title: Characterization of a pyridoxal-5'-phosphate-dependent l-lysine decarboxylase/oxidase from Burkholderia sp. AIU 395.
abstract: A novel enzyme, which catalyzed decarboxylation of l-lysine into cadaverine with release of carbon dioxide and oxidative deamination of l-lysine into l-2-aminoadipic 5-semialdehyde with release of ammonia and hydrogen peroxide, was found from a newly isolated Burkholderia sp. AIU 395. The enzyme was specific to l-lysine and did not exhibit enzyme activities for other l-amino acids, l-lysine derivatives, d-amino acids, and amines. The apparent Km values for l-lysine in the oxidation and decarboxylation reactions were estimated to be 0.44 mM and 0.84 mM, respectively. The molecular mass was estimated to be 150 kDa, which was composed of two identical subunits with molecular mass of 76.5 kDa. The enzyme contained one mol of pyridoxal 5'-phosphate per subunit as a prosthetic group. The enzyme exhibiting decarboxylase and oxidase activities for l-lysine was first reported here, while the deduced amino acid sequence was homologous to that of putative lysine decarboxylases from the genus Burkholderia.
authors.affiliation: Department of Biological Chemistry and Food Science, Faculty of Agriculture, Iwate University, 3-18-8 Ueda, Morioka 020-8550, Japan.
authors.forename: Asami
authors.initials: A
authors.lastname: Sugawara
authors.affiliation: Biotechnology Research Center and Department of Biotechnology, Toyama Prefectural University, 5180 Kurokawa, Imizu, Toyama 939-0398, Japan; Asano Active Enzyme Molecule Project, ERATO, JST, 5180 Kurokawa, Imizu, Toyama 939-0398, Japan.
authors.forename: Daisuke
authors.initials: D
authors.lastname: Matsui
authors.affiliation: Department of Biological Chemistry and Food Science, Faculty of Agriculture, Iwate University, 3-18-8 Ueda, Morioka 020-8550, Japan.
authors.forename: Narumi
authors.initials: N
authors.lastname: Takahashi
authors.affiliation: Department of Biological Chemistry and Food Science, Faculty of Agriculture, Iwate University, 3-18-8 Ueda, Morioka 020-8550, Japan.
authors.forename: Miwa
authors.initials: M
authors.lastname: Yamada
authors.affiliation: Biotechnology Research Center and Department of Biotechnology, Toyama Prefectural University, 5180 Kurokawa, Imizu, Toyama 939-0398, Japan; Asano Active Enzyme Molecule Project, ERATO, JST, 5180 Kurokawa, Imizu, Toyama 939-0398, Japan.
authors.forename: Yasuhisa
authors.initials: Y
authors.lastname: Asano
authors.affiliation: Department of Biological Chemistry and Food Science, Faculty of Agriculture, Iwate University, 3-18-8 Ueda, Morioka 020-8550, Japan. Electronic address: kiso@iwate-u.ac.jp.
authors.forename: Kimiyasu
authors.initials: K
authors.lastname: Isobe
mesh_terms: D000594:Amino Acid Oxidoreductases / Q000096:biosynthesis / Q000737:chemistry / Q000302:isolation & purification / Q000378:metabolism*; D000595:Amino Acid Sequence; D019117:Burkholderia / Q000201:enzymology*; D002262:Carboxy-Lyases / Q000096:biosynthesis / Q000737:chemistry / Q000302:isolation & purification / Q000378:metabolism*; D003067:Coenzymes / Q000378:metabolism; D003653:Decarboxylation; D004926:Escherichia coli / Q000235:genetics / Q000378:metabolism; D007526:Isoelectric Point; D008239:Lysine / Q000378:metabolism; D008969:Molecular Sequence Data; D008970:Molecular Weight; D010084:Oxidation-Reduction; D011487:Protein Conformation; D011732:Pyridoxal Phosphate / Q000378:metabolism*; D013379:Substrate Specificity
chemical_list: D003067:Coenzymes; D011732:Pyridoxal Phosphate; D000594:Amino Acid Oxidoreductases; C041123:L-lysine oxidase; D002262:Carboxy-Lyases; C021520:lysine decarboxylase; D008239:Lysine
keywords: Burkholderia; Putrescine oxidase; Pyridoxal-5′-phosphate; l-Amino acid decarboxylase; l-Amino acid oxidase; l-Lysine; l-Lysine decarboxylase; l-Lysine oxidase