Abstract
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.
| Original language | English |
|---|---|
| Pages (from-to) | 605-607 |
| Number of pages | 3 |
| Journal | ACS Chemical Biology |
| Volume | 3 |
| Issue number | 10 |
| DOIs | |
| State | Published - Oct 17 2008 |
Fingerprint
Dive into the research topics of 'Restoring a metabolic pathway'. Together they form a unique fingerprint.Cite this
- APA
- Author
- BIBTEX
- Harvard
- Standard
- RIS
- Vancouver