Isabel Oroz-Guinea

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A bifunctional aldolase/kinase enzyme named DLF has been constructed by gene fusion through overlap extension. This fusion enzyme consists of monomeric fructose-1,6-bisphosphate aldolase (FBPA) from Staphylococcus carnosus and the homodimeric dihydroxyacetone kinase (DHAK) from Citrobacter freundii CECT 4626 with an intervening linker of five amino acid(More)
To transfer to the laboratory, the excellent efficiency shown by enzymes in Nature, biocatalysis, had to mimic several synthetic strategies used by the living organisms. Biosynthetic pathways are examples of tandem catalysis and may be assimilated in the biocatalysis field for the use of isolated multi-enzyme systems in the homogeneous phase. The concurrent(More)
Rhamnulose-1-phosphate aldolase from Thermotoga maritima (Rhu1PATm) has been recently cloned and characterized. This hyperthermophilic enzyme offers intriguing possibilities for practical catalysis. This is due to its high stability under extreme reaction conditions, such as high temperature or the presence of organic co-solvents. The Rhu1PATm potentiality(More)
The TM1072 gene from Thermotoga maritima codifies for a putative form of a rhamnulose-1-phosphate aldolase (Rha-1PA Tm). To investigate this enzyme further, its gene was cloned and expressed in Escherichia coli. The purified enzyme was activated by Co2+ as a divalent metal ion cofactor, instead of Zn2+ as its E. coli homologue, and exhibited a maximum of(More)
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