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

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...

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Veröffentlicht in:	Journal of bioscience and bioengineering 2014-11, Vol.118 (5), p.496-501
Hauptverfasser:	Sugawara, Asami, Matsui, Daisuke, Takahashi, Narumi, Yamada, Miwa, Asano, Yasuhisa, Isobe, Kimiyasu
Format:	Artikel
Sprache:	eng
Schlagworte:	Amino Acid Oxidoreductases - biosynthesis Amino Acid Oxidoreductases - chemistry Amino Acid Oxidoreductases - isolation & purification Amino Acid Oxidoreductases - metabolism Amino Acid Sequence Biological and medical sciences Biotechnology Burkholderia Burkholderia - enzymology Carboxy-Lyases - biosynthesis Carboxy-Lyases - chemistry Carboxy-Lyases - isolation & purification Carboxy-Lyases - metabolism Coenzymes - metabolism Decarboxylation Escherichia coli - genetics Escherichia coli - metabolism Fundamental and applied biological sciences. Psychology Isoelectric Point l-Amino acid decarboxylase l-Amino acid oxidase l-Lysine l-Lysine decarboxylase l-Lysine oxidase Lysine - metabolism Molecular Sequence Data Molecular Weight Oxidation-Reduction Protein Conformation Putrescine oxidase Pyridoxal Phosphate - metabolism Pyridoxal-5′-phosphate Substrate Specificity
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