Lysine-cysteine NOS bonds: Difference between revisions
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Oxidation breaks the NOS bond. In transaldolase, breaking the NOS bond causes subtle allosteric shifts in the catalytic site, decreasing enzymatic activity by several orders of magnitude<ref name="wensien2021" />. Thus, the NOS bond is described as an allosteric redox switch<ref name="wensien2021" />. | Oxidation breaks the NOS bond. In transaldolase, breaking the NOS bond causes subtle allosteric shifts in the catalytic site, decreasing enzymatic activity by several orders of magnitude<ref name="wensien2021" />. Thus, the NOS bond is described as an '''allosteric redox switch'''<ref name="wensien2021" />. | ||
A survey of the data in the [[Protein Data Bank]] revealed that the NOS bond likely exists "in diverse protein families across all domains of life (including ''Homo sapiens'') and that it is often located at catalytic or regulatory hotspots."<ref name="wensien2021" /> Because the NOS bond was unknown before 2021, it could easily have been overlooked in earlier interpretations of [[electron density maps]].<ref name="wensien2021" /> | A survey of the data in the [[Protein Data Bank]] revealed that the NOS bond likely exists "in diverse protein families across all domains of life (including ''Homo sapiens'') and that it is often located at catalytic or regulatory hotspots."<ref name="wensien2021" /> Because the NOS bond was unknown before 2021, it could easily have been overlooked in earlier interpretations of [[electron density maps]].<ref name="wensien2021" /> | ||