Cloning and Characterization of Fructosamine-6-Kinase from Arthrobacter aurescens |
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Authors: | Akane Sakaguchi-Mikami Miho Kameya Stefano Ferri Wakako Tsugawa Koji Sode |
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Affiliation: | 1. Graduate School of Bionics, Computer and Media Sciences, Tokyo University of Technology, Hachioji, Japan 2. Department of Biotechnology, Graduate School of Engineering, Tokyo University of Agriculture and Technology, Koganei, Japan 3. Department of Technology Risk Management, Graduate School of Technology Management, Tokyo University of Agriculture and Technology, Tokyo, Japan
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Abstract: | Fructosamine-6-kinases (FN6Ks) that catalyze phosphorylation of glycated amino acids, i.e., fructosyl amino acids (FAs), have been shown as a potential recognition element for glycated protein detection. However, there are only two available FN6Ks: those from Escherichia coli which is specific for ε-fructosyl lysine (ε-FK) and Bacillus subtilis which recognizes both ε-FK and α-FA as substrates. In this study, we characterized an FN6K homologue isolated from Arthrobacter, some of whose species are reported to assimilate FA. The BLAST searches of Arthrobacter genomic database, using the bacterial FN6K primary structure information, revealed the presence of an FN6K homologue in Arthrobacter aurescens TC1 strain. Indeed, enzymatic assays confirmed that the putative FN6K from A. aurescens is an FN6K that is specific for ε-FK, although the primary sequence alignments showed similarity of A. aurescens FN6Ks with FN6Ks from B. subtilis and E. coli at the same level. In this study, we describe for the first time the presence of FN6K in Arthrobacter spp. and ε-FK-specific degradation pathway from Gram-positive bacteria, providing important information for the development of FA-recognizing molecules as well as for the FA assimilation system in bacteria. |
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