| 1. | HIV-1 Protease has the classic AspThrGly of Aspartyl Proteases.
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| 2. | The overall conserved aspartyl residue required for phosphotransfer in response regulators.
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| 3. | The aspartyl residues are involved in the hydrolysis of the peptide bonds.
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| 4. | Chronologically, action of cathepsin S follows two cleavages performed by aspartyl proteases.
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| 5. | Aspartyl-tRNA synthetase charges its cognate tRNA with aspartate during protein biosynthesis.
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| 6. | It has, however, diminished discrimination, so that it can also form aspartyl-tRNAAsn.
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| 7. | A methyltransferase dependent pathway exists for the conversion of L-isoaspartyl back to l-aspartyl.
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| 8. | Similar methods may be used to specifically cleave tryptophanyl, aspartyl, cysteinyl, and asparaginyl peptide bonds.
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| 9. | Aspartyl-tRNA synthetase ( DARS ) is part of a multienzyme complex of aminoacyl-tRNA synthetases.
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| 10. | HIV protease inhibitors are peptide-like chemicals that competitively inhibit the action of the virus aspartyl protease.
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