Protein phosphatase methylesterase-1

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Protein phosphatase methylesterase-1
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EC no. 3.1.1.89
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The enzyme protein phosphatase methylesterase-1 (EC 3.1.1.89, PME-1, PPME1; systematic name (phosphatase 2A protein)-leucine ester acylhydrolase [1] [2] catalyses the reaction

[phosphatase 2A protein]-leucine methyl ester + H2O [phosphatase 2A protein]-leucine + methanol

A key regulator of protein phosphatase 2A.

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(phosphatase 2A protein)-leucine-carboxy methyltransferase is an enzyme with systematic name S-adenosyl-L-methionine:(phosphatase 2A protein)-leucine O-methyltransferase. This enzyme catalyses the following chemical reaction

Protein methylation is a type of post-translational modification featuring the addition of methyl groups to proteins. It can occur on the nitrogen-containing side-chains of arginine and lysine, but also at the amino- and carboxy-termini of a number of different proteins. In biology, methyltransferases catalyze the methylation process, activated primarily by S-adenosylmethionine. Protein methylation has been most studied in histones, where the transfer of methyl groups from S-adenosyl methionine is catalyzed by histone methyltransferases. Histones that are methylated on certain residues can act epigenetically to repress or activate gene expression.

References

  1. Ogris E, Du X, Nelson KC, Mak EK, Yu XX, Lane WS, Pallas DC (May 1999). "A protein phosphatase methylesterase (PME-1) is one of several novel proteins stably associating with two inactive mutants of protein phosphatase 2A". The Journal of Biological Chemistry. 274 (20): 14382–91. doi: 10.1074/jbc.274.20.14382 . PMC   3503312 . PMID   10318862.
  2. Xing Y, Li Z, Chen Y, Stock JB, Jeffrey PD, Shi Y (April 2008). "Structural mechanism of demethylation and inactivation of protein phosphatase 2A". Cell. 133 (1): 154–63. doi: 10.1016/j.cell.2008.02.041 . PMID   18394995.