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Similarities and differences in the biochemical and enzymological properties of the four isomaltases from Saccharomyces cerevisiae

机译：酿酒酵母中四种异麦芽糖酶的生化和酶学性质的异同

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The yeast Saccharomyces cerevisiae IMA multigene family encodes four isomaltases sharing high sequence identity from 65% to 99%. Here, we explore their functional diversity, with exhaustive in-vitro characterization of their enzymological and biochemical properties. The four isoenzymes exhibited a preference for the @a-(1,6) disaccharides isomaltose and palatinose, with Michaelis-Menten kinetics and inhibition at high substrates concentration. They were also able to hydrolyze trisaccharides bearing an @a-(1,6) linkage, but also @a-(1,2), @a-(1,3) and @a-(1,5) disaccharides including sucrose, highlighting their substrate ambiguity. While Ima1p and Ima2p presented almost identical characteristics, our results nevertheless showed many singularities within this protein family. In particular, Ima3p presented lower activities and thermostability than Ima2p despite only three different amino acids between the sequences of these two isoforms. The Ima3p
机译：酵母啤酒酵母IMA多基因家族编码4种异麦芽糖酶，共有65％至99％的高序列同一性。在这里，我们探索了它们的功能多样性，并对其酶学和生化特性进行了详尽的体外表征。四种同工酶表现出对@ a-（1,6）二糖异麦芽糖和帕拉金糖的偏爱，在高底物浓度下具有Michaelis-Menten动力学和抑制作用。他们还能够水解带有@ a-（1,6）键的三糖，还可以水解@ a-（1,2），@ a-（1,3）和@ a-（1,5）二糖，包括蔗糖。 ，突出显示了他们的内容歧义。虽然Ima1p和Ima2p呈现几乎相同的特征，但我们的结果显示该蛋白家族中有许多奇异之处。特别是，尽管这两个同工型的序列之间只有三个不同的氨基酸，但Ima3p的活性和热稳定性却低于Ima2p。 Ima3p

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