By a News Reporter-Staff News Editor at Biotech Week -- A new study on Enzymes and Coenzymes is now available. According to news reporting originating in Montreal, Canada, by NewsRx journalists, research stated, "The great importance of amide bonds in industrial synthesis has encouraged the search for efficient catalysts of amide bond formation. Microbial transglutaminase (MTG) is heavily utilized in crosslinking proteins in the food and textile industries, where the side chain of a glutamine reacts with the side chain of a lysine, forming a secondary amide bond."
The news reporters obtained a quote from the research from the University of Montreal, "Long alkylamines carrying diverse chemical entities can substitute for lysine as acyl-acceptor substrates, to link molecules of interest onto peptides or proteins. Here, we explore short and chemically varied acyl-acceptor substrates, to better understand the nature of nonnatural substrates that are tolerated by MTG, with the aim of diversifying biocatalytic applications of MTG. We show, for the first time, that very short-chain alkyl-based amino acids such as glycine can serve as acceptor substrates. The esterified alpha-amino acids Thr, Ser, Cys, and Trp-but not Ile-also showed reactivity. Extending the search to nonnatural compounds, a ring near the amine group-particularly if aromatic-was beneficial for reactivity, although ring substituents reduced reactivity. Overall, amines attached to a less hindered carbon increased reactivity. Importantly, very small amines carrying either the electron-rich azide or the alkyne groups required for click chemistry were highly reactive as acyl-acceptor substrates, providing a robust route to minimally modified, 'clickable' peptides."
According to the news reporters, the research concluded: "These results demonstrate that MTG is tolerant to a variety of chemically varied natural and nonnatural acyl-acceptor substrates, which broadens the scope for modification of Gln-containing peptides and proteins."
For more information on this research see: Microbial transglutaminase displays broad acyl-acceptor substrate specificity. Applied Microbiology and Biotechnology, 2014;98(1):219-230. Applied Microbiology and Biotechnology can be contacted at: Springer, 233 Spring St, New York, NY 10013, USA. (Springer - www.springer.com; Applied Microbiology and Biotechnology - www.springerlink.com/content/0175-7598/)
Our news correspondents report that additional information may be obtained by contacting M.T. Gundersen, University of Montreal, Dept. of Chim, Montreal, PQ H3C 3J7, Canada. Additional authors for this research include J.W. Keillor and J.N. Pelletier (see also Enzymes and Coenzymes).
Keywords for this news article include: Quebec, Canada, Montreal, Peptides, Proteins, Proteomics, Amino Acids, Transglutaminases, Aminoacyltransferases, Enzymes and Coenzymes, North and Central America
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