Table 1 The catalytic activity of Cphy1178 against aldehyde substrates.

From: Insight into Coenzyme A cofactor binding and the mechanism of acyl-transfer in an acylating aldehyde dehydrogenase from Clostridium phytofermentans

Substrate

kcat (s−1)

KM(mM)

kcat/KM(s−1 mM−1)

Ki(mM)

Acetaldehyde

1.62 ± 0.02

5.16 ± 0.10

0.31

n/a

Propionaldehyde

3.45 ± 0.03

0.82 ± 0.02

4.21

17.31 ± 0.46

Butyraldehyde

3.44 ± 0.7

1.74 ± 0.07

1.98

144.3 ± 30.2

Pentanaldehyde

5.44 ± 0.10

2.2 ± 0.7

2.47

12.61 ± 0.46

Hexanaldehyde

5.61 ± 0.12

2.90 ± 0.10

1.93

23.52 ± 1.28

  1. (Values for kcat, KM and Ki shown calculated standard errors) (See Supplementary Fig. 3 for kinetics curves).
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