Labile protein-methyl ester: comparison between chemically and enzymatically synthesized.
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.
D001224:Aspartic Acid / Q000031:analogs & derivatives; D004952:Esters; D005971:Glutamates; D006868:Hydrolysis; D008745:Methylation; D008780:Methyltransferases / Q000378:metabolism*; D012260:Ribonucleases
D004952:Esters; D005971:Glutamates; D001224:Aspartic Acid; D008780:Methyltransferases; D012260:Ribonucleases