DD-transpeptidase
DD-Transpeptidase (, DD-peptidase, DD-transpeptidase, DD-carboxypeptidase, D-alanyl-D-alanine carboxypeptidase, D-alanyl-D-alanine-cleaving-peptidase, D-alanine carboxypeptidase, D-alanyl carboxypeptidase, and serine-type D-Ala-D-Ala carboxypeptidase.) is a bacterial enzyme that catalyzes the transfer of the R-L-αα-D-alanyl moiety of R-L-αα-D-alanyl-D-alanine carbonyl donors to the γ-OH of their active-site serine and from this to a final acceptor. It is involved in bacterial cell wall biosynthesis, namely, the transpeptidation that crosslinks the peptide side chains of peptidoglycan strands.
Key facts
- Enzyme.Name
- Serine-type D-Ala-D-Ala carboxypeptidase
- Enzyme.EC_number
- 3.4.16.4
- Enzyme.CAS_number
- 9077-67-2
- Enzyme.image
- DD-Transpeptidase.png
- Enzyme.caption
- Structure of the streptomyces K15 DD-transpeptidase
via Wikipedia infobox
Research
25 papers- A mechanism-based inhibitor targeting the DD-transpeptidase activity of bacterial penicillin-binding proteins.Journal of the American Chemical Society · 2003
- Catalytic mechanism of the Streptomyces K15 DD-transpeptidase/penicillin-binding protein probed by site-directed mutagenesis and structural analysis.Biochemistry · 2003
- Secretion by overexpression and purification of the water-soluble Streptomyces K15 DD-transpeptidase/penicillin-binding protein.The Biochemical journal · 1992
Article
7 sectionsContents
- Mechanism
- Structure
- Biological Function
- Disease Relevance
- See also
- References
- External links
DD-Transpeptidase (, DD-peptidase, DD-transpeptidase, DD-carboxypeptidase, D-alanyl-D-alanine carboxypeptidase, D-alanyl-D-alanine-cleaving-peptidase, D-alanine carboxypeptidase, D-alanyl carboxypeptidase, and serine-type D-Ala-D-Ala carboxypeptidase.) is a bacterial enzyme that catalyzes the transfer of the R-L-αα-D-alanyl moiety of R-L-αα-D-alanyl-D-alanine carbonyl donors to the γ-OH of their active-site serine and from this to a final acceptor. It is involved in bacterial cell wall biosynthesis, namely, the transpeptidation that crosslinks the peptide side chains of peptidoglycan strands.
The antibiotic penicillin irreversibly binds to and inhibits the activity of the transpeptidase enzyme by forming a highly stable penicilloyl-enzyme intermediate. Because of the interaction between penicillin and transpeptidase, this enzyme is also known as penicillin-binding protein (PBP).