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Table 5 Kinetic parameters of enzymes Tt_Hbd and St_Ter and their variants, purified from E. coli

From: Metabolic engineering of Clostridium thermocellum for n-butanol production from cellulose

Enzyme

NADH

NADPH

Km (mM)

Vmax (µmol/min/mg)

Km (mM)

Vmax (µmol/min/mg)

Hbda

0.05 ± 0.02c

61.4 ± 7.2

1.1 ± 0.2a

15.2 ± 2.5

Hbd (D31A)

0.06 ± 0.02

38.5 ± 4.5

0.03 ± 0.01

485.3 ± 34.2

Hbd (I32R)

0.08 ± 0.02

25.1 ± 6.3

0.04 ± 0.02

152.1 ± 12.2

Hbd (P36I)

0.08 ± 0.01

24.2 ± 2.1

0.04 ± 0.01

128.2 ± 15.3

Hbd M3 (D31A I32R P36I)

0.11 ± 0.02

26.6 ± 3.7

0.03 ± 0.01

764.9 ± 35.7

Terb

0.03 ± 0.01

18.2 ± 2.3

0.4 ± 0.1

12.2 ± 1.5

Ter M (E75A)

0.6 ± 0.1

10.3 ± 1.5

0.02 ± 0.01

68.1 ± 6.5

  1. aAcetoacetyl-CoA was substrate of Hbd assay
  2. bCrotonyl-CoA was the substrate of Ter assay
  3. cError represents one standard deviation, n = 3