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Mining and rational design of psychrophilic catalases using metagenomics and deep learning models

文献类型： 外文期刊

作者： Wu, Shuning 1 ; Xu, Guoshun 3 ; Su, Yongping 1 ; Huang, Huoqing 3 ; Xu, Xinxin 1 ; Zhang, Yuhong 1 ; Tian, Jian 1 ; Zhang, Wei 1 ; Zhang, Zhiwei 2 ; Liu, Bo 1 ;

作者机构： 1.Chinese Acad Agr Sci, Biotechnol Res Inst, 12 Zhongguancun South St, Beijing 100081, Peoples R China

2.Shanxi Agr Univ, Coll Forestry, 81 Longcheng St, Taiyuan 030031, Shanxi, Peoples R China

3.Chinese Acad Agr Sci, Inst Anim Sci, 2 Yuanmingyuan West Rd, Beijing 100193, Peoples R China

关键词： Catalase; Optimum temperature; Metagenomics; Deep learning model; Rational design

期刊名称：APPLIED MICROBIOLOGY AND BIOTECHNOLOGY （ 影响因子：5.0； 五年影响因子：5.2 ）

ISSN： 0175-7598

年卷期： 2024 年 108 卷 1 期

页码：

收录情况： SCI

摘要： Osmolytes are produced by various microorganisms as a defense mechanism to protect cells and macromolecules from damage caused by external stresses in harsh environments. Due to their useful stabilizing properties, these molecules are applied as active ingredients in a wide range of cosmetics and healthcare products. The metabolic pathways and biocatalytic syntheses of glycosidic osmolytes such as 2-O-alpha-D-glucosyl-D-glycerate often involve the action of a glycoside phosphorylase. Here, we report the discovery of a glucosylglycerate phosphorylase from carbohydrate-active enzyme family GH13 that is also active on sucrose, which contrasts the strict specificity of known glucosylglycerate phosphorylases that can only use alpha-D-glucose 1-phosphate as glycosyl donor in transglycosylation reactions. The novel enzyme can be distinguished from other phosphorylases from the same family by the presence of an atypical conserved sequence motif at specificity-determining positions in the active site. The promiscuity of the sucrose-active glucosylglycerate phosphorylase can be exploited for the high-yielding and rapid synthesis of 2-O-alpha-D-glucosyl-D-glycerate from sucrose and D-glycerate. Key points . A Xylanimonas protaetiae glycoside phosphorylase can use both d-glycerate and fructose as glucosyl acceptor with high catalytic efficiency . Biocatalytic synthesis of the osmolyte 2-O-alpha-D-glucosyl-D-glycerate . Positions in the active site of GH13 phosphorylases act as convenient specificity fingerprints

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