Methylesterase

spinqualitylabelsall models Human protein phosphatase methylesterase (green) complex with protein phosphatase 2A subunit A (cyan) and subunit C (magenta) (PDB entry 3c5w) Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Function Methylesterase (ME) or pectinesterase removes a methyl group from the Υ-glutamyl methyl esther residues of methyl-accepting chemotaxis proteins. ME participates in several metabolic pathways. CheB ME is a phosphorylation-activated response regulator involved in reversible modification of bacterial chemotaxis receptors. See Chemotaxis protein. Pectin ME causes demethylation of cell wall polygalactorunanas. It is involved in pectin digestion. The reaction products liberate frothing agents causing bloating in cattle. Aclacinomycin ME modifies the aklavinone skeleton in the biosynthesis of anthracyclins in Streptomyces species. Protein phosphatase ME is involved in the reversible methylation of protein phosphatase 2A which is active in cellular regulation. 4-o-methyl-glucuronoyl ME has a significant role in biomass degradation. Structural highlights Human protein phosphatase methylesterase with protein phosphatase 2A subunits A and C. Protein phosphatase ME binds to the active site of subunit C of phospholipase 2A. It inactivates phospholipase 2A by interacting with the latter's subunit C by removing two catalytic Mn+2 ions from it. 3D structures of methylesterase Methylesterase 3D structures

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