Methylesterase: Difference between revisions

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{{STRUCTURE_3uw0|  PDB=3uw0  | SIZE=400| SCENE= |right|CAPTION=Pectin methylesterase [[3uw0]] }}
<StructureSection load='3c5w' size='350' side='right' caption='Human protein phosphatase methylesterase (green) complex with protein phosphatase 2A subunit A (cyan) and subunit C (magenta) (PDB entry [[3c5w]])' scene='48/489289/Cv/1'>
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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.  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. 


==3D structures of methylesterase==
__TOC__
== 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.  <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 />
*  '''Aclacinomycin ME''' modifies the aklavinone skeleton in the biosynthesis of anthracyclins in ''Streptomyces'' species<ref>PMID:11934504</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 />


'''CheB methylesterase'''
== Structural highlights ==
*<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>.


[[1chd]], [[1a2o]] – ME – ''Salmonella typhimurium''<br />
==3D structures of methylesterase==
[[3sft]] – TmME catalytic domain – ''Thermotoga maritima''<br />
[[Methylesterase 3D structures]]
[[3t8y]] – TmME response regulator domain
 
'''Pectin methylesterase'''
 
[[1qjv]] – EcME – ''Erwinia chrysanthemi''<br />
[[1gq8]] – ME – carrot<br />
[[3uw0]] – ME – ''Yersinia enterocolitica''<br />
[[1xg2]] – ME + protein inhibitor – ''Solanum lycopersicum''<br />
[[2nsp]], [[2nst]], [[2nt6]], [[2nt9]] – EcME (mutant) + hexasaccharide<br />
[[2ntp]], [[2ntb]], [[2ntq]] – EcME + hexasaccharide
 
'''Aclacinomycin methylesterase'''
 
[[1q0r]], [[1q0z]] – ME + product analog – ''Streptomyces purpurascens''
 
'''Protein phosphatase methylesterase'''


[[3c5v]] – hME1 – human<br />
</StructureSection>
[[3c5w]] – hME1 + protein phosphatase 2A


== References ==
<references/>
[[Category:Topic Page]]
[[Category:Topic Page]]

Latest revision as of 13:21, 30 October 2019


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

  • .
  • . It inactivates phospholipase 2A by interacting with the latter's subunit C by removing two catalytic Mn+2 ions from it[6].

3D structures of methylesterase

Methylesterase 3D structures


Human protein phosphatase methylesterase (green) complex with protein phosphatase 2A subunit A (cyan) and subunit C (magenta) (PDB entry 3c5w)

Drag the structure with the mouse to rotate

ReferencesReferences

  1. ↑ 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
  2. ↑ Micheli F. Pectin methylesterases: cell wall enzymes with important roles in plant physiology. Trends Plant Sci. 2001 Sep;6(9):414-9. PMID:11544130
  3. ↑ 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
  4. ↑ 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
  5. ↑ 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
  6. ↑ 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

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