Structural analysis and molybdenum‐dependent expression of the pAO1‐encoded nicotine dehydrogenase genes of Arthrobacter nicotinovorans
作者： Susanne Grether-Beck , Gabor L. Igloi , Stefan Pust , Emil Schilz , Karl Decker
DOI: 10.1111/J.1365-2958.1994.TB00484.X
关键词: Molybdopterin 、 Biochemistry 、 Gene cluster 、 Homology (biology) 、 Nicotine dehydrogenase 、 Cofactor 、 Protein subunit 、 Xanthine dehydrogenase 、 Protein primary structure 、 Molecular biology 、 Biology
摘要: The genes of nicotine dehydrogenase (NDH) were identified, cloned and sequenced from the catabolic plasmid pAO1 Arthrobacter nicotinovorans. In immediate proximity to this gene cluster is beginning 6-hydroxy-L-niotine oxidase (6-HLNO) gene. NDH composed three subunits (A, B C) M(r) 30,011, 14,924 87,677. It belongs a family bacterial hydroxylases with similar subunit structure; they have molybdopterin dinucleotide, FAD Fe-S clusters as cofactors. Here first complete primary structure hydroxylase provided. Sequence alignments each show similarities sequences eukaryotic xanthine (XDH) but not other known molybdenum-containing enzymes. Based on alignment XDH it inferred that smallest (NDHB) carries an iron-sulphur cluster, middle-sized (NDHA) binds FAD, largest (NDHC) corresponds molybdopterin-binding domain XDH. Expression both ndh 6-hino required presence molybdenum in culture medium. Tungsten inhibited enzyme activity synthesis protein. was found A. nicotinovorans cells soluble form membrane-associated form. tungsten fraction increased.
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