class="head no_bottom_margin" id="idm139847699469344title">AbstractGlycoside hydrolases (GHs) are classified into >100 sequence-based families. These enzymes process a wide variety of complex carbohydrates with varying stereochemistry at the anomeric and other ring positions. The shapes that these sugars adopt upon binding to their cognate GHs, and the conformational changes that occur along the catalysis reaction coordinate is termed the conformational itinerary. Efforts to define the conformational itineraries of GHs have focussed upon the critical points of the reaction: substrate-bound (Michaelis), transition state, intermediate (if relevant) and product-bound. Recent approaches to defining conformational itineraries that marry X-ray crystallography of enzymes bound to ligands that mimic the critical points, along with advanced computational methods and kinetic isotope effects are discussed.
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机译：<！-fig ft0-> <！-fig @ position =“ anchor” mode =文章f4-> <！-fig mode =“ anchred” f5-> <！-fig / graphic | fig / alternatives / graphic mode =“ anchored” m1-> class =“ head no_bottom_margin” id =“ idm139847699469344title”>摘要糖苷水解酶（GHs）分为> 100个基于序列的家族。这些酶加工各种复杂的碳水化合物，在异头异构体和其他环位置具有不同的立体化学。这些糖结合其同源GH后所采用的形状，以及沿着催化反应坐标发生的构象变化被称为构象路线。定义GHs构象路线的工作集中在反应的关键点：底物结合（Michaelis），过渡态，中间（如果相关）和产物结合。讨论了定义构象路线的最新方法，这些构象路线结合了与模拟临界点的配体结合的酶的X射线晶体学，以及先进的计算方法和动力学同位素效应。
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