Authors
Yupeng Wan, Long Jiang, Yaojie Liu, Zongjiang Yu, Mo Xian, Chao Xu
Published in
Journal of agricultural and food chemistry. Sep 30, 2025. Epub Sep 30, 2025.
Abstract
1-Aminocyclopropane-1-carboxylic acid (ACC) is a nonprotein amino acid commonly found in plants, serving as an ethylene precursor with independent hormone functions that regulate plant growth, development, and stress resistance. Due to its agricultural significance, efforts have focused on boosting its production. In this study, ACC biosynthesis was achieved in E. coli via LaACS (1-aminocyclopropane-1-carboxylate synthase) from Lycoris aurea, which catalyzes S-adenosylmethionine (SAM). To enhance the yield, structural prediction of LaACS using AlphaFold2 and MOE docking identified the mutant LaACSL243A, which exhibited a doubled Vmax (0.018 mM/L/min) and Kcat (12.033 min-1) and 20% higher Kcat/Km (15.88 mM-1 min- 1) than that of the wild type. The intrinsic reasons for the enhanced catalytic efficiency were elucidated through molecular dynamics simulation. Subsequently, through screening of S-adenosylmethionine synthase (SAMS), SAMSa (from Arabidopsis thaliana) was identified as having the highest catalytic activity. Overexpression of the genes encoding SAMSa, MetA (homoserine O-succinyltransferase), and MetH (methionine synthase) successfully increased the ACC yield to 109 mg/L in 50 mL of M9 medium, which is twice that of the unmodified strain. The development of a green, safe, and efficient ACC biosynthetic process is of significant importance for promoting the application of ACC in agricultural science, biology, and medicine.
PMID:
41026927
Bibliographic data and abstract were imported from PubMed on 01 Oct 2025.
Read full publication at:
Please sign in
to see all details.
Advertisement
Stats
- Recommendations n/a n/a positive of 0 vote(s)
- Views 37
- Comments 0