The endo-β-N-acetylglucosaminidases (ENGases) are an enzyme class (EC 3.2.1.96) produced by a range of organisms, ranging from bacteria, through fungi, to higher order species, including humans, comprising two-sub families of glycosidases which all cleave the chitobiose core of N-linked glycans. Synthetic applications of these enzymes, i.e. to catalyse the reverse of their natural hydrolytic mode of action, allow the attachment of N-glycans to a wide variety of substrates which contain an N-acetylglucosamine (GlcNAc) residue to act as an ‘acceptor’ handle. The use of N-glycan oxazolines, high energy intermediates on the hydrolytic pathway, as activated donors allows their high yielding attachment to almost any amino acid, peptide or protein that contains a GlcNAc residue as an acceptor. The synthetic effectiveness of these biocatalysts has been significantly increased by the production of mutant glycosynthases; enzymes which can still catalyse synthetic processes using oxazolines as donors, but which do not hydrolyse the reaction products. ENGase biocatalysts are now finding burgeoning application for the production of biologically active glycopeptides and glycoproteins, including therapeutic monoclonal antibodies (mAbs) for which the oligosaccharides have been remodelled to optimise effector functions.

中文翻译：

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ENGases：通用的生物催化剂，用于生产均质的N-连接的糖肽和糖蛋白

的内切-β- Ñ -acetylglucosaminidases（ENGases）是由一系列的生物体产生的酶种类（EC 3.2.1.96），范围从细菌，真菌通过，到更高阶的物种，包括人类，包括糖苷酶的两个子家庭它们均裂解N-连接的聚糖的壳二糖核心。这些酶的合成应用，即催化其天然水解作用方式的逆转，使N-聚糖可以附着在多种包含N-乙酰氨基葡萄糖（GlcNAc）残基的底物上，充当“受体”手柄。 。N的使用-聚糖恶唑啉，水解途径上的高能中间体，因为它是活化的供体，因此它们可以高产率地附着在几乎任何含有GlcNAc残基作为受体的氨基酸，肽或蛋白质上。这些生物催化剂的合成效力通过产生突变的糖合酶而大大提高了。这些酶仍然可以催化使用恶唑啉作为供体的合成过程，但不会水解反应产物。ENGase生物催化剂现在正在迅速发展，用于生产具有生物活性的糖肽和糖蛋白，包括治疗性单克隆抗体（mAb），已对其寡糖进行重塑以优化效应子功能。