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An enzymatic activity in bovine brain that catalyzes the reversal of the C-terminal methyl esterification of protein phosphatase 2A.

Abstract：

:A novel protein methyltransferase has been recently described that catalyzes the esterification of the C-terminal leucine residue of the catalytic subunit of protein phosphatase 2A in a variety of eucaryotic cells. This reaction can potentially modulate the phosphatase's activity, subunit interactions, or interactions with specific phosphoprotein substrates. We present evidence here that the methylation reaction is reversible and that an enzymatic activity is present in bovine brain cytosol that catalyzes the hydrolysis of the methyl ester. We show that this activity is sensitive to inhibition by the serine-hydrolase inhibitor phenylmethanesulfonyl fluoride but is not affected by the small molecule substrate analog N-acetyl-L-leucine methyl ester. These results suggest that protein methylation and demethylation reactions can be utilized in eucaryotic cells to modulate enzyme activity in a parallel fashion to protein phosphorylation and dephosphorylation reactions.

journal_name

Biochem Biophys Res Commun

journal_title

Biochemical and biophysical research communications

authors

Xie H,Clarke S

doi

10.1006/bbrc.1994.2383

subject

Has Abstract

pub_date

1994-09-30 00:00:00

pages

1710-5

issue

3

eissn

0006-291X

issn

1090-2104

pii

S0006291X84723837

journal_volume

203

pub_type

杂志文章

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