Table 2 Catalytic properties of the recombinant aldehyde dehydrogenase from Rps. palustris (AldDH).

From: In Vitro Characterization and Concerted Function of Three Core Enzymes of a Glycyl Radical Enzyme - Associated Bacterial Microcompartment

 

Vmax [μmol min−1 mg−1]

kcat [s−1]*

apparent KM [mM]

kcat/KM [M−1 s−1]*

acetaldehyde

117 ± 8

433

4.1 ± 0.7

105.6 × 103

propionaldehyde

242 ± 14

895

1.2 ± 0.17

745.8 × 103

acetyl-CoA

5.3 ± 0.3

19.6 ± 1.1

n.d.

n.d.

propionyl-CoA

31.6 ± 1.9

116.9 ± 7.0

n.d.

n.d.

3OHP -CoA

2.4 ± 0.05

8.9 ± 0.2

n.d.

n.d.

  1. *Per tetrameric enzyme, at 250 μM, n.d. – not determined.