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Characterization and biochemical investigation of the potential inositol monophosphate phosphatase involved in bacterial mycothiol biosynthesis
Authors:Yuchuan Guo  Wei Gong  Lizhen Wang  Jiatong Guo  Guoxia Jin
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
Abstract:Abstract

Mycothiol (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.
Keywords:Mycothiol  MshA2  Cg0911  inositol monophosphatase  Corynebacterium glutamicum
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