Biochemical and crystallographic studies of l,d-transpeptidase 2 from Mycobacterium tuberculosis with its natural monomer substrate

Autor: Mariska de Munnik, Pauline A. Lang, Karina Calvopiña, Patrick Rabe, Jürgen Brem, Christopher J. Schofield

Publikováno v: Communications Biology, Vol 7, Iss 1, Pp 1-11 (2024)

Abstract The essential l,d-transpeptidase of Mycobacterium tuberculosis (LdtMt2) catalyses the formation of 3 $$\to$$ → 3 cross-links in cell wall peptidoglycan and is a target for development of antituberculosis therapeutics. Efforts to inhibit Ld

Externí odkaz: https://doaj.org/article/1e73630de0924f099b634058bd952bf2

Non‐Hydrolytic β‐Lactam Antibiotic Fragmentation by l,d‐Transpeptidases and Serine β‐Lactamase Cysteine Variants

Autor: Christopher T. Lohans, H. T. Henry Chan, Tika R. Malla, Kiran Kumar, Jos J. A. G. Kamps, Darius J. B. McArdle, Emma van Groesen, Mariska de Munnik, Catherine L. Tooke, James Spencer, Robert S. Paton, Jürgen Brem, Christopher J. Schofield

Publikováno v: Angewandte Chemie International Edition, 131(7), 2012-2016
Angewandte Chemie (International Ed. in English)
Lohans, C T, Chan, H T H, Malla, T R, Kumar, K, Kamps, J J A G, McArdle, D J B, van Groesen, E, de Munnik, M, Tooke, C L, Spencer, J, Paton, R S, Brem, J & Schofield, C J 2019, ' Non-Hydrolytic β-Lactam Antibiotic Fragmentation by l,d-Transpeptidases and Serine β-Lactamase Cysteine Variants ', Angewandte Chemie-International Edition, vol. 58, no. 7, pp. 1990-1994 . https://doi.org/10.1002/anie.201809424

Enzymes often use nucleophilic serine, threonine, and cysteine residues to achieve the same type of reaction; the underlying reasons for this are not understood. While bacterial d,d‐transpeptidases (penicillin‐binding proteins) employ a nucleophi

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e5833a70a8db9f9e937d333f0c3ad1a6
https://ora.ox.ac.uk/objects/uuid:1c5ee022-e6a5-4f45-8f03-1291de0d874b