Isolation and characterization of a fructosyl-amine oxidase from an Arthrobacter sp.
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.
Ferri
Stefano
S
Department of Biotechnology, Tokyo University of Agriculture and Technology, 2-24-16 Naka-cho, 184-8588, Tokyo, Koganei, Japan.
Sakaguchi
Akane
A
Goto
Hiroki
H
Tsugawa
Wakako
W
Sode
Koji
K
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
D011994:Recombinant Proteins; D000594:Amino Acid Oxidoreductases