?!DOCTYPE html> A variable loop involved in the substrate selectivity of pinoresinol/lariciresinol reductase from-安徽农业大学-茶与食品科技学院
<span id="h7f9l"><dl id="h7f9l"><del id="h7f9l"></del></dl></span>
<strike id="h7f9l"></strike>
<span id="h7f9l"></span>
<strike id="h7f9l"><i id="h7f9l"><cite id="h7f9l"></cite></i></strike>
<span id="h7f9l"><dl id="h7f9l"><strike id="h7f9l"></strike></dl></span>
<span id="h7f9l"></span>
<span id="h7f9l"></span>
<span id="h7f9l"></span>
<span id="h7f9l"><dl id="h7f9l"><ruby id="h7f9l"></ruby></dl></span><strike id="h7f9l"><i id="h7f9l"></i></strike>
<span id="h7f9l"><i id="h7f9l"></i></span>
<strike id="h7f9l"></strike><span id="h7f9l"></span><strike id="h7f9l"><dl id="h7f9l"></dl></strike>
<strike id="h7f9l"><i id="h7f9l"><ruby id="h7f9l"></ruby></i></strike><strike id="h7f9l"></strike>
您现在的位置是: 首页 > 科学研究 > 科研成果 > 正文

A variable loop involved in the substrate selectivity of pinoresinol/lariciresinol reductase from

作?  文章来源:   点击? 更新日期:2019-04-23


A variable loop involved in the substrate selectivity of pinoresinol/

lariciresinol reductase from Camellia sinensis


Yingling Wua, Dawei Xinga, Guoliang Maa, Xinlong Daia, Liping Gaob∗∗, Tao Xia?/span>


Phytochemistry 162 (2019) 1?



Pinoresinol/lariciresinol reductase (PLR), an NADPH-dependent reductase that catalyzes the sequential reduction of pinoresinol into secoisolariciresinol via Lariciresinol, can lead to the structural and stereochemical diversity of lignans. The relationship between substrate-selective reaction of PLR and sequence homology still remains unclear. In this study, we focused on the contribution of the variable region between PLRs in determining substrate selectivity. Here, two CsPLRs (CsPLR1 and CsPLR2) were identified in the tea plant (Camellia sinensis var. sinensis cv. Shuchazao). In vitro enzymatic assays showed that CsPLR1 could convert (+)- and (?-pinoresinol into lariciresinol or secoisolariciresinol, whereas CsPLR2 catalyzed (+)-pinoresinol enantioselectively into (?-secoisolariciresinol. Homology modeling and site-directed mutagenesis were used to examine the role of a variable loop in catalysis and substrate selectivity. The L174I mutant in CsPLR1 lost the capacity to reduce either (+)- or (?-pinoresinol but retained the ability to catalyze the reduction of (?-lariciresinol. These findings provide a basis for better understanding of the substrate-selective reaction of PLR.