title: Isolation and characterization of a fructosyl-amine oxidase from an Arthrobacter sp.
abstract: An Arthrobacter sp. was isolated that, when induced by fructosyl-valine, expressed a fructosyl-amine oxidase (FAOD) that was specific for alpha-glycated amino acids. The N-terminal amino acid sequence of the purified oxidase was determined and used to design oligonucleotides to amplify the gene by inverse PCR. Expression of the gene in Escherichia coli produced 0.23 units FAOD per mg protein, over 30-fold greater than native expression levels, with properties almost indistinguishable from the native enzyme. The presence of FAOD was confirmed in other Arthrobacter ssp.
authors.affiliation: Department of Biotechnology, Tokyo University of Agriculture and Technology, 2-24-16 Naka-cho, 184-8588, Tokyo, Koganei, Japan.
authors.forename: Stefano
authors.initials: S
authors.lastname: Ferri
authors.forename: Akane
authors.initials: A
authors.lastname: Sakaguchi
authors.forename: Hiroki
authors.initials: H
authors.lastname: Goto
authors.forename: Wakako
authors.initials: W
authors.lastname: Tsugawa
authors.forename: Koji
authors.initials: K
authors.lastname: Sode
mesh_terms: D000594:Amino Acid Oxidoreductases / Q000737:chemistry / Q000235:genetics / Q000302:isolation & purification* / Q000378:metabolism; D000595:Amino Acid Sequence; D000818:Animals; D001173:Arthrobacter / Q000201:enzymology*; D001483:Base Sequence; D015374:Biosensing Techniques; D004926:Escherichia coli / Q000235:genetics; D008969:Molecular Sequence Data; D011994:Recombinant Proteins / Q000737:chemistry / Q000235:genetics / Q000302:isolation & purification / Q000378:metabolism; D017386:Sequence Homology, Amino Acid
chemical_list: D011994:Recombinant Proteins; D000594:Amino Acid Oxidoreductases