User:Naki0515/Amino acid activation
Article Draft[edit]
It's the hydrolyzation of the ATP that makes peptide bond formation a favorable reaction because of the inorganic phosphate acting as a leaving group, resulting in a high negative free energy.[1]
However, depending on the chirality of the amino acid, an aminoacyl-tRNA-synthase can actually disrupt the ester bond between D-amino acids and tRNA. This can happen if there is an editing domain that's lacking in the active site of that aminoacyl-tRNA-synthase.[2]
References
- ^ "Prebiotic Peptide Bond Formation Through Amino Acid Phosphorylation. Insights from Quantum Chemical Simulations". Life – via MDPI.
- ^ "Stereospecificity control inaminoacyl-tRNA-synthetases: new evidence of D-amino acids activation and editing".
{{cite journal}}: Cite journal requires|journal=(help); line feed character in|title=at position 72 (help)