Structural basis of the bifunctionality of Marinobacter salinexigens ZYF650<sup>T</sup> glucosylglycerol phosphorylase in glucosylglycerol catabolism.

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作者： Di,Lu ^[1] ; Keke,Zhang ^[2] ; Chen,Cheng ^[1] ; Danni,Wu ^[2] ; Lei,Yin ^[3] ; Quan,Luo ^[2] ; Meiyun,Shi ^[4] ; Honglei,Ma ^[5] ; Xuefeng,Lu ^[2]

作者单位： School of Chemical Engineering, Marine and Life Sciences, Dalian University of Technology, Panjin, China; Key Laboratory of Biofuels, Qingdao Institute of Bioenergy and Bioprocess Technology, Chinese Academy of Sciences, Qingdao, China. ^[1] Key Laboratory of Biofuels, Qingdao Institute of Bioenergy and Bioprocess Technology, Chinese Academy of Sciences, Qingdao, China; Shandong Energy Institute, Qingdao, China; Qingdao New Energy Shandong Laboratory, Qingdao, China. ^[2] School of Chemical Engineering, Marine and Life Sciences, Dalian University of Technology, Panjin, China. ^[3] School of Chemical Engineering, Marine and Life Sciences, Dalian University of Technology, Panjin, China. Electronic address: shimy@dlut.edu.cn. ^[4] Key Laboratory of Biofuels, Qingdao Institute of Bioenergy and Bioprocess Technology, Chinese Academy of Sciences, Qingdao, China; Shandong Energy Institute, Qingdao, China; Qingdao New Energy Shandong Laboratory, Qingdao, China. Electronic address: mahonglei@qibebt.ac.cn. ^[5]

关键词 GH13_18 family crystal structure double displacement mechanism glucosylglycerol phosphorylase α-d-glucose-1-phosphate

DOI 10.1016/j.jbc.2024.108127

PMID 39725037

发布时间 2025-02-04

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