Insights into the Unusual Activity of a Novel Homospermidine Synthase with a Promising Application to Produce Spermidine

Spermidine is a naturally occurring polyamine with multiple biological activities and potential food and agricultural applications. However, sustainable and scalable spermidine production has not yet been attained. In this study, a homospermidine synthase (HSS) from Pseudomonas frederiksbergensis (PfHSS) capable of catalyzing the synthesis of spermidine from 1,3-diaminopropane and putrescine was identified based on multiple sequence alignment using Blastochloris viridis HSS (BvHSS) as a template. The optimal reaction pH and temperature for purified Pf HSS were determined to be 8.5 and 45 degrees C, respectively, and K+ was able to promote the enzyme activity. Further analysis of the structural and functional relationships through molecular docking and molecular dynamics simulation indicates that glutamic acid at position 359 is the essential residue for the enzyme-catalyzed synthesis of spermidine. The whole-cell catalytic reaction yielded 1321.4 mg/L spermidine and 678.2 mg/L of homospermidine. This study presents a novel, promising, and sustainable biological method for producing spermidine.

Automated summary

In this study, a homospermidine synthase (HSS) from Pseudomonas frederiksbergensis (PfHSS) was identified and found to be capable of synthesizing spermidine from 1,3-diaminopropane and putrescine. Further analysis revealed that glutamic acid at position 359 is essential for the enzyme-catalyzed synthesis of spermidine. The whole-cell catalytic reaction yielded 1321.4 mg/L spermidine and 678.2 mg/L of homospermidine, providing a novel and promising biological method for sustainable spermidine production.