Historical review: the field of protein methylation.

Tissue distribution of carnitine biosynthetic enzymes in man.

Stoichiometric methylation of porcine adrenocorticotropin by protein carboxyl methyltransferase requires deamidation of asparagine 25. Evidence for methylation at the alpha-carboxyl group of atypical L-isoaspartyl residues.

Protein carboxyl methyltransferase facilitates conversion of atypical L-isoaspartyl peptides to normal L-aspartyl peptides.

Purification and molecular identification of two protein methylases I from calf brain. Myelin basic protein- and histone-specific enzyme.

A rapid method for the purification of S-adenosylmethionine: Protein-carboxyl O-methyltransferase by affinity chromatography

https://www.cell.com/trends/biochemical-sciences/pdf/0968-0004(77)90365-6.pdf

Carnitine biosynthesis via protein methylation

Effect of modification of inhibitory amino acids on arginase activity

Post-synthetic modifications of nuclear proteins, especially histones, are frequently investigated enigmatic reactions. The biological significance of these particular modification reactions is not thoroughly understood. The relatively high degree of evolutionary stability of the histone’s primary structure and to a large extent its modification sites suggests that proper chromatin organization depends a great deal on precise post-synthetic modification reactions. This idea is substantiated by a number of reports indicating that these reactions occur predominantly around the time that cells, in preparation for division, are replicating their chromosomes and processing newly synthesized histones.

Enzymatic modification of nuclear proteins during neoplastic growth.

Publisher Summary The enzymes responsible for methylating the lysine residues of proteins (protein–lysine methyltransferase) have been termed as “protein methylase III” or, more properly, S -adenosylmethionine. This enzyme has been found to be elevated in rapidly proliferating tissues. In mammalian cells, the enzyme is localized within the nucleus associated with the chromatin. Histones have been implicated as major protein substrates for the enzyme in studies performed on HeLa S -3 cells. The products of the reaction are ɛ- 4-mono-, ɛ - N -di, and ɛ - N -trimethyllysine. In bacteria, a ribosomal protein methylase III that is responsible for methylating predominantly the L-11 protein of the 50 S ribosomal subunit can be purified 380-fold. In this chapter, a protein methylase III is purified from Neurosporu crassa , which is responsible for methylating cytochrome c .

Samuel Nochumson

Papers

A rapid method for the purification of S-adenosylmethionine: Protein-carboxyl O-methyltransferase by affinity chromatography

Carnitine biosynthesis via protein methylation

Effect of modification of inhibitory amino acids on arginase activity

Enzymatic modification of nuclear proteins during neoplastic growth.

The methylation and demethylation of protein lysine residues.