
doi: 10.1021/cb800238s
pmid: 18928248
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.
Dihydroxyacetone Phosphate, Escherichia coli, Gluconeogenesis, Glyceraldehyde 3-Phosphate, Metabolic Networks and Pathways, Plasmids, Sugar Alcohol Dehydrogenases, Triose-Phosphate Isomerase
Dihydroxyacetone Phosphate, Escherichia coli, Gluconeogenesis, Glyceraldehyde 3-Phosphate, Metabolic Networks and Pathways, Plasmids, Sugar Alcohol Dehydrogenases, Triose-Phosphate Isomerase
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