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- W2079841870 abstract "Microbial transglutaminase (EC 2.3.2.13) (mTGase) catalyses a calcium-independent acyl-transfer reaction in which ɛ-(γ-glutamyl)lysine bonds are formed using the γ-carboxyamide groups of peptide-bound glutamine residues and the amino group of lysine side-chains. Here we present a comparative study on alternative lysine and glutamine substitutes in mTGase catalysis. A homologous series of ω-amino acids, serving as lysine substitutes, was incorporated into carbobenzoxy-l-glutaminylglycine (CBZ-Gln-Gly). The rate constants and particular conversion rates increased with increasing chain length. As for the glutamine substitutes, adipic diamide, glutaric monoamide, and glutaric diamide were converted with monodansylcadaverine (DNS-cadaverine) under mTGase catalysis. For the synthetic glutamine substitutes, the substrates of natural chain length, glutaric mono- and diamide, are better converted than the longer adipic diamide indicating that the window of opportunity seems to be smaller. Synthetic substrates, serving as amine acceptors, offer new opportunities in the field of transglutaminase-catalysed reactions." @default.
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- W2079841870 date "2009-05-01" @default.
- W2079841870 modified "2023-09-24" @default.
- W2079841870 title "Synthetic substrates as amine donors and acceptors in microbial transglutaminase-catalysed reactions" @default.
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- W2079841870 doi "https://doi.org/10.1016/j.molcatb.2008.09.010" @default.
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