Structural characterization of EnpA D,L-Endopeptidase from Enterococcus faecalis prophage provides insights into substrate specificity of M23 peptidases

Małecki, P.H., Mitkowski, P., Jagielska, E. et al. (3 more authors) (2021) Structural characterization of EnpA D,L-Endopeptidase from Enterococcus faecalis prophage provides insights into substrate specificity of M23 peptidases. International Journal of Molecular Sciences, 22 (13). 7136.

Abstract

Metadata

Authors/Creators:
  • Małecki, P.H.
  • Mitkowski, P.
  • Jagielska, E.
  • Trochimiak, K.
  • Mesnage, S.
  • Sabała, I.
Copyright, Publisher and Additional Information: © 2021 The Authors. Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (https://creativecommons.org/licenses/by/4.0/).
Keywords: Enterococcus faecalis; M23 peptidase; endopeptidase; peptidoglycan hydrolase; Amino Acid Sequence; Bacterial Proteins; Catalytic Domain; Endopeptidases; Enterococcus faecalis; N-Acetylmuramoyl-L-alanine Amidase; Peptide Hydrolases; Peptidoglycan; Prophages; Protein Binding; Staphylococcus; Staphylococcus aureus; Substrate Specificity
Dates:
  • Accepted: 29 June 2021
  • Published (online): 1 July 2021
  • Published: 1 July 2021
Institution: The University of Sheffield
Academic Units: The University of Sheffield > Faculty of Science (Sheffield) > School of Biological Sciences (Sheffield) > Department of Molecular Biology and Biotechnology (Sheffield)
Depositing User: Symplectic Sheffield
Date Deposited: 20 Aug 2021 07:10
Last Modified: 20 Aug 2021 07:49
Status: Published
Publisher: MDPI AG
Refereed: Yes
Identification Number: https://doi.org/10.3390/ijms22137136
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