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Updated: Jan 11, 2026

Enzymatic Cascade Reactions for the Synthesis of Chiral Amino Alcohols from L-lysine
Published on: February 16, 2018
Functional characterization of aldo-keto reductase genes from Lycoris aurea that participate in galantamine
Yiyu Xiang1, Xiaoran Jiang2, Jie Li2
1Nanjing University of Chinese Medicine, Nanjing 210023, China; Institute of Botany, Jiangsu Province and Chinese Academy of Sciences, Nanjing 210014, China.
Abstract:
Galantamine is an important secondary metabolite in plants that possesses a wide range of biological activities. The reduction of narwedine to form galantamine in planta has been proven to be catalyzed by enzymes in the aldo-keto reductase (AKR) gene family. In this study, ten homologous AKR unigenes were screened from the transcriptome data of Lycoris species, and two AKR homologs (LauAKR1 and LauAKR2) were cloned from Lycoris aurea. Both LauAKR1 and LauAKR2 belong to the AKR4B subfamily and share similarities with known plant AKRs. They have retained most of the conserved active-site residues found in the AKR superfamily of enzymes. LauAKR1 and LauAKR2 were ubiquitously expressed in different tissues of L. aurea, and they were expressed at relatively higher levels in the leaves, seeds, and bulbs. In addition, the transcripts of LauAKR1 and LauAKR2 were induced by treatment with sodium chloride but were unaffected by treatments with methyl jasmonate and mannitol. Additionally, LauAKR1 and LauAKR2 tagged with green fluorescent protein were subjected to agroinfiltration for transient expression in Nicotiana benthamiana, which showed that both LauAKR1 and LauAKR2 are localized to the cytoplasm. LauAKR1 and LauAKR2 facilitated the NADPH-dependent reduction of the substrates demethylnarwedine and narwedine. This study provides direct evidence that LauAKR catalyzes the crucial reduction reactions involved in the formation of galantamine.
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