Stephanie Bringer-Meyer

TL;DR: It is shown that an open reading frame at 9 min on the chromosomal map of E. coli encodes an enzyme (deoxyxylulose-5-phosphate synthase, DXP synthase) that catalyzes a thiamin diphosphate-dependent acyloin condensation reaction between C atoms 2 and 3 of pyruvate and glyceraldehyde 3-ph phosphate to yield DXP.

TL;DR: Incorporation of 13C-labeled glycerol or pyruvate into the ubiquinone Q8 of Escherichia coli mutants lacking enzymes of the triose phosphate metabolism and of (U-13C6)glucose into the triterpenoids of the hopane series of Zymomonas mobilis showed that glyceraldehyde 3-phosphate and a C2 unit derived from pyruVate decarboxylation were the

TL;DR: The current state of biotechnological alternatives using bacteria, yeasts, and microalgae is described and the potential for direct production of l-ascorbic acid exploiting novel bacterial pathways is discussed.

TL;DR: The functional overexpression of alcohol dehydrogen enzyme in the presence of formate dehydrogenase was sufficient to enable and sustain the desired reduction reaction via the relatively low specific activity of alcohol dehydrationase with NADH, instead of NADPH, as a cofactor.

TL;DR: Results show that the recombinant strain of E. coli can be utilized as an efficient biocatalyst for d-mannitol formation.