The enzyme isolated from the methanogenic archaea Methanogenium liminatans catalyses the reversible oxidation of various secondary and cyclic alcohols to the corresponding ketones.
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SYSTEMATIC NAME
IUBMB Comments
secondary-alcohol:coenzyme F420 oxidoreductase
The enzyme isolated from the methanogenic archaea Methanogenium liminatans catalyses the reversible oxidation of various secondary and cyclic alcohols to the corresponding ketones.
activity with ethanol or 1-propanol at the same concentration is only 0.1% compared to activity with 2-propanol. Acetaldehyde and propionaldehyde are reduced at the same rate as 2-propanone
the enzyme catalysed the oxidation of various secondary and cyclic alcohols to the corresponding ketones and the reverse reaction. No primary alcohols are oxidized. 1,3-butandiol, glycerol, methanol, ethanol, 1,2-ethandiol, 1 -propanol, 1-amino-2-propanol, 1-butanol, 1-pentanol, 1-hexanol and benzylalcohol are not oxidized nor are the respective aldehydes or ketones reduced
the enzyme catalysed the oxidation of various secondary and cyclic alcohols to the corresponding ketones and the reverse reaction. No primary alcohols are oxidized. 1,3-butandiol, glycerol, methanol, ethanol, 1,2-ethandiol, 1 -propanol, 1-amino-2-propanol, 1-butanol, 1-pentanol, 1-hexanol and benzylalcohol are not oxidized nor are the respective aldehydes or ketones reduced
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
hanging drop vapor diffusion method, crystal structure of the enzyme at 1.8 A resolution in complex with a F420-acetone adduct. The position of F420and isopropanol defines the active site for hydride transfer in the interior of Adf that is completely shielded from bulk solvent. The distance of 2.9 A between the C2 atom of isopropanol and the C5 atom of F420 is optimal for hydride transfer
pH 5.8, the activity of a 20-fold dilution decreases to 5% within 20 min. If 100 mM potassium sulfate is present 40% of the activity is left after 20 min
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
unstable in 40 mM phosphate or Tris-HC1 buffer at 4°C and also in low-ionic-strength buffers in which precipitation occurrs and enzyme activity is lost irreversibly. The enzyme can be stabilized by addition of 200 mM sodium sulfate and 10 mM 2-propanol to the buffer
Expression of secondary alcohol dehydrogenase in methanogenic bacteria and purification of the F420-specific enzyme from Methanogenium thermophilum strain TCI
Purification and properties of F420- and NADP(+)-dependent alcohol dehydrogenases of Methanogenium liminatans and Methanobacterium palustre, specific for secondary alcohols
Si-face stereospecificity at C5 of coenzyme F420 for F420-dependent glucose-6-phosphate dehydrogenase from Mycobacterium smegmatis and F420-dependent alcohol dehydrogenase from Methanoculleus thermophilicus
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1.1.98.5 secondary-alcohol dehydrogenase (coenzyme-F420)
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