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. 2016 Jul 15;27(14):2331–2340. doi: 10.1091/mbc.E16-03-0137

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© 2016 Rubinstein et al. This article is distributed by The American Society for Cell Biology under license from the author(s). Two months after publication it is available to the public under an Attribution–Noncommercial–Share Alike 3.0 Unported Creative Commons License (http://creativecommons.org/licenses/by-nc-sa/3.0).

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FIGURE 1: — Mixed, processive, and distributive mechanisms. S₀₀, S₀₁, and S₁₁ denote unphosphorylated, monophosphorylated, and bisphosphorylated forms of the substrate, respectively. (A) In our model, dual phosphorylation and dephosphorylation are assumed to occur by a mixed mechanism. Processive and distributive mechanisms are limiting cases of the mixed mechanism. (B) In a processive mechanism, the same enzyme phosphorylates the substrate twice, without dissociating. This corresponds to the limit where for the complex of enzyme and monophosphorylated substrate. (C) In a distributive mechanism, upon the first phosphorylation event, the enzyme–substrate complex dissociates immediately, allowing the molecules to find new binding partners. This corresponds to the limit where for the complex of enzyme and monophosphorylated substrate.

Inline graphic — Mixed, processive, and distributive mechanisms. S₀₀, S₀₁, and S₁₁ denote unphosphorylated, monophosphorylated, and bisphosphorylated forms of the substrate, respectively. (A) In our model, dual phosphorylation and dephosphorylation are assumed to occur by a mixed mechanism. Processive and distributive mechanisms are limiting cases of the mixed mechanism. (B) In a processive mechanism, the same enzyme phosphorylates the substrate twice, without dissociating. This corresponds to the limit where for the complex of enzyme and monophosphorylated substrate. (C) In a distributive mechanism, upon the first phosphorylation event, the enzyme–substrate complex dissociates immediately, allowing the molecules to find new binding partners. This corresponds to the limit where for the complex of enzyme and monophosphorylated substrate.