Abstract
Posttranslational side-chain modification reactions of protein constitute one of the most rapidly developing and exciting frontiers in modern biologic science. These reactions are accomplished at an expense of energy equivalent to 1 mole of adenosine triphosphate (ATP), and evidence indicates that these modifications of protein side-chain structures are accompanied by simultaneous alterations of the protein function. The posttranslational side-chain modification reactions of protein might be one of the nature's most efficient means to manipulate the protein function by bypassing the elaborate and energy-consuming protein de novo biosynthetic pathway. One such side-chain modification reaction of protein, protein methylation, occurs ubiquitously in nature, in organisms ranging from prokaryotic to eukaryotic, and involves side chains of various amino acids, such as lysine, arginine, histidine, alanine, proline, and glutamine, for N -methylation and glutamic and aspartic acid for O -methylesterification. Among these amino acid residues, the enzymatic methylation of lysine, arginine, histidine, and glutamic acid residues have been investigated.
Sign-in/Register to access full text options 
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a callDisclaimer: All third-party content on this website/platform is and will remain the property of their respective owners and is provided on "as is" basis without any warranties, express or implied. Use of third-party content does not indicate any affiliation, sponsorship with or endorsement by them. Any references to third-party content is to identify the corresponding services and shall be considered fair use under The CopyrightLaw.
