Cloning, expression, and functional analysis of lysine decarboxylase in mulberry (Morus alba L.)

1-Deoxynojirimycin (DNJ) is the main bioactive compound of Morus alba L.. DNJ has pharmacological effects, including blood sugar level regulation and antiviral activity. In this study, the mulberry lysine decarboxylase gene (MaLDC), which is involved in the biosynthesis of DNJ alkaloids, was cloned, expressed, and functionally verified. MaLDC was induced and expressed in Escherichia coli BL21 (DE3). The recombinant soluble MaLDC protein had a relative molecular mass of 24.0 kDa. The protein was purified by Ni-NTA separation. The results showed that MaLDC protein could catalyze lysine decarboxylation to produce cadaverine. The K_m and V_max values were 19.2 μM and 3.31 μM/min, respectively. Quantitative real-time reverse transcription polymerase chain reaction revealed that MaLDC expression was positively correlated with DNJ content (P < 0.001), indicating that the MaLDC could encode a functional protein involved in the biosynthesis of DNJ alkaloid in mulberry. Our results provided a foundation for further studies of the enzymatic properties of LDC and established a basis for the analysis of key enzymes involved in the biosynthetic pathway of mulberry DNJ alkaloid.