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| *<scene name='48/489289/Cv/6'>Human protein phosphatase methylesterase with protein phosphatase 2A subunits A and C</scene>. | | *<scene name='48/489289/Cv/6'>Human protein phosphatase methylesterase with protein phosphatase 2A subunits A and C</scene>. |
| *<scene name='48/489289/Cv/5'>Protein phosphatase ME binds to the active site of subunit C of phospholipase 2A</scene>. 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>. | | *<scene name='48/489289/Cv/5'>Protein phosphatase ME binds to the active site of subunit C of phospholipase 2A</scene>. 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>. |
| | |
| | ==3D structures of methylesterase== |
| | [[Methylesterase 3D structures]] |
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| </StructureSection> | | </StructureSection> |
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| **[[4g4i]] – MtME (mutant)<br /> | | **[[4g4i]] – MtME (mutant)<br /> |
| **[[4g4j]] – MtME (mutant) + 4-o-methyl-β-D-glucopyranuronate<br /> | | **[[4g4j]] – MtME (mutant) + 4-o-methyl-β-D-glucopyranuronate<br /> |
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| | *Methylesterase 5 or a-hydroxynitrile lyase |
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| | **[[6cob]], [[6cof]] – AtME5 (mutant) – ''Arabidopsis thaliana''<br /> |
| | **[[6coc]], [[6cod]], [[6cog]] – AtME5 (mutant) + benzaldehyde<br /> |
| | **[[6coe]], [[6coh]] – AtME5 (mutant) + benzaldehyde + mandelic acid nitrile<br /> |
| | **[[6coi]] – AtME5 (mutant) + benzaldehyde + mandelic acid nitrile + CN<br /> |
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| *CheB methylesterase see [[Chemotaxis protein]] | | *CheB methylesterase see [[Chemotaxis protein]] |
| Function
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].
Structural highlights
3D structures of methylesterase
Methylesterase 3D structures
- ↑ 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:https://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:https://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:https://dx.doi.org/10.1016/j.cell.2008.02.041
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3D structures of methylesterase
Updated on 30-October-2019
{"openlevels":0}
- Pectin methylesterase
- 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
- Methylesterase 5 or a-hydroxynitrile lyase
- 6cob, 6cof – AtME5 (mutant) – Arabidopsis thaliana
- 6coc, 6cod, 6cog – AtME5 (mutant) + benzaldehyde
- 6coe, 6coh – AtME5 (mutant) + benzaldehyde + mandelic acid nitrile
- 6coi – AtME5 (mutant) + benzaldehyde + mandelic acid nitrile + CN
- CheB methylesterase see Chemotaxis protein
References
