title: Cloning and characterization of fructosamine-6-kinase from Arthrobacter aurescens.
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.
authors.affiliation: Graduate School of Bionics, Computer and Media Sciences, Tokyo University of Technology, Hachioji, Japan.
authors.forename: Akane
authors.initials: A
authors.lastname: Sakaguchi-Mikami
authors.forename: Miho
authors.initials: M
authors.lastname: Kameya
authors.forename: Stefano
authors.initials: S
authors.lastname: Ferri
authors.forename: Wakako
authors.initials: W
authors.lastname: Tsugawa
authors.forename: Koji
authors.initials: K
authors.lastname: Sode
mesh_terms: D000595:Amino Acid Sequence; D001173:Arthrobacter / Q000201:enzymology*; D001426:Bacterial Proteins / Q000235:genetics* / Q000378:metabolism; D003001:Cloning, Molecular; D004926:Escherichia coli / Q000235:genetics; D008239:Lysine / Q000031:analogs & derivatives / Q000378:metabolism; D008969:Molecular Sequence Data; D017853:Phosphotransferases (Alcohol Group Acceptor) / Q000235:genetics* / Q000378:metabolism; D016415:Sequence Alignment; D013379:Substrate Specificity
chemical_list: D001426:Bacterial Proteins; C033186:fructosyl-lysine; D017853:Phosphotransferases (Alcohol Group Acceptor); D008239:Lysine