Biotin (vitamin H or B7) is a coenzyme essential for all forms of life. Biotin has biological activity only when covalently attached to a few key metabolic enzyme proteins. Most organisms have only one attachment enzyme, biotin protein ligase (BPL), which attaches biotin to all target proteins. The sequences of these proteins and their substrate proteins are strongly conserved throughout biology. Structures of both the biotin ligase- and biotin-acceptor domains of mammals, plants, several bacterial species, and archaea have been determined. These, together with mutational analyses of ligases and their protein substrates, illustrate the exceptional specificity of this protein modification. For example, the Escherichia coli BPL biotinylates only one of the >4000 cellular proteins. Several bifunctional bacterial biotin ligases transcriptionally regulate biotin synthesis and/or transport in concert with biotinylation. The human BPL has been demonstrated to play an important role in that mutations in the BPL encoding gene cause one form of the disease, biotin-responsive multiple carboxylase deficiency. Promiscuous mutant versions of several BPL enzymes release biotinoyl-AMP, the active intermediate of the ligase reaction, to solvent. The released biotinoyl-AMP acts as a chemical biotinylation reagent that modifies lysine residues of neighboring proteins in vivo. This proximity-dependent biotinylation (called BioID) approach has been heavily utilized in cell biology.

中文翻译：

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您喜欢的生物素蛋白连接酶：异常特异性或混杂的蛋白质生物素化

生物素（维生素 H 或 B7）是所有生命形式必需的辅酶。生物素仅在与一些关键代谢酶蛋白共价连接时才具有生物活性。大多数生物体只有一种附着酶，即生物素蛋白连接酶 (BPL)，它将生物素附着到所有目标蛋白上。这些蛋白质及其底物蛋白质的序列在整个生物学中高度保守。哺乳动物、植物、几种细菌物种和古细菌的生物素连接酶和生物素受体结构域的结构已被确定。这些，连同连接酶及其蛋白质底物的突变分析，说明了这种蛋白质修饰的特殊特异性。例如，大肠杆菌BPL 仅对超过 4000 种细胞蛋白中的一种进行生物素化。几种双功能细菌生物素连接酶与生物素化一致转录调节生物素合成和/或运输。人类 BPL 已被证明发挥重要作用，BPL 编码基因的突变会导致一种疾病，即生物素反应性多重羧化酶缺乏症。几种 BPL 酶的混杂突变版本将连接酶反应的活性中间体生物素酰-AMP 释放到溶剂中。释放的生物素酰-AMP 作为化学生物素化试剂，在体内修饰邻近蛋白质的赖氨酸残基。这种邻近依赖性生物素化（称为 BioID）方法已在细胞生物学中得到广泛应用。