794528-57-7Relevant academic research and scientific papers
A straightforward synthesis of an aminocyclitol based on an enzymatic aldol reaction and a highly stereoselective intramolecular Henry reaction
El Blidi, Lahssen,Crestia, Dominique,Gallienne, Estelle,Demuynck, Colette,Bolte, Jean,Lemaire, Marielle
, p. 2951 - 2954 (2004)
The reactions of 4-nitroaldehydes 9 and 10 with dihydroxyacetonephosphate (DHAP) catalyzed by fructose-1,6-diphosphate aldolase from rabbit muscle were studied. Starting from 9 or 10, only one main stereomer of nitrocyclitol 8 was isolated. A highly stere
Genome mining for innovative biocatalysts: New Dihydroxyacetone aldolases for the chemist's toolbox
Guérard-Hélaine, Christine,De Berardinis, Véronique,Besnard-Gonnet, Marielle,Darii, Ekaterina,Debacker, Marine,Debard, Adrien,Fernandes, Carlos,Hélaine, Virgil,Mariage, Aline,Pellouin, Virginie,Perret, Alain,Petit, Jean-Louis,Sancelme, Martine,Lemaire, Marielle,Salanoubat, Marcel
, p. 1871 - 1879 (2015/06/23)
Stereoselective carboligating enzymes were discovered by a genome mining approach to extend the biocatalysis toolbox. Seven hundred enzymes were selected by sequence comparison from diverse prokaryotic species as representatives of the aldolase (FSA) family diversity. The aldol reaction tested involved dihydroxyacetone (DHA) and glyceraldehyde-3-phosphate. The hexose-6-phosphate formation was monitored by mass spectrometry. Eighteen enzymes annotated either as transaldolases or aldolases were found to exhibit a DHA aldolase activity. Remarkably, six of them proven as aldolases, and not transaldolases, shared very limited similarities with those currently described. Multiple sequence alignment performed on all enzymes revealed a Tyr in the new DHA aldolases as found in FSAcoli instead of a Phe usually found in transaldolases. Four of these DHA aldolases were biochemically characterised in comparison with FSAcoli. In particular, an aldolase from Listeria monocytogenes exhibited interesting catalytic properties. Exploiting nature′s catalyst mines: A universal high-throughput screening strategy based on mining genomes and selection of enzyme representatives of the aldolase family is applied. Out of ten hits proven as dihydroxyacetone aldolases, one from Listeria monocytogenes exhibited highly interesting catalytic properties, comparable to those of FSAcoli.
A mutant D-fructose-6-phosphate aldolase (Ala129Ser) with improved affinity towards dihydroxyacetone for the synthesis of polyhydroxylated compounds
Castillo, Jose A.,Guerard-Helaine, Christine,Gutierrez, Mariana,Garrabou, Xavier,Sancelme, Martine,Schuermann, Melanie,Inoue, Tomoyuki,Helaine, Virgil,Charmantray, Franck,Gefflaut, Thierry,Hecquet, Laurence,Joglar, Jesus,Clapes, Pere,Sprenger, Georg A.,Lemaire, Marielle
experimental part, p. 1039 - 1046 (2010/07/14)
A mutant of D-fructose-6-phosphate aldo-lase (FSA) of Escherichia coli, FSA A129S, with im-proved catalytic efficiency towards dihydroxyacetone (DHA), the donor substrate in aldol addition reac-tions, was explored for synthetic applications. The Kcat/KM value for DHA was 17-fold higher with FSA A129S than that with FSA wild type (FSA wt). On the other hand, for hydroxyacetone as donor sub-strate FSA A129S was found to be 3.5-fold less effi-cient than FSA wt. Furthermore, FSA A129S also ac-cepted glycolaldehyde (GA) as donor substrate with 3.3-fold lower affinity than FSA wt. This differential selectivity of both FSA wt and FSA A129S for GA makes them complementary biocatalysts allowing a control over donor and acceptor roles, which is par-ticularly useful in carboligation multi-step cascade synthesis of polyhydroxylated complex compounds. Production of the mutant protein was also improved for its convenient use in synthesis. Several carbohy-drates and nitrocyclitols were efficiently prepared, demonstrating the versatile potential of FSA A129S as biocatalyst in organic synthesis.
