کد مقاله کد نشریه سال انتشار مقاله انگلیسی نسخه تمام متن
20380 43172 2014 6 صفحه PDF دانلود رایگان
عنوان انگلیسی مقاله ISI
Characterization of a pyridoxal-5′-phosphate-dependent l-lysine decarboxylase/oxidase from Burkholderia sp. AIU 395
موضوعات مرتبط
مهندسی و علوم پایه مهندسی شیمی بیو مهندسی (مهندسی زیستی)
پیش نمایش صفحه اول مقاله
Characterization of a pyridoxal-5′-phosphate-dependent l-lysine decarboxylase/oxidase from Burkholderia sp. AIU 395
چکیده انگلیسی

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.

ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Journal of Bioscience and Bioengineering - Volume 118, Issue 5, November 2014, Pages 496–501
نویسندگان
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