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Table 1 Specific NAD(H)-dependent oxidoreductase activities determined for the heterologously expressed and purified Debia-MDR protein

From: Cloning, functional expression and characterization of a bifunctional 3-hydroxybutanal dehydrogenase /reductase involved in acetone metabolism by Desulfococcus biacutus

Reduction with NADH Oxidation with NAD+
Substrate1) Spec. activity
mU mg−1
Substrate2) Spec. activity
mU mg−1
Formaldehyde b.d. Methanol n.d.
Acetaldehyde 52 ± 14 Ethanol 73 ± 13
Propanal 380 ± 15 1-Propanolb 22 ± 2
Butanal 301 ± 24 1-Butanol 47 ± 15
Isobutanal 276 ± 30 Isobutanol n.d.
Pentanal 325 ± 35 1-Pentanol 11 ± 3
Benzaldehyde b.d. Benzyl alcohol n.d.
Propanone (Acetone) 93 ± 2 2-Propanola (Isopropanol) 21 ± 1
Butanone 65 ± 11 2-Butanolb 115 ± 8
2-Pentanone 126 ± 38 2-Pentanol n.d.
3-Pentanone 141 ± 19 3-Pentanol n.d.
2-Hexanone 45 ± 9 2-Hexanol n.d.
3-Hydroxybutanone (Acetoine) 326 ± 38 2,3-Butanediol 150 ± 8
2,3-Butandione (Diacetyl) 298 ± 42 3-Hydroxybutanone (Acetoine) b.d.
3-Hydroxybutanal 248 ± 59 1,3-Butanediol 80 ± 23
4-Hydroxy-2-butanone 155 ± 31
3-Oxobutanal (Acetoacetaldehyde) n.s. 3-Hydroxybutanal 83 ± 18
4-Hydroxy-2-butanone 18 ± 3
  1. b.d. below detection limit (<1 mU mg−1 protein), n.d. not determined, n.s. no substrate was available for testing
  2. 1)Assay conditions: anoxic 25 mM MOPS buffer (pH 7.2) plus 3 mM DTT and 50 μM ZnCl2, 30 °C. Reactions in reductive direction were assayed with 0.1 mM NADH. Reactions were started by addition of 5 mM substrate
  3. 2)Assay conditions: anoxic 25 mM MOPS buffer (pH 8.0) plus 3 mM DTT and 50 μM ZnCl2, 30 °C. Reactions in the oxidative direction were assayed with 2.5 mM NAD+, or at pH 7.2 with 0.5 mM NAD+(a), or at pH 7.2 with 2.5 mM NAD+(b)