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PubMed · 955034

Labile protein-methyl ester: comparison between chemically and enzymatically synthesized.

S Kim·W K Paik
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Abstract

The rate of hydrolysis of protein-methyl ester, the enzymatic product of S-adenosylmethionine: protein-carboxyl methyltransferase (EC.2.1.1.24) acting on oxidized ribonuclease, was measured at pH 7.1 and 8.6 at 37 degrees C. The half-life of the hydrolysis of the ester is 25 min at pH 7.1, and 4 min at 8.6. The rate of hydrolysis of the enzymatically formed esters at pH 7.0, in 0.1 M phosphate buffer, was about 25 times faster than that of esters formed chemically by reaction with methanol in HCl. The lability of the enzymatically synthesized protein-methyl ester suggests that the esterification is specific to sites such that ionization of neighboring amino acid side chains enhances the rate of the hydrolysis.

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Aspartic AcidEstersGlutamatesHydrolysisMethylationMethyltransferasesRibonucleasesComparative StudyJournal ArticleResearch Support, U.S. Gov't, P.H.S.

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S Kim, W K Paik. 1976-08-15. Labile protein-methyl ester: comparison between chemically and enzymatically synthesized.. https://doi.org/10.1007/bf01933924

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