{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,9,26]],"date-time":"2026-09-26T22:34:10Z","timestamp":1790462050784,"version":"4.1.0"},"reference-count":42,"publisher":"Microbiology Society","issue":"6","funder":[{"name":"Department of Biotechnology, Government of India","award":["BT\/PR24255\/NER\/95\/716\/2017"],"award-info":[{"award-number":["BT\/PR24255\/NER\/95\/716\/2017"]}]}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":[],"published-print":{"date-parts":[[2020,6,1]]},"abstract":"\n Mycobacterial peptidoglycan (PG) is an unsolved puzzle due to its complex structure and involvement of multiple enzymes in the process of its remodelling.\n dd<\/jats:sc>\n -Carboxypeptidases are low molecular mass penicillin-binding proteins (LMM-PBPs) that catalyzes the cleavage of terminal\n d<\/jats:sc>\n -Ala of muramyl pentapeptide branches and thereby helps in the PG remodelling process. Here, we have assigned the function of a putative LMM-PBP, MSMEG_2432 of\n \n \n Mycobacterium smegmatis<\/jats:ext-link>\n <\/jats:named-content>\n <\/jats:italic>\n , by showing that it exhibits both\n dd<\/jats:sc>\n -CPase and \u03b2-lactamase activities. Like conventional\n dd<\/jats:sc>\n -CPase (PBP5 from\n E. coli<\/jats:italic>\n ), upon ectopic complementation in a deformed seven PBP deletion mutant of\n E. coli<\/jats:italic>\n , MSMEG_2432 has manifested its ability to restore ~75\u200a% of the cell population to their normal rod shape. Further,\n in vitro<\/jats:italic>\n dd<\/jats:sc>\n -CPase assay has confirmed its ability to release terminal\n d<\/jats:sc>\n -Ala from the synthetic tripeptide and the peptidoglycan mimetic pentapeptide substrates ending with\n d<\/jats:sc>\n -Ala-\n d<\/jats:sc>\n -Ala. Also, elevated resistance against penicillins and cephalosporins upon ectopic expression of MSMEG_2432 suggests the presence of \u03b2-lactamase activity, which is further confirmed\n in vitro<\/jats:italic>\n through nitrocefin hydrolysis assay. Moreover, it is found apparent that D169A substitution in MSMEG_2432 influences both of its\n in vivo<\/jats:italic>\n and\n in vitro<\/jats:italic>\n dd<\/jats:sc>\n -CPase and \u03b2-lactamase activities. Thus, we infer that MSMEG_2432 is a dual function enzyme that possesses both\n dd<\/jats:sc>\n -CPase and \u03b2-lactamase activities.\n <\/jats:p>","DOI":"10.1099\/mic.0.000902","type":"journal-article","created":{"date-parts":[[2020,4,17]],"date-time":"2020-04-17T12:25:06Z","timestamp":1587126306000},"page":"546-553","source":"Crossref","is-referenced-by-count":9,"title":["MSMEG_2432 of Mycobacterium smegmatis mc2155 is a dual function enzyme that exhibits DD-carboxypeptidase and \u03b2-lactamase activities"],"prefix":"10.1099","volume":"166","author":[{"ORCID":"https:\/\/orcid.org\/0000-0002-4923-1913","authenticated-orcid":false,"given":"Satya Deo","family":"Pandey","sequence":"first","affiliation":[{"name":"University of Kansas Medical Center, USA"},{"name":"Department of Biotechnology, Indian Institute of Technology, Kharagpur, West Bengal PIN-721302, 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