Primary research data for: "Substrate-Cofactor Synergistic Reorientation and Substrate Tunnel Engineering of SspLCD for Efficient L-Pipecolic Acid Biosynthesis"

This dataset contains enzyme activity profiles and time-course data supporting the findings in:"Substrate-Cofactor Synergistic Reorientation and Substrate Tunnel Engineering of SspLCD for Efficient L-Pipecolic Acid Biosynthesis" ## Included Data1. Wild-type (NspLCD/SspLCD) and mutant enzyme activities at varying substrate concentrations (50-1000 mM)2. Detailed time-course conversions for wild-type and optimized quadruple mutant (M4)3. Complete replicate measurements with statistical analysis ## Experimental Conditions- Substrate: L-Lysine- Buffer: 100 mM phosphate, pH 7.5- Temperature: 37°C- Detection: HPLC quantification of L-Pipecolic acid ## File Contents- Enzyme_Activity.xlsx: Raw conversion data- README_Gao_etal_OL2025.txt: Detailed data guide ## Corresponding ManuscriptOrganic Letters (Manuscript ID: ol-2025-022975.R1)