Methylesterase

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Template:STRUCTURE 3uw0 Methylesterase (ME) removes a methyl group from the Υ-glutamyl methyl esther residues of methyl-accepting chemotaxis proteins. ME participates in several metabolic pathways. Protein phosphatase ME is involved in the reversible methylation of protein phosphatase 2A which is active in cellular regulation. 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.

Contents

3D structures of methylesterase

Updated on 19-August-2014

CheB methylesterase

1chd, 1a2o – ME – Salmonella typhimurium
3sft – TmME catalytic domain – Thermotoga maritima
3t8y – TmME response regulator domain

Pectin methylesterase

1qjv – EcME – Erwinia chrysanthemi
1gq8 – ME – carrot
3uw0 – ME – Yersinia enterocolitica
1xg2 – ME + protein inhibitor – Solanum lycopersicum
2nsp, 2nst, 2nt6, 2nt9 – EcME (mutant) + hexasaccharide
2ntp, 2ntb, 2ntq – EcME + hexasaccharide

Aclacinomycin methylesterase

1q0r, 1q0z – ME + product analog – Streptomyces purpurascens

Protein phosphatase methylesterase

3c5v – hME1 – human
3c5w – hME1 + protein phosphatase 2A

4-o-methyl-glucuronoyl methylesterase

4g4g – MtME – Myceliophthora thermophila
4g4i – MtME (mutant)
4g4j – MtME (mutant) + 4-o-methyl-β-D-glucopyranuronate

Proteopedia Page Contributors and Editors (what is this?)

Michal Harel, Alexander Berchansky

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