Elucidation of a Self-Sustaining Cycle in Escherichia coli l-Serine Biosynthesis That Results in the Conservation of the Coenzyme, NAD<sup/>

Biochemistry
G A Grant

Abstract

The equilibrium of the reaction catalyzed by d-3-phosphoglycerate dehydrogenase (PGDH), the first enzyme in the l-serine biosynthetic pathway, is far in the direction away from serine synthesis. As such, the enzyme is usually assayed in this direction. To easily assay it in the direction of l-serine synthesis, it can be coupled to the next enzyme in the pathway, phosphoserine aminotransferase (PSAT), with the activity monitored by the conversion of NAD+ to NADH by PGDH. However, when PGDHs from several different species were coupled to PSAT, it was found that one of them, ecPGDH, conserves the coenzyme in the production of l-serine by utilizing an intrinsic cycle of NAD+/NADH interconversion coupled with the conversion of α-ketoglutarate (αKG) to α-hydroxyglutarate. Furthermore, the cycle can be maintained by production of αKG by the second enzyme in the pathway, PSAT, and does not require any additional enzymes. This is not the case for PGDH from another bacterial source, Mycobacterium tuberculosis, and a mammalian source, human liver, where net consumption of NAD+ occurs. Both NAD+ and NADH appear to remain tightly bound to ecPGDH during the cycle, effectively removing a requirement for the presence of an exogenous coenzyme p...Continue Reading

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Citations

Aug 12, 2018·The FEBS Journal·Julia Becker-KetternCarole L Linster
Jul 6, 2019·Frontiers in Plant Science·Li TaiKun-Ming Chen
Jan 9, 2019·Frontiers in Molecular Biosciences·Gregory A Grant
Mar 24, 2021·The Journal of Biological Chemistry·Hanyu XuLuhua Lai
May 1, 2021·International Journal of Molecular Sciences·Giulia MurtasLoredano Pollegioni

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