Purification and analysis of a flavoprotein functional as NADH oxidase from Amphibacillus xylanus overexpressed in Escherichia coli

The gene encoding the Amphibacillus xylanus flavoprotein has been cloned into pTTQ18 and overexpressed in Escherichia coli. The recombinant enzyme has been purified to homogeneity yielding 15 mg of pure enzyme/liter of cell culture. Recombinant flavoprotein is fully active and has an absorption spec...

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Veröffentlicht in:	The Journal of biological chemistry 1994-12, Vol.269 (50), p.31418-31423
Hauptverfasser:	Ohnishi, K, Niimura, Y, Yokoyama, K, Hidaka, M, Masaki, H, Uchimura, T, Suzuki, H, Uozumi, T, Kozaki, M, Komagata, K, Nishino, T
Format:	Artikel
Sprache:	eng
Schlagworte:	Amino Acid Sequence Bacteria - enzymology Catalysis Cysteine - analysis Dithionite - chemistry Escherichia coli Flavins - metabolism Flavoproteins - isolation & purification Kinetics Metals - analysis Molecular Sequence Data Multienzyme Complexes - genetics Multienzyme Complexes - isolation & purification NAD - metabolism NADH, NADPH Oxidoreductases - genetics NADH, NADPH Oxidoreductases - isolation & purification Oxidation-Reduction Recombinant Proteins - isolation & purification Recombinant Proteins - metabolism Sequence Alignment Sequence Homology, Amino Acid Thioredoxin-Disulfide Reductase - chemistry
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