63323-91-1Relevant academic research and scientific papers
Facile Enzymatic Synthesis of Phosphorylated Ketopentoses
Wen, Liuqing,Huang, Kenneth,Liu, Yunpeng,Wang, Peng George
, p. 1649 - 1654 (2016/03/15)
An efficient and convenient platform for the facile synthesis of phosphorylated ketoses is described. All eight phosphorylated ketopentoses were produced using this platform starting from two common and inexpensive aldoses (d-xylose and l-arabinose) in more than 84% isolated yield (gram scale). In this method, reversible conversions (isomerization or epimerization) were accurately controlled toward the formation of desired ketose phosphates by targeted phosphorylation reactions catalyzed by substrate-specific kinases. The byproducts were selectively removed by silver nitrate precipitation avoiding the tedious and time-consuming separation of sugar phosphate from adenosine phosphates (ATP and ADP). Moreover, the described strategy can be expanded for the synthesis of other sugar phosphates.
Facile enzymatic synthesis of ketoses
Wen, Liuqing,Huang, Kenneth,Wei, Mohui,Meisner, Jeffrey,Liu, Yunpeng,Garner, Kristina,Zang, Lanlan,Wang, Xuan,Li, Xu,Fang, Junqiang,Zhang, Houcheng,Wang, Peng George
supporting information, p. 12654 - 12658 (2015/10/28)
Studies of rare ketoses have been hampered by a lack of efficient preparation methods. A convenient, efficient, and cost-effective platform for the facile synthesis of ketoses is described. This method enables the preparation of difficult-to-access ketopentoses and ketohexoses from common and inexpensive starting materials with high yield and purity and without the need for a tedious isomer separation step. A spoonful of sugar: A convenient, efficient, and cost-effective platform for the facile synthesis of ketoses is described. This method, which involves a one-pot mulitenzyme (OPME) reaction, enables the preparation of rare ketopentoses and ketohexoses from common and inexpensive starting materials with high yield and purity and without the need for a tedious isomer separation step.
Fructose 1,6-bisphosphate aldolase from Staphylococcus carnosus: Overexpression, structure prediction, stereoselectivity, and application in the synthesis of bicyclic sugars
Zannetti, Maria Teresa,Walter, Christiane,Knorst, Marion,Fessner, Wolf-Dieter
, p. 1882 - 1890 (2007/10/03)
The gene for the fructose 1,6-bisphosphate aldolase from Staphylococcus carnosus (FruA(sca)) was subcloned for overexpression in Escherichia coli using the expression vector pKK223-3. An efficient, single-step purification by DEAE ion-exchange chromatography furnished the recombinant enzyme ready for synthetic applications. Sequence analysis indicated that FruA(sca) shares the overall α/β-barrel structure and most of the active site residues with the structurally well-defined FruA catalyst from rabbit muscle which signaled its functional equivalence for synthetic applications. A preparative study with generic aliphatic and hydroxylated aldehydes indeed confirmed a high level of stereoselectivity for both newly created asymmetric centers, and suggested a kinetic enantioselectivity for anionically charged 3- hydroxyaldehydes. In fact, the monomeric FruA(sca) was found to tolerate even the presence of highly reactive glutardialdehyde derivatives, which otherwise rapidly denature the rabbit muscle enzyme, and to allow their stereoselective conversion to bicyclic sugars.
Fructose-1,6-diphosphate aldolase from spinach leaves, a challenger for enzymatic synthesis of ketoses
Valentin,Bolte
, p. 8103 - 8106 (2007/10/02)
Fructose-1,6-diphosphate aldolase is easily extracted from spinach leaves in a form sufficiently pure to be used in synthesis. Its specificity, different from that of the commercial rabbit muscle aldolase make it a new interesting tool for the synthesis of ketoses-1-phosphates.
