The lytic polysaccharide monooxygenase JdLPMO10A is the N-terminal domain of the multimodular protein Jd1381. The isolated JdLPMO10A domain is one of the smallest chitin-active lytic polysaccharide monooxygenases known to date with a size of only 15.5 kDa. JdLPMO10A is a copper-dependent oxidative enzyme that depolymerizes chitin by hydroxylating the C1 carbon in the glycosidic bond. JdLPMO10A has been isotopically labeled and recombinantly expressed. Here, we report the ¹H, ¹³C, ¹⁵N resonance assignment of JdLPMO10A. Secondary structural elements predicted based on the NMR assignment are in excellent agreement with the crystal structure of JdLPMO10A.

裂解性多糖单加氧酶Jd LPMO10A 是多模块蛋白Jd 1381 的 N 端结构域。分离的Jd LPMO10A 结构域是迄今为止已知的最小的几丁质活性裂解性多糖单加氧酶之一，大小仅为 15.5 kDa。 Jd LPMO10A 是一种铜依赖性氧化酶，通过羟基化糖苷键中的 C1 碳来解聚甲壳素。 Jd LPMO10A 已被同位素标记并重组表达。在这里，我们报告了Jd LPMO10A 的¹ H、 ¹³ C、 ¹⁵ N 共振分配。基于 NMR 分配预测的二级结构元素与Jd LPMO10A 的晶体结构非常一致。