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Cited by 348

The DOI matches its Crossref record; 198 of the 198 references it cites were found in a registry or an index.

Cell Wall Hydrolases in Bacteria: Insight on the Diversity of Cell Wall Amidases, Glycosidases and Peptidases Toward Peptidoglycan

Open access
Vermassen, Aurore, Leroy, Sabine, Talon, Régine, Provot, Christian, Popowska, Magdalena, Desvaux, Mickaël·2019·Frontiers in Microbiology
DOI 10.3389/fmicb.2019.00331
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Abstract

The cell wall (CW) of bacteria is an intricate arrangement of macromolecules, at least constituted of peptidoglycan (PG) but also of (lipo)teichoic acids, various polysaccharides, polyglutamate and/or proteins. During bacterial growth and division, there is a constant balance between CW degradation and biosynthesis. The CW is remodeled by bacterial hydrolases, whose activities are carefully regulated to maintain cell integrity or lead to bacterial death. Each cell wall hydrolase (CWH) has a specific role regarding the PG: (i) cell wall amidase (CWA) cleaves the amide bond between N-acetylmuramic acid and L-alanine residue at the N-terminal of the stem peptide, (ii) cell wall glycosidase (CWG) catalyses the hydrolysis of the glycosidic linkages, whereas (iii) cell wall peptidase (CWP) cleaves amide bonds between amino acids within the PG chain. After an exhaustive overview of all known conserved catalytic domains responsible for CWA, CWG, and CWP activities, this review stresses that the CWHs frequently display a modular architecture combining multiple and/or different catalytic domains, including some lytic transglycosylases as well as CW binding domains. From there, direct physiological and collateral roles of CWHs in bacterial cells are further discussed.

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Metadata

Authors
Vermassen, A., Leroy, S., Talon, R., Provot, C., Popowska, M., & Desvaux, M.
Venue
Frontiers in Microbiology
Publisher
Frontiers Media SA
Published
2019-02-28
Volume
10
Pages
331-331
ISSN
1664-302X (ISSN-L)
DOI
10.3389/fmicb.2019.00331
OpenAlex
W2920691960
Cited by
348
References
198
FWCI
23.43
Type
journal article
Language
en
Open access
gold

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