Related DHAP Aldolases

Overall practical features make the FucA and RhuA enzymes quite similar for synthetic applications. Both metalloproteins are quite robust under conditions of organic synthesis and show a very high stability in the presence of low Zn concentrations with half-lives in the range of months at room temperature. The 

---

The stereodivergent action of DHAP aldolases is also preparatively useful under conditions of thermodynamic control [202,230, 294]. Starting from racemic 3-hydroxybutanal 84 the enantiocomplementary nature of the FruA RhuA enzyme couple will extend to the selection of the dependent stereocenter at C-6 to yield the corresponding mirror imaged products 78 with high selectivity [189], Conversely, the FucA will contribute a different major diastereomer 173, albeit only at a low de because of more balanced energetic relations [362],... 

Functionally related to FruA is the novel class I fructose 6-phosphate aldolase (FSA) from E. coli, which catalyzes the reversible cleavage of fructose 6-phosphate (30) to give dihydroxyacetone (31) and d-(18) [90]. It is the only known enzyme that does not require the expensive phosphorylated nucleophile DHAP for synthetic purpose. 

---