Molecular insights into the mechanism of substrate binding and catalysis of bifunctional FAD synthetase from Staphylococcus aureus.

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第一作者： Anusree,Lohithakshan

第一单位： Department of Molecular Nutrition, CSIR-Central Food Technological Research Institute (CFTRI), Mysore, Karnataka, 570020, India; Academy of Scientific and Innovative Research (AcSIR), Ghaziabad, 201002, India.

作者： Anusree,Lohithakshan ^[1] ; Raja,Narayanasamy ^[2] ; Upasana S,Potteth ^[3] ; Shwetha,Keshava ^[3] ; Vibha,Nagaraja ^[3] ; Dandamudi,Usharani ^[2] ; Ravi,Kumar ^[4]

作者单位： Department of Molecular Nutrition, CSIR-Central Food Technological Research Institute (CFTRI), Mysore, Karnataka, 570020, India; Academy of Scientific and Innovative Research (AcSIR), Ghaziabad, 201002, India. ^[1] Department of Food Safety and Analytical Quality Control Laboratory, CSIR-Central Food Technological Research Institute (CFTRI), Mysore, Karnataka, 570020, India; Academy of Scientific and Innovative Research (AcSIR), Ghaziabad, 201002, India. ^[2] Department of Molecular Nutrition, CSIR-Central Food Technological Research Institute (CFTRI), Mysore, Karnataka, 570020, India. ^[3] Department of Molecular Nutrition, CSIR-Central Food Technological Research Institute (CFTRI), Mysore, Karnataka, 570020, India; Academy of Scientific and Innovative Research (AcSIR), Ghaziabad, 201002, India. Electronic address: ravik@cftri.res.in. ^[4]

关键词 FAD synthetase FMNAT Molecular dynamics RFK domain