Characterization and overproduction of the Escherichia coli appA encoded bifunctional enzyme
which exhibits both phytase and acid phosphatase activities.
Catalase-peroxidase (KatG) is a bifunctional enzyme
degrading H2O2 in bacteria and lower eukaryotes.
Because it possesses both 17[alpha]-hydroxylase and 17,20 lyase activities, P450c17 is considered a bifunctional enzyme
that has a profound impact on the flux through the steroidogenic pathway for its selective cellular localization in zona fasciculate and zona reticularis and its absence in zona glomerulosa.
This suggests that PO may act as a bifunctional enzyme, involved in both the biosynthesis of melanin in the melanization reaction and the degradation of DNA in vivo, although experimental support for this hypothesis is lacking.
There are many precedents for a bifunctional enzyme with distinct catalytic capacities, such as phosphofructo-kinase II and fructose-2,6-bisphosphatase.
For example, MOTIF software locates the aspartate kinase domain of the bifunctional enzyme at the N terminus of the protein and the homoserine dehydrogenase domain toward the C terminus which contains the conserved sequences in Fig.
coli b0002 bifunctional enzyme closer in sequence to the monofunctional enzymes in yeast and in the plant than to the other biofunctional enzyme in E.
ExoS is a bifunctional enzyme
with both GTPase-activating activity and ADP-ribosyltransferase activity.
The resulting bifunctional enzyme
can be efficiently produced using Escherichia coli, a factor that is crucial for producing carbohydrate products at a reasonable cost.