DD-Transpeptidase

DD-Transpeptidase (<a href="/facts/Enzyme_Commission_number/Y5GNLRKX">EC</a> <a href="https://enzyme.expasy.org/EC/3.4.16.4">3.4.16.4</a>, DD-peptidase, DD-transpeptidase, DD-carboxypeptidase, D-alanyl-D-alanine <a href="/facts/Carboxypeptidase/RmQNzvCR">carboxypeptidase</a>, 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 <a href="/facts/Moiety_(chemistry)/WxKqcJe1">moiety</a> 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 <a href="/facts/Antibiotic/sF1kIfxg">antibiotic</a> <a href="/facts/Penicillin/Abo8VQ3p">penicillin</a> 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 <a href="/facts/Penicillin-binding_protein/NHUFDpy2">penicillin-binding protein</a> (PBP).

DD-Transpeptidase open-in-new

DD-Transpeptidase