Terminal Uridylyl Transferase: Difference between revisions
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In the most general sense, the transferase reaction consists of the RNA substrate nucleophile (with some nucleotide selectivity) attacking the α-phosphorus atom of the nucleotide triphosphate [[ligand]].<ref name="primary citation">PMID:17785418</ref> The Mg<sup>2+</sup> ions are an important component of this reaction as one is thought to aid nucleophile deprotonation with the catalytic base (expected to be D136) and the other is thought to stabilize the leaving group (pyrophosphate).<ref name="primary citation">PMID:17785418</ref> However, due to steric constraints between the ATP [[ligand]] and the active site and RNA substrate, RNA binding is destabilized, thus slowing catalysis and the transfer of adenosine nucleotides.<ref name="primary citation">PMID:17785418</ref> | In the most general sense, the transferase reaction consists of the RNA substrate nucleophile (with some nucleotide selectivity) attacking the α-phosphorus atom of the nucleotide triphosphate [[ligand]].<ref name="primary citation">PMID:17785418</ref> The Mg<sup>2+</sup> ions are an important component of this reaction as one is thought to aid nucleophile deprotonation with the catalytic base (expected to be D136) and the other is thought to stabilize the leaving group (pyrophosphate).<ref name="primary citation">PMID:17785418</ref> However, due to steric constraints between the ATP [[ligand]] and the active site and RNA substrate, RNA binding is destabilized, thus slowing catalysis and the transfer of adenosine nucleotides.<ref name="primary citation">PMID:17785418</ref> | ||
