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Characterization of a pyridoxal-5′-phosphate-dependent l-lysine decarboxylase/oxidase from Burkholderia sp. AIU 395

Paper ID Volume ID Publish Year Pages File Format Full-Text
20380 43172 2014 6 PDF Available
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.

Keywords
l-Amino acid oxidase; l-Amino acid decarboxylase; Putrescine oxidase; l-Lysine oxidase; l-Lysine decarboxylase; l-Lysine; Pyridoxal-5′-phosphate; Burkholderia
First Page Preview
Characterization of a pyridoxal-5′-phosphate-dependent l-lysine decarboxylase/oxidase from Burkholderia sp. AIU 395
Publisher
Database: Elsevier - ScienceDirect
Journal: Journal of Bioscience and Bioengineering - Volume 118, Issue 5, November 2014, Pages 496–501
Authors
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Subjects
Physical Sciences and Engineering Chemical Engineering Bioengineering