EC Number |
General Information |
Reference |
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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 | more |
the enzyme is part of the peptidyl transferase center (PTC) |
-, 759048, 759697, 759863 |
2.3.2.12 | more |
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 |