![]() Birth & Early Lifeīorn on 1 January 2003 in the United States, Emma Bugg her career at a young age. Let’s now have a glimpse into the Early Life, Career, Personal Life and Body Measurements of the celebrated actress Emma Bugg. She has additionally been honoured with numerous awards throughout her career. These findings culminate 50 years of speculation and debate concerning the chlamydial anomaly and are the strongest evidence so far that chlamydial species possess functional PG.Emma Bugg is an American model and film star who has graced numerous films and captivated everyone through her magazine and advertisement photoshoots. Replicating Chlamydia trachomatis were labelled with these probes throughout their biphasic developmental life cycle, and the results of differential probe incorporation experiments conducted in the presence of ampicillin are consistent with the presence of chlamydial PG-modifying enzymes. We used a novel approach to metabolically label chlamydial PG using d-amino acid dipeptide probes and click chemistry. Chlamydia harbour genes for PG biosynthesis and exhibit susceptibility to 'anti-PG' antibiotics, yet attempts to detect PG in any chlamydial species have proven unsuccessful (the 'chlamydial anomaly'). Bacteria comprising the Chlamydiales were thought to be one of the few exceptions. Peptidoglycan (PG), an essential structure in the cell walls of the vast majority of bacteria, is critical for division and maintaining cell shape and hydrostatic pressure. Given the large number of Chlamydia species (as well as members of the Planctomycetes-Verrucomicrobiae-Chlamydiae superphylum) that possess DapF but lack homologues of MurI, it is likely that DapF is a primordial isomerase that functions as both racemase and epimerase in these organisms, suggesting that specialized D-glutamate racemase enzymes never evolved in these microbes. Enzyme promiscuity is thought to be the hallmark of early microbial life on this planet, and there is currently an active debate as to whether " moonlighting enzymes " represent primordial evolutionary relics or are a product of more recent reductionist evolutionary pressures. We have determined that the diaminopimelate epimerase (DapF) encoded by Chla-mydia trachomatis is capable of carrying out both the epimerization of DAP and the pyridoxal phosphate-dependent racemization of glutamate. IMPORTANCE Here we describe one of the last remaining " missing " steps in pepti-doglycan synthesis in pathogenic Chlamydia species, the synthesis of D-glutamate. Genetic complementation, enzymatic characterization, and bioinformatic analyses indicate that chlamydial DapF shares characteristics with other promiscuous/primordial enzymes, presenting a potential mechanism for D-glutamate synthesis not only in Chlamydia but also numerous other genera within the Planctomycetes-Verrucomicrobiae-Chlamydiae superphylum that lack recognized glutamate racemases. Biochemical analysis showed robust activity, but unlike canonical glutamate racemases, activity was dependent on the cofactor pyridoxal phosphate. Genetic complementation of an Escherichia coli murI mutant demonstrated that Chlamydia DapF can generate D-glutamate. DapF catalyzes the final step in the synthesis of meso-diaminopimelate, another amino acid unique to peptidoglycan. trachomatis synthesizes D-glutamate by utilizing a novel, bifunctional homologue of diaminopimelate epim-erase (DapF). ![]() trachomatis and confirmed that its pentapeptide includes D-glutamate. Recent studies have revealed the presence of peptidoglycan in C. While its genome encodes a majority of the enzymes involved in peptidoglycan synthesis, no murI homologue has ever been annotated. ![]() ![]() Chlamydia tra-chomatis is the leading cause of infectious blindness and sexually transmitted bacterial infections worldwide. In Gram-negative bacteria, D-glutamate is generated via the racemization of L-glutamate by glutamate racemase (MurI). D-Glutamate is present at the second position of the pentapeptide stem and is strictly conserved in all bacterial species. The D-amino acids that make up its cross-linked stem peptides are not abundant in nature and must be synthesized by bacteria de novo. Peptidoglycan is a sugar/amino acid polymer unique to bacteria and essential for division and cell shape maintenance. ![]()
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