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Updated: Sep 13, 2025
A Customizable Approach for the Enzymatic Production and Purification of Diterpenoid Natural Products
Published on: October 4, 2019
Substrate-Cofactor Synergistic Reorientation and Substrate Tunnel Engineering of SspLCD for Efficient l-Pipecolic
Weijie Gao1, Ziyan Huang1, Yanjun Li1
1State Key Laboratory of Bioreactor Engineering New World Institute of Biotechnology, East China University of Science and Technology, 130 Meilong Road, 200237 Shanghai, China.
None:
Homology screening and structural selection identified a novel lysine cyclodeaminase (SspLCD) with high substrate tolerance for l-pipecolic acid (l-PA) synthesis, rapamycin's key intermediate. Mutant M4 (I61V/I94V/I233V/A235S), developed via substrate-cofactor reorientation and tunnel engineering, exhibited 87.3-fold higher catalytic efficiency than the wild-type. At 1,000 mM substrate loading, M4 achieved >99.9% conversion in 3 h, yielding 1,033 g·L-1·day-1─the highest reported l-PA space-time yield to date. This study establishes an industrially viable pathway for efficient l-PA bioproduction.
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