Transpeptidase
DD-transpeptidase
| N° EC | EC |
|---|---|
| N° CAS |
| IUBMB | Entrée IUBMB |
|---|---|
| IntEnz | Vue IntEnz |
| BRENDA | Entrée BRENDA |
| KEGG | Entrée KEGG |
| MetaCyc | Voie métabolique |
| PRIAM | Profil |
| PDB | RCSB PDB PDBe PDBj PDBsum |
| GO | AmiGO / EGO |
La transpeptidase est une hydrolase qui catalyse l'hydrolyse des liaisons peptidiques présentant préférentiellement la configuration (Ac)2–L-Lys–D-Ala┼D-Ala. Il s'agit d'une enzyme bactérienne responsable de la réticulation du peptidoglycane pour former une paroi cellulaire rigide.
Les pénicillines sont des inhibiteurs de la transpeptidase, raison pour laquelle la famille d'antibiotiques apparentés — dits antibiotiques β-lactame — sont efficaces principalement contre des bactéries à Gram positif.
Notes et références
- (en) Jean-Marie Ghuysen, Jean-Marie Frère, Mélina Leyh-Bouille, Martine Nguyen-Distèche, Jacques Coyette, Jean Dusart, Bernard Joris, Colette Duez, Otto Dideberg, Paulette Charlier, Georges Dive et Josette Lamotte-Brasseur, « Bacterial wall peptidoglycan, DD-peptidases and beta-lactam antibiotics », Scandinavian Journal of Infectious Diseases. Supplementum, vol. 42, , p. 17-37 (PMID 6597561)
- (en) Jean Marie Frère, Bernard Joris et Gerald D. Shockman, « Penicillin-Sensitive Enzymes in Peptidoglycan Biosynthesis », Critical Reviews in Microbiology, vol. 11, no 4, , p. 299-396 (PMID 3888533, DOI 10.3109/10408418409105906, lire en ligne)
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