The MSMEG_1586 of M. smegmatis Is a Penicillin-Interactive Enzyme That Can Potentially Hydrolyse Aztreonam and Cephalosporins
Author:
Funder
Albert David Limited, IN
Department of Biotechnology, Ministry of Science and Technology, India
Publisher
Springer Science and Business Media LLC
Subject
Applied Microbiology and Biotechnology,General Medicine,Microbiology
Link
https://link.springer.com/content/pdf/10.1007/s00284-023-03545-0.pdf
Reference24 articles.
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2. De Jager V, Gupte N, Nunes S, Barnes GL, van Wijk RC, Mostert J, Dorman SE, Abulfathi AA, Upton CM, Faraj A, Nuermberger EL, Lamichhane G, Svensson EM, Simonsson USH, Diacon AH, Dooley KE, Team CS (2022) Early bactericidal activity of meropenem plus clavulanate (with or without rifampin) for tuberculosis the COMRADE randomized, phase 2A clinical trial. Am J Resp Crit Care 205(10):1228–1235. https://doi.org/10.1164/rccm.202108-1976OC
3. Pandey SD, Pal S, Kumar NG, Bansal A, Mallick S, Ghosh AS (2018) Two DD-carboxypeptidases from mycobacterium smegmatis affect cell surface properties through regulation of peptidoglycan cross-linking and glycopeptidolipids. J Bacteriol 200(14):e00760-17. https://doi.org/10.1128/JB.00760-17
4. Ghosh AS, Chowdhury C, Nelson DE (2008) Physiological functions of D-alanine carboxypeptidases in Escherichia coli. Trends Microbiol 16(7):309–317. https://doi.org/10.1016/j.tim.2008.04.006
5. Mizoguchi A, Hitomi S (2019) Cefotaxime-non-susceptibility of Haemophilus influenzae induced by additional amino acid substitutions of G555E and Y557H in altered penicillin-binding protein 3. J Infect Chemother 25(7):509–513. https://doi.org/10.1016/j.jiac.2019.02.010
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