Sajid Moon, Stone Shane R, Kaur Parwinder
UWA School of Agriculture and Environment, The University of Western Australia, Perth, WA 6009, Australia.
Bioengineering (Basel). 2022 Oct 24;9(11):609. doi: 10.3390/bioengineering9110609.
Isoflavonoid synthase (IFS) is a critical enzyme for the biosynthesis of over 2400 isoflavonoids. Isoflavonoids are an important class of plant secondary metabolites that have a range of pharmaceutical and nutraceutical properties. With growing interest in isoflavonoids from both research and industrial perspectives, efforts are being forwarded to enhance isoflavonoid production in-planta and ex-planta; therefore, in-silico analysis and characterisation of available IFS protein sequences are needed. The present study is the first-ever attempt toward phylogenetic analysis and protein modelling of available IFS protein sequences. Phylogenetic analysis has shown that IFS amino acid sequences have 86.4% pairwise identity and 26.5% identical sites, and the sequences were grouped into six different clades. The presence of a β-hairpin and extra loop at catalytic sites of , and , respectively, compared with are critical structural differences that may affect catalytic function. Protein docking highlighted the preference of selected IFS for liquiritigenin compared with naringenin and has listed as the most efficient candidate for heterologous biosynthesis of isoflavonoids. The in-silico characterisation of IFS represented in this study is vital in realising the new bioengineering endeavours and will help in the characterisation and selection of IFS candidate enzymes for heterologous biosynthesis of isoflavonoids.
异黄酮合酶（IFS）是超过2400种异黄酮生物合成的关键酶。异黄酮是一类重要的植物次生代谢产物，具有一系列药学和营养保健特性。随着从研究和工业角度对异黄酮的兴趣日益增加，人们正在努力提高植物体内和体外的异黄酮产量；因此，需要对现有的IFS蛋白序列进行计算机分析和表征。本研究是对现有IFS蛋白序列进行系统发育分析和蛋白质建模的首次尝试。系统发育分析表明，IFS氨基酸序列的成对同一性为86.4%，相同位点为26.5%，这些序列被分为六个不同的进化枝。与相比，、和催化位点分别存在β-发夹结构和额外环，这是可能影响催化功能的关键结构差异。蛋白质对接突出了所选IFS对甘草素的偏好性高于柚皮素，并将列为异源生物合成异黄酮最有效的候选物。本研究中对IFS的计算机表征对于实现新的生物工程努力至关重要，并将有助于表征和选择用于异源生物合成异黄酮的IFS候选酶。
