Department of Life Sciences, University of Bath, Claverton Down, Bath BA2 7AY, UK.
Chem Commun (Camb). 2024 Aug 29;60(71):9463-9471. doi: 10.1039/d4cc03191a.
The tertiary and quaternary structures of many proteins are stabilized by strong covalent forces, of which disulfide bonds are the most well known. A new type of intramolecular and intermolecular covalent bond has been recently reported, consisting of the Lys and Cys side-chains linked by an oxygen atom (NOS). These post-translational modifications are widely distributed amongst proteins, and are formed under oxidative conditions. Similar linkages are observed during antibiotic biosynthesis, where hydroxylamine intermediates are tethered to the sulfur of enzyme active site Cys residues. These linkages open the way to understanding protein structure and function, give new insights into enzyme catalysis and natural product biosynthesis, and offer new strategies for drug design.
许多蛋白质的三级和四级结构是通过强共价键稳定的，其中二硫键最为人所知。最近报道了一种新的分子内和分子间共价键，由赖氨酸和半胱氨酸侧链通过氧原子（NOS）连接而成。这些翻译后修饰广泛存在于蛋白质中，并在氧化条件下形成。在抗生素生物合成过程中也观察到类似的键合，其中羟胺中间体与酶活性位点半胱氨酸残基的硫连接。这些键合为理解蛋白质结构和功能提供了新的途径，为酶催化和天然产物生物合成提供了新的见解，并为药物设计提供了新的策略。
