2.3.2.12	evolution	for the ribosomal PTC used (U2673-C2836), there is 100% identity between Mycobacterium tuberculosis and Mycobacterium smegmatis. The Staphylococcus aureus peptidyl transferase center (PTC) is homologous to Mycobacterium tuberculosis PTC	-, 759048	
2.3.2.12	evolution	reconstruction of the three-dimensional structure of the ancestral peptidyl transferase center (PTC) built by concatamers of ancestral sequences of tRNAs, analysis of its possible interactions with tRNAs molecules, three-dimensional modeling, overview. Docking experiments between the ancestral PTC and tRNAs suggest that in the origin of the translation system, the PTC functioned as an adhesion center for tRNA molecules. Structure PDB ID4V8X is used as a template. The origin of the translation system is a major evolutionary transition because it enabled the establishment of the ribonucleoprotein world. The transfer RNA (tRNA) molecule played a central role during the origin of translation, bridging RNA and (RNA + proteins) worlds. These tRNAs may offer clues towards the elucidation of the origin of the genetic code. The ribosome is also at the core of this process: more specifically, the PTC responsible for peptide bond formation. The PTC is perhaps the oldest ribozyme due to its essential function of protein synthesis and because it is highly conserved in all cellular organisms. Since natural selection works without anticipation, the early PTC could have acted as a ribozyme that randomly produced peptide chains	759697	
2.3.2.12	evolution	the Staphylococcus aureus peptidyl transferase center (PTC) is homologous to Mycobacterium tuberculosis PTC	759048	
2.3.2.12	malfunction	bypass of classical penicillin-binding proteins by the L,D-transpeptidase leads to high-level ampicillin resistance in Enterococcus faecium mutants	-, 718599	
2.3.2.12	malfunction	loss of L,D-transpeptidase gene MT2594 does not alter susceptibility to isoniazid and D-cycloserine, but is associated with increased susceptibility to amoxicillin in the presence of clavulanic acid	-, 720522	
2.3.2.12	malfunction	Mycobacterium tuberculosis lacking a functional copy of LdtMt5 displays aberrant growth and is more susceptible to killing by crystal violet, osmotic shock, and select carbapenem antibiotics	-, 736488	
2.3.2.12	metabolism	mechanism of peptidyltransferase centre (PTC) completion, overview. Requirement of the universally conserved Gly-Gly-Gln (GGQ) tripeptide in the highly conserved peptidyl transferase center suggesting that the reported conformation is likely shared during termination of protein synthesis in all domains of life	759119	
2.3.2.12	metabolism	the peptidoglycans of the rough and smooth morphotypes contain predominantly 3->3 cross-links generated by L,D-transpeptidases	-, 719736	
2.3.2.12	additional information	the enzyme is part of the peptidyl transferase center (PTC)	-, 759048, 759697, 759863	
2.3.2.12	additional information	the enzyme is part of the peptidyl transferase center (PTC), conformation of methylated-GGQ in the peptidyl transferase center of the ribosome during canonical translational termination and co-translation quality control, structure modeling, overview	759119	
2.3.2.12	additional information	the ribosome is capable of polymerizing at a similar rate at least 20 different kinds of amino acids from aminoacyl-tRNA carriers while using just one catalytic site, the peptidyl-transferase center (PTC). The PTC uses an induced-fit mechanism, analysis of published ribosome structures supports the hypothesis that the induced fit eliminates unreactive rotamers predominantly populated for some A-site aminoacyl esters before induction. The hypothesis is fully consistent with the wealth of kinetic data obtained with these substrates. Induction constrains the amino acids into a reactive conformation in a side-chain independent manner. The rationale of the PTC structural organization confers to the ribosome the very unusual ability to handle large as well as small substrates. An induced fit (or conformational change) is identified in the peptidyl-transferase center (PTC) of the ribosome, in which the binding of the 3' acceptor arm of an A-site aminoacyl tRNA triggers a major rearrangement of two ribosome residues, U2506 and U2585, modeling, overview. The room available inside the PTC cavity and its flexibility in the uninduced state leave some conformational freedom to the esterified amino acids. The induced fit orients the aminoacyl ester for nucleophilic attack. PTC structure-function relationship, detailed overview	760119	
2.3.2.12	physiological function	changes of 23S rRNA nucleotides in the 2585 region of the peptidyl transferase center, G2583A and U2584C, reduce maximum induction of tna operon expression by tryptophan in vivo without affecting the concentration of tryptophan necessary to obtain 50% induction. The growth rate of strains with ribosomes with either of these changes is not altered appreciably. In vitro analyses show that tryptophan is not as efficient in protecting TnaC-tRNAPro from puromycin action as wild-type ribosomes. However, added tryptophan does prevent sparsomycin action as it normally does with wild-type ribosomes. These two mutational changes act by reducing the ability of ribosome-bound tryptophan to inhibit peptidyl transferase activity rather than by reducing the ability of the ribosome to bind tryptophan	698614	
2.3.2.12	physiological function	recombinant Mycobacterium bovis strain BCG overexpressing a L,D-transpeptidase that is nutrient starved elicits a stronger Th1 type response against virulent MMycobacterium tuberculosis and is at least as protective as parent Mycobacterium bovis strain BCG	-, 720812	
2.3.2.12	physiological function	some of the indigenous posttranscriptional modifications of rRNA can be viewed as intrinsic antibiotic resistance mechanisms. The lack of pseudouridine at position 2504 of 23S rRNA significantly increases the susceptibility of Escherichia coli to peptidyl transferase inhibitors	699543	
2.3.2.12	physiological function	the enzyme catalyzes the formation of 3 -> 3 peptidoglycan cross-links of the cell wall and facilitates resistance against classical beta-lactams	-, 736552	
2.3.2.12	physiological function	the enzyme LdtMt5 is necessary for properly maintaining cell wall integrity	-, 736488	
2.3.2.12	physiological function	the LdtMt2 protein is required for virulence and resistance to amoxicillin	-, 720522