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Changes in the allosteric site of human liver pyruvate kinase upon activator binding include the breakage of an intersubunit cation–π bond
Human liver pyruvate kinase (hLPYK) converts phosphoenolpyruvate to pyruvate in the final step of glycolysis. hLPYK is allosterically activated by fructose-1,6-bisphosphate (Fru-1,6-BP). The allosteric site, as defined by previous structural studies, is located in domain C between the phosphate-bind...
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| Pubblicato in: | Acta Crystallogr F Struct Biol Commun |
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| Autori principali: | , , , , , |
| Natura: | Artigo |
| Lingua: | Inglês |
| Pubblicazione: |
International Union of Crystallography
2019
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| Soggetti: | |
| Accesso online: | https://ncbi.nlm.nih.gov/pmc/articles/PMC6572093/ https://ncbi.nlm.nih.gov/pubmed/31204694 https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1107/S2053230X19007209 |
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