
lysostaphin과 LytM은 S. aureus 펩티도글리칸의 D-Ala-Gly 교차결합 부위를 선호적으로 가수분해한다.


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Orchestrated action of peptidoglycan (PG) synthetases and hydrolases is vital for bacterial growth and viability. Although the function of several PG synthetases and hydrolases is well-understood, the function, regulation, and mechanism of action of PG hydrolases characterized as lysostaphin-like endopeptidases have remained elusive. Many of these M23 family members can hydrolyse glycyl-glycine peptide bonds and show lytic activity against Staphylococcus aureus whose PG contains a pentaglycine bridge, but their exact substrate specificity and hydrolysed bonds are still vaguely determined.

In this work, we have employed NMR spectroscopy to study both the substrate specificity and the bond cleavage of the bactericide lysostaphin and the S. aureus PG hydrolase LytM. Yet, we provide substrate-level evidence for the functional role of these enzymes. Indeed, our results show that the substrate specificities of these structurally highly homologous enzymes are similar, but unlike observed earlier both LytM and lysostaphin prefer the D-Ala-Gly cross-linked part of mature peptidoglycan. However, we show that while lysostaphin is genuinely a glycyl-glycine hydrolase, LytM can also act as a D-alanyl-glycine endopeptidase.

### Competing Interest Statement

The authors have declared no competing interest.

Reassessing the substrate specificities of the major Staphylococcus aureus peptidoglycan hydrolases lysostaphin and LytM

s-aureus-펩티도글리칸-가수분해효소-lysostaphin과-lytm의-기질-특이성-재평가


S. aureus 펩티도글리칸 가수분해효소 lysostaphin과 LytM의 기질 특이성 재평가
