Section 39.2 discussed the mechanism by which threonyl - tRNA synthetase attaches threonine to the proper tRNA while preventing the attachment of the similar amino acids valine and serine. Using this as a model, explain how an isoleucyl - tRNA synthetase might prevent the incorrect addition of the similar amino acids leucine and valine to its target tRNA.

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∻Answer∻ ⚹ Isoleucyl-tRNA synthetase prevents the incorrect addition of similar amino acids leucine and valine to its target tRNA by utilizing a combination of size exclusion and editing mechanisms. ⚹ ∻Solution∻ ‖ a ⋮ Size Exclusion: The active site of isoleucyl-tRNA synthetase is specifically shaped to accommodate isoleucine, which has a unique side chain. This shape prevents larger or smaller amino acids, such as leucine and valine, from fitting properly. ‖‖ b ⋮ Editing Mechanism: If a similar amino acid like leucine or valine is mistakenly attached, the enzyme has an editing site that hydrolyzes the incorrect amino acid-tRNA complex, ensuring only the correct isoleucine is attached. ‖ ∻Key Concept∻ ⚹ Specificity and Editing Mechanisms in Aminoacyl-tRNA Synthetases ⚹ ∻Explanation∻ ⚹ Isoleucyl-tRNA synthetase ensures the correct amino acid is attached to its tRNA by using a combination of size exclusion to prevent incorrect amino acids from binding and an editing mechanism to remove any incorrectly attached amino acids. ⚹◊How does isoleucyl - tRNA synthetase prevent the incorrect addition of leucine and valine to its target tRNA?⍭ Generate me a similar question◊

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