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File:Duplication events and changes in specificity and activity in evolution of Saccharomyces cerevisiae MalS enzymes - Journal.pbio.1001446.g002.png

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English: Duplication events and changes in specificity and activity in evolution of S. cerevisiae MalS enzymes.

The hydrolytic activity of all seven present-day alleles of Mal and Ima enzymes as well as key ancestral (anc) versions of these enzymes was measured for different α-glucosides. The width of the colored bands corresponds to kcat/Km of the enzyme for a specific substrate. Specific values can be found in Table S2. Note that in the case of present-day Ima5, we were not able to obtain active purified protein. Here, the width of the colored (open) bands represents relative enzyme activity in crude extracts derived from a yeast strain overexpressing IMA5 compared to an ima5 deletion mutant. While these values are a proxy for the relative activity of Ima5 towards each substrate, they can therefore not be directly compared to the other parts of the figure. For ancMalS and ancMal-Ima, activity is shown for the variant with the highest confidence (279G for ancMalS and 279A for ancMal-Ima). Activity for all variants can be found in Table S2.

doi:10.1371/journal.pbio.1001446.g002
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Source Voordeckers K, Brown CA, Vanneste K, van der Zande E, Voet A, et al. (2012) Reconstruction of Ancestral Metabolic Enzymes Reveals Molecular Mechanisms Underlying Evolutionary Innovation through Gene Duplication. PLoS Biol 10(12): e1001446. doi:10.1371/journal.pbio.1001446
Author Voordeckers K, Brown CA, Vanneste K, van der Zande E, Voet A, et al. (2012)
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