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Table 2 Enzyme characteristic of FadB’ in comparison with other enzymes

From: (S)-3-hydroxyacyl-CoA dehydrogenase/enoyl-CoA hydratase (FadB’) from fatty acid degradation operon of Ralstonia eutropha H16

 

Cofactor

Trifunctional activity

Specificity to (S)- or (R)-3-hydroxyacyl-CoA

Reference

NAD+

NADP+

FadB’ Re

100*

5*

+

S**

this work

PhaB1 Re

20

100

-

R

Haywood et al. [1988b]

Unidentified acetoacetyl-CoA reductase (R. eutropha H16)

100

2

n.a.

S/R

Haywood et al. [1988b]

FadB Ec

+

n.a.

+

S

Binstock and Schulz [1981]

  1. *-The activity of FadB’ was measured at 340 nm and 30°C with acetoacetyl-CoA in direction of 3-hydroxybutyryl-CoA formation as described in “Materials and Methods”.
  2. **-The stereospecificity of FadB’ was measured at 303 nm and 30°C with (S)- and (R)-3hydroxybutyryl-CoA as described in “Materials and Methods”.