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how do class i and class ii aminoacyl-trna synthetases differ? choose one or more: a. structure of the active site b. atp binding domain c. types of reactions they catalyze d. mechanism of interaction with the trna

Sagot :

The two kinds of synthetases catalyze the same global process, the attachment of an amino acid to the tRNA, but differ in where the amino acid is put on the terminal adenosine of the tRNA: Class I enzymes prefer 2' hydroxyl groups, whereas class II enzymes prefer 3' hydroxyl groups.

ARSs catalyze the ligation of amino acids to their corresponding transfer RNAs (tRNAs), and so play a crucial role in protein synthesis. These enzymes can be found in free form or as part of a multi-tRNA synthetase complex in eukaryotic cells (MSC).

Aminoacyl tRNA synthetases feature a proofreading mechanism that allows them to distinguish between various amino acids.

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