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Restoring a metabolic pathway.

Authors :
Richard JP
Source :
ACS chemical biology [ACS Chem Biol] 2008 Oct 17; Vol. 3 (10), pp. 605-7.
Publication Year :
2008

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.

Details

Language :
English
ISSN :
1554-8937
Volume :
3
Issue :
10
Database :
MEDLINE
Journal :
ACS chemical biology
Publication Type :
Academic Journal
Accession number :
18928248
Full Text :
https://doi.org/10.1021/cb800238s