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In tRNA charging, the Km (ATP) is unaffected in the heterodimer, but the Kcat is one half that of wild type enzyme.

In tRNA charging, the Km (ATP) is unaffected in the heterodimer, but the Kcat is one half that of wild type enzyme. Correct Answer True

The above statement is true. The C-terminal domain of tyrosyl-tRNA synthetase contains major binding determinants for the tRNA. Thus, the heterodimer appears to be a fully refolded, active molecule, in which one subunit can complement a lesion on the other subunit.

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