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DD-transpeptidase : ウィキペディア英語版 | DD-transpeptidase
A 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''.〔(【引用サイトリンク】 work=Enzyme Structures Database )〕) is a bacterial enzyme that cross-links peptidoglycan chains to form rigid cell walls. 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). == See also ==
* Vancomycin, an antibiotic that binds the D-ala-D-ala residues, inhibiting elongation via glycosyltransferase
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