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ACS Chem Biol. 2008 Oct 17;3(10):605-7. doi: 10.1021/cb800238s.

Restoring a metabolic pathway.

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  • 1Department of Chemistry, University at Buffalo, SUNY, Buffalo, New York 14260-3000, USA.


Gluconeogenesis is blocked in a strain of Escherichia coli that is deficient in triosephosphate isomerase, but it was restored by the insertion of a plasmid coding for an L-glyceraldehyde 3-phosphate reductase (YghZ). This reductase provides a "bypass" that produces dihydroxyacetone phosphate (DHAP) by the consecutive enzyme-catalyzed reduction of L-glyceraldehyde 3-phosphate ( L-GAP) by NADPH to give L-glycerol 3-phosphate and reoxidation by NAD(+) catalyzed by endogenous L-glycerol 3-phosphate dehydrogenase to give DHAP. The origin of cellular L-GAP remains to be determined.

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