A structural and computational study of citrulline in biochemical reactions
Citrulline, a non-essential amino acid, is used therapeutically in mitochondrial diseases, especially since it is a well-tolerated medicinal compound. Athletes use citrulline to enhance performance during sustained exercise activity. In the body, citrullination is an important biochemical reaction in proteins which involves post-translational hydrolysis of arginine residues to form citrulline residues and ammonia. Proteins modified through extensive citrullination play a key role in the pathogenesis of a variety of diseases such as multiple sclerosis, autoimmune disorders, and potentially cancer. In our studies, we describe the experimental results of a structure determination using highly accurate X-ray data that were collected at low temperature (125 K). Through intensive crystallization studies, we obtained the delta polymorph of citrulline. There are seven strong N-H…O hydrogen bonds, an unusually high number for a small molecule. We utilized computational methods to understand the complex biochemistry of citrulline/arginine. Our DFT investigation offers clues for describing and understanding the complex biochemistry of citrulline/arginine. In addition, it is evident that the hydrolysis of arginine to citrulline is energetically favored and can be considered a driving force for important citrullination reactions.
Publisher URL: https://link.springer.com/article/10.1007/s11224-017-0996-x
Keeping up-to-date with research can feel impossible, with papers being published faster than you'll ever be able to read them. That's where Researcher comes in: we're simplifying discovery and making important discussions happen. With over 19,000 sources, including peer-reviewed journals, preprints, blogs, universities, podcasts and Live events across 10 research areas, you'll never miss what's important to you. It's like social media, but better. Oh, and we should mention - it's free.
Researcher displays publicly available abstracts and doesn’t host any full article content. If the content is open access, we will direct clicks from the abstracts to the publisher website and display the PDF copy on our platform. Clicks to view the full text will be directed to the publisher website, where only users with subscriptions or access through their institution are able to view the full article.