Methylesterase
From Proteopedia
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| - | + | <StructureSection load='3c5w' size='350' side='right' caption='Human protein phosphatase methylesterase (green) complex with protein phosphatase 2A subunit A (grey) and subunit C (pink) (PDB entry [[3c5w]])' scene=''> | |
| - | <StructureSection load='3c5w' size='350' side='right' caption='Human | + | == Function == |
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'''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 /> | '''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 /> | ||
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* '''Protein phosphatase ME''' is involved in the reversible methylation of protein phosphatase 2A which is active in cellular regulation<ref>PMID:24928782</ref>.<br /> | * '''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 /> | ||
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| + | == Structural highlights == | ||
| + | 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<ref>PMID:18394995</ref>. | ||
| + | </StructureSection> | ||
==3D structures of methylesterase== | ==3D structures of methylesterase== | ||
Revision as of 08:45, 27 April 2016
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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
- ↑ Xing Y, Li Z, Chen Y, Stock JB, Jeffrey PD, Shi Y. Structural mechanism of demethylation and inactivation of protein phosphatase 2A. Cell. 2008 Apr 4;133(1):154-63. PMID:18394995 doi:http://dx.doi.org/10.1016/j.cell.2008.02.041
