Methylesterase
From Proteopedia
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{{STRUCTURE_3uw0| PDB=3uw0 | SIZE=400| SCENE= |right|CAPTION=Pectin methylesterase [[3uw0]] }} | {{STRUCTURE_3uw0| PDB=3uw0 | SIZE=400| SCENE= |right|CAPTION=Pectin methylesterase [[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. | + | '''Methylesterase''' (ME) removes a methyl group from the Υ-glutamyl methyl esther residues of methyl-accepting chemotaxis proteins. ME participates in several metabolic pathways. <br /> |
* '''CheB ME''' is a phosphorylation-activated response regulator involved in reversible modification of bacterial chemotaxis receptors<ref>PMID:2991277</ref>. See [[Chemotaxis protein]].<br /> | * '''CheB ME''' is a phosphorylation-activated response regulator involved in reversible modification of bacterial chemotaxis receptors<ref>PMID:2991277</ref>. See [[Chemotaxis protein]].<br /> | ||
* '''Pectin ME''' causes demethylation of cell wall polygalactorunanas. It is involved in pectin digestion. The reaction products liberate frothing agents causing bloating in cattle<ref>PMID:11544130</ref>.<br /> | * '''Pectin ME''' causes demethylation of cell wall polygalactorunanas. It is involved in pectin digestion. The reaction products liberate frothing agents causing bloating in cattle<ref>PMID:11544130</ref>.<br /> | ||
* '''Aclacinomycin ME''' modifies the aklavinone skeleton in the biosynthesis of anthracyclins in ''Streptomyces'' species<ref>PMID:11934504</ref>. <br /> | * '''Aclacinomycin ME''' modifies the aklavinone skeleton in the biosynthesis of anthracyclins in ''Streptomyces'' species<ref>PMID:11934504</ref>. <br /> | ||
| - | * '''Protein phosphatase ME''' is | + | * '''Protein phosphatase ME''' is involved in the reversible methylation of protein phosphatase 2A which is active in cellular regulation<ref>PMID:24928782</ref>.<br /> |
* '''4-o-methyl-glucuronoyl ME''' has a significant role in biomass degradation<ref>PMID:16876163</ref>.<br /> | * '''4-o-methyl-glucuronoyl ME''' has a significant role in biomass degradation<ref>PMID:16876163</ref>.<br /> | ||
Revision as of 08:08, 27 April 2016
Methylesterase (ME) 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[1]. 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[2].
- Aclacinomycin ME modifies the aklavinone skeleton in the biosynthesis of anthracyclins in Streptomyces species[3].
- Protein phosphatase ME is involved in the reversible methylation of protein phosphatase 2A which is active in cellular regulation[4].
- 4-o-methyl-glucuronoyl ME has a significant role in biomass degradation[5].
3D structures of methylesterase
Updated on 27-April-2016
References
- ↑ Simms SA, Keane MG, Stock J. Multiple forms of the CheB methylesterase in bacterial chemosensing. J Biol Chem. 1985 Aug 25;260(18):10161-8. PMID:2991277
- ↑ Micheli F. Pectin methylesterases: cell wall enzymes with important roles in plant physiology. Trends Plant Sci. 2001 Sep;6(9):414-9. PMID:11544130
- ↑ Wang Y, Niemi J, Mantsala P. Modification of aklavinone and aclacinomycins in vitro and in vivo by rhodomycin biosynthesis gene products. FEMS Microbiol Lett. 2002 Feb 19;208(1):117-22. PMID:11934504
- ↑ Wandzioch E, Pusey M, Werda A, Bail S, Bhaskar A, Nestor M, Yang JJ, Rice LM. PME-1 modulates protein phosphatase 2A activity to promote the malignant phenotype of endometrial cancer cells. Cancer Res. 2014 Aug 15;74(16):4295-305. doi: 10.1158/0008-5472.CAN-13-3130. Epub, 2014 Jun 13. PMID:24928782 doi:http://dx.doi.org/10.1158/0008-5472.CAN-13-3130
- ↑ Spanikova S, Biely P. Glucuronoyl esterase--novel carbohydrate esterase produced by Schizophyllum commune. FEBS Lett. 2006 Aug 21;580(19):4597-601. Epub 2006 Jul 21. PMID:16876163 doi:http://dx.doi.org/10.1016/j.febslet.2006.07.033
