15991.
    View publication on PubMed

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
3.4.16.4 by hanging drop vapor diffusion, to 2.8 A resolution, PBP3 folds into an NH2-terminal,D,D-carboxypeptidase-like domain and a COOH-terminal, elongated beta-rich region Streptomyces pneumoniae

Inhibitors

EC Number Inhibitors Comment Organism Structure
3.4.16.4 (3H)benzylpenicillin
-
 Streptomyces pneumoniae
3.4.16.4 N,N-diacetyl-L-Lys-D-Ala-D-Ala inhibition of PBP3 by its own substrate above a ligand concentration of 15 mM Streptomyces pneumoniae
3.4.16.4 penicillin
-
 Streptomyces pneumoniae

Organism

EC Number Organism UniProt Comment Textmining
3.4.16.4 Streptomyces pneumoniae
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
3.4.16.4
-
 Streptomyces pneumoniae

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.4.16.4 N,N'-diacetyl-L-Lys-D-Ala-D-Ala + H2O
-
 Streptomyces pneumoniae ?
-
 ?

Subunits

EC Number Subunits Comment Organism
3.4.16.4 monomer multiwavelength anomalous diffraction Streptomyces pneumoniae

Synonyms

EC Number Synonyms Comment Organism
3.4.16.4 D-Ala-D-Ala(D,D) carboxypeptidase
-
 Streptomyces pneumoniae
3.4.16.4 PBP3
-
 Streptomyces pneumoniae
3.4.16.4 penicillin-binding protein
-
 Streptomyces pneumoniae