The enzyme, characterized from the bacterium Arthrobacter sp. TS-15, acts on a broad range of different aryl-alkyl ketones, such as haloketones, ketoamines, diketones, and ketoesters. It accepts various types of aryl groups including phenyl-, pyridyl-, thienyl-, and furyl-rings, but the presence of an aromatic ring is essential for the activity. In addition, the presence of a functional group on the alkyl chain, such as an amine, a halogen, or a ketone, is also crucial. The enzyme exhibits a strict anti-Prelog enantioselectivity. When acting on diketones, it catalyses the reduction of only the keto group closest to the ring, with no further reduction to the diol. cf. EC 1.1.1.423, ephedrine dehydrogenase.
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The expected taxonomic range for this enzyme is: Arthrobacter sp.
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SYSTEMATIC NAME
IUBMB Comments
(+)-(1S,2S)-pseudoephedrine:NAD+ 1-oxoreductase
The enzyme, characterized from the bacterium Arthrobacter sp. TS-15, acts on a broad range of different aryl-alkyl ketones, such as haloketones, ketoamines, diketones, and ketoesters. It accepts various types of aryl groups including phenyl-, pyridyl-, thienyl-, and furyl-rings, but the presence of an aromatic ring is essential for the activity. In addition, the presence of a functional group on the alkyl chain, such as an amine, a halogen, or a ketone, is also crucial. The enzyme exhibits a strict anti-Prelog enantioselectivity. When acting on diketones, it catalyses the reduction of only the keto group closest to the ring, with no further reduction to the diol. cf. EC 1.1.1.423, ephedrine dehydrogenase.
34.6% of the activity as compared to methyl benzoylformate. (S)-Phenylacetylcarbinol is formed with more than 99% yield and more than 99% enantiomeric excess
the enzyme displays no apparent activity with NADP(H) and full catalytic activity with NAD(H). A model of the active site in complex with NAD+ and 1-phenyl-1,2-propanedione suggests key roles for S143 and W152 in recognition of the substrate and positioning for the reduction reaction
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
hanging-drop vapor diffusion method, the crystal structure of the enzyme-NAD+ complex, refined to a resolution of 1.83 A, reveales a tetrameric structure, which is confirmed by solution studies
the wide substrate spectrum of these dehydrogenases, combined with their regio- and enantioselectivity, suggests a high potential for the industrial production of valuable chiral compounds
the wide substrate spectrum of these dehydrogenases, combined with their regio- and enantioselectivity, suggests a high potential for the industrial production of valuable chiral compounds
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1.1.1.422 pseudoephedrine dehydrogenase
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