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B6db references: 24863180

type Journal Article
authors Sugawara A, Matsui D, Takahashi N, Yamada M, Asano Y, Isobe K
title Characterization of a pyridoxal-5'-phosphate-dependent l-lysine decarboxylase/oxidase from Burkholderia sp. AIU 395
journal J Biosci Bioeng
sel selected
ui 24863180
year (2010)
volume 118
number 5
pages 496-501
keywords Burkholderia; Putrescine oxidase; Pyridoxal-5′-phosphate; l-Amino acid decarboxylase; l-Amino acid oxidase; l-Lysine; l-Lysine decarboxylase; l-Lysine oxidase
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.
last changed 2018/05/21 14:02

B6db references