Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 3.4.16.4 extracted from

  • Diaz, N.; Sordo, T.L.; Suarez, D.
    Insights into the base catalysis exerted by the DD-transpeptidase from Streptomyces K15: A molecular dynamics study (2005), Biochemistry, 44, 3225 - 3240.
    View publication on PubMed

Crystallization (Commentary)

Crystallization (Comment) Organism
X-ray structure, the energetically most stable configuration has a neutral Lys213 residue, the K15 active site is characterized by a dense hydrogen-bonding network that interconnects the catalytically relevant residues and some solvent molecules, the hydroxyl group of the nucleophilic serine (Ser35) is located in the oxy-anion-hole formed by the backbone NH groups of Ser35 and Ser216 Streptomyces sp.

Inhibitors

Inhibitors Comment Organism Structure
benzylpenicillin
-
Streptomyces sp.

Organism

Organism UniProt Comment Textmining
Streptomyces sp.
-
-
-

Synonyms

Synonyms Comment Organism
DD-transpeptidase
-
Streptomyces sp.
penicillin-binding protein
-
Streptomyces sp.