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Temperature dependence of binding and catalysis for the Cdc25B phosphatase

Using a combination of steady-state and single-turnover kinetics, we probe the temperature dependence of substrate association and chemistry for the reaction of Cdc25B phosphatase with its Cdk2-pTpY/CycA protein substrate. The transition state for substrate association is dominated by an enthalpic b...

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Autori principali: Sohn, Jungsan, Rudolph, Johannes
Natura: Artigo
Lingua:Inglês
Pubblicazione: 2006
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Accesso online:https://ncbi.nlm.nih.gov/pmc/articles/PMC1849978/
https://ncbi.nlm.nih.gov/pubmed/17174465
https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1016/j.bpc.2006.11.005
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