Functional characterization and protein engineering of a O-methyltransferase involved in benzylisoquinoline alkaloid biosynthesis of Stephania tetrandra.

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Tác giả: Yue Feng, Guoyin Kai, Kunlun Li, Jiaqian Mao, Zengyuan Wang, Zhoulu Wang, Yanting Wu, Hao Zhan

Ngôn ngữ: eng

Ký hiệu phân loại:

Thông tin xuất bản: Netherlands : International journal of biological macromolecules , 2025

Mô tả vật lý:

Bộ sưu tập: NCBI

ID: 253805

Benzylisoquinoline alkaloids (BIAs) are the primary active components of Stephania tetrandra. However, the molecular mechanisms underlying BIA biosynthesis in S. tetrandra remain poorly understood. Here, we reported the isolation and characterization of a novel O-methyltransferase, designated as St7OMT1, from S. tetrandra. St7OMT1 exhibited strict substrate specificity and regioselectivity, catalyzing the conversion of (S)-coclaurine to norarmepavine at the C7 position. Optimal enzymatic activity of St7OMT1 was detected at 30 °C and pH 6.0 in sodium citrate buffer, with kinetic parameters of K
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