N-glycosylation is one of the most important posttranslational modifications of proteins. It plays important roles in the biogenesis and functions of proteins by influencing their folding, intracellular localization, stability and solubility. N-glycans are synthesized by glycosyltransferases, a complex group of ubiquitous enzymes that occur in most kingdoms of life. A growing body of evidence shows that N-glycans may influence processing and functions of glycosyltransferases, including their secretion, stability and substrate/acceptor affinity. Changes in these properties may have a profound impact on glycosyltransferase activity. Indeed, some glycosyltransferases have to be glycosylated themselves for full activity. N-glycans and glycosyltransferases play roles in the pathogenesis of many diseases (including cancers), so studies on glycosyltransferases may contribute to the development of new therapy methods and novel glycoengineered enzymes with improved properties. In this review, we focus on the role of N-glycosylation in the activity of glycosyltransferases and attempt to summarize all available data about this phenomenon.

中文翻译：

---

糖基化如何影响糖基化：N-聚糖在糖基转移酶活性中的作用。

N-糖基化是蛋白质最重要的翻译后修饰之一。它通过影响蛋白质的折叠、细胞内定位、稳定性和溶解性，在蛋白质的生物发生和功能中发挥重要作用。N-聚糖是由糖基转移酶合成的，糖基转移酶是一组复杂的普遍存在的酶，存在于大多数生命王国中。越来越多的证据表明，N-聚糖可能会影响糖基转移酶的加工和功能，包括它们的分泌、稳定性和底物/受体亲和力。这些特性的变化可能对糖基转移酶活性产生深远的影响。事实上，一些糖基转移酶必须自身糖基化才能发挥全部活性。N-聚糖和糖基转移酶在许多疾病（包括癌症）的发病机制中发挥作用，因此，对糖基转移酶的研究可能有助于开发新的治疗方法和具有改进特性的新型糖工程酶。在这篇综述中，我们专注于 N-糖基化在糖基转移酶活性中的作用，并试图总结关于这种现象的所有可用数据。