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KMID : 0624620080410110790
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BMB Reports
2008 Volume.41 No. 11 p.790 ~ p.795
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Molecular characterization of lysine 6-dehydrogenase from Achromobacter denitrificans
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Ruldeekulthamrong Prakarn
Maeda Sayaka
Kato Shin-ichiro
Shinji Nagata
Sittipraneed Siriporn
Packdibamrung Kanoktip
Misono Haruo
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Abstract
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An inducible lysine 6-dehydrogenase (Lys 6-DH), which catalyzes the oxidative deamination of the 6-amino group of L-lysine in the presence of NAD+, was purified to homogeneity from Achromobacter denitrificans, yielding a homodimeric protein of 80 kDa. The enzyme was specific for the substrate L-lysine and NAD+ served as a cofactor. The dimeric enzyme associated into a hexamer in the presence of 10 mM L-lysine. The Km values for L-lysine andNAD+ were 5.0 and 0.09 mM, respectively. The lys 6-dh gene was cloned and overexpressed in E. coli. The open reading frame was 1,107 nucleotides long and encoded a peptide containing 368 amino acids with 39,355 Da. The recombinant enzyme was purified to homogeneity and characterized. Enzyme activities and kinetic properties of the recombinant enzyme were almost the same as those of the endogenous enzyme obtained from A. denitrificans. Crystals of the enzyme were obtained using the hanging drop method.
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KEYWORD
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Achromobacter denitrificans, Delta-1-piperideine-6-carboxylate, DQ165182, Lysine 6-dehydrogenase
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