Characterization and biochemical investigation of the potential inositol monophosphate phosphatase involved in bacterial mycothiol biosynthesis |
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Authors: | Yuchuan Guo Wei Gong Lizhen Wang Jiatong Guo Guoxia Jin |
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Institution: | 1. National Glycoengineering Research Center and Shandong Provincial Key Laboratory of Carbohydrate Chemistry and Glycobiology, Shandong University, Jinan, China;2. Department of Chemistry, University of Florida, Gainesville, USA;3. Department of Chemistry, University of Florida, Gainesville, USA;4. College of Chemistry, Chemical Engineering and Materials Science, Shandong Normal University, Jinan, China |
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Abstract: | AbstractMycothiol (MSH) is the predominant form of small molecule thiols produced by actinomycetes and plays a pivotal role in the bacterial detoxication process. The only enzyme involved in MSH biosynthesis that has not been characterized yet is a phosphatase MshA2, which was proposed to catalyze the hydrolysis of 3-phospho-1-D-myo-inosityl-2-acetamido-2-deoxy-α-D-glucopyranoside (GlcNAc-Ins-3-P) to GlcNAc-Ins. In this study, a new inositol monophosphate phosphatase from Corynebacterium glutamicum, designated as Cg0911, was discovered, expressed and characterized. Detailed biochemical studies on Cg0911 revealed that GlcNAc-Ins-3-P was its preferred substrate for efficient conversion into GlcNAc-Ins. |
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Keywords: | Mycothiol MshA2 Cg0911 inositol monophosphatase Corynebacterium glutamicum |
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