Molecular mechanism of key enzymes in lignan biosynthesis

On May 14, 2021, Zhang Peng's research group at the State Key Laboratory of Plant Molecular Genetics jointly published a research result entitled "Structure-based engineering of substrate specificity for pinoresinol-lariciresinol reductases" in Nature Communications, revealing lignans The molecular mechanism of PLR substrate selectivity for the key enzyme of biosynthesis

Isatis indigotica is the dried root of the cruciferous plant Isatis indigotica, and is a representative Chinese medicine for clearing away heat and detoxifying

The research team selected three PLRs with highly similar sequences (Identity>80%) but with different substrate selectivity (Isatis IiPLR1 can efficiently catalyze Pin to Lar and further generate Sec, while Arabidopsis AtPrR1 catalyzes the efficiency of Pin to Lar Significantly stronger than the efficiency of catalyzing Lar to Sec; AtPrR2 can only catalyze Pin to Lar)

By comparing the structure of the co-crystal of IiPLR1/AtPrR1/AtPrR2 and the substrate Pin, it is found that the disordered β4 loop in IiPLR1 turns over in AtPrR1/AtPrR2 and covers the substrate binding pocket

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Link to the paper: https:// 

Figure 1.