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Serine-type D-Ala-D-Ala carboxypeptidase : 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

抄文引用元・出典: フリー百科事典『 ウィキペディア(Wikipedia)
ウィキペディアで「DD-transpeptidase」の詳細全文を読む



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