DD-transpeptidase
Sign in to saveAlso known as D-alanyl-D-alanine carboxypeptidase, D-alanyl-D-alanine-cleaving peptidase, D-alanyl-D-alanine-carboxypeptidase, DD-peptidase, D-alanyl-D-alanine-cleaving-peptidase, D-alanyl carboxypeptidase, 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
- Streptomyces K15 active-site serine DD-transpeptidase: specificity profile for peptide, thiol ester and ester carbonyl donors and pathways of the transfer reactions.The Biochemical journal · 1995
- The crystal structure of a penicilloyl-serine transferase of intermediate penicillin sensitivity. The DD-transpeptidase of streptomyces K15.The Journal of biological chemistry · 1999
via PubMed
Wikidata facts
- Image
- DD-Transpeptidase.png
- Said to be same as
- penicillin binding proteins
Show 1 more fact
- EC enzyme number
- 3.4.16.4
Sources (1)
via Wikidata · CC0
~6 min read
Encyclopedic overview
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).
Excerpted from Wikipedia’s “DD-transpeptidase” article, available under the CC BY-SA 4.0 licence.