Lysine-cysteine NOS bonds
From Proteopedia
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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" /> | ||
Revision as of 23:52, 25 May 2021
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References
- ↑ 1.0 1.1 1.2 1.3 1.4 Wensien M, von Pappenheim FR, Funk LM, Kloskowski P, Curth U, Diederichsen U, Uranga J, Ye J, Fang P, Pan KT, Urlaub H, Mata RA, Sautner V, Tittmann K. A lysine-cysteine redox switch with an NOS bridge regulates enzyme function. Nature. 2021 May 5. pii: 10.1038/s41586-021-03513-3. doi:, 10.1038/s41586-021-03513-3. PMID:33953398 doi:http://dx.doi.org/10.1038/s41586-021-03513-3
