Structure–Reactivity
Effects on Intrinsic Primary
Kinetic Isotope Effects for Hydride Transfer Catalyzed by Glycerol-3-phosphate
Dehydrogenase
Version 4 2017-10-21, 13:13
Version 3 2016-11-10, 09:23
Version 2 2016-11-03, 13:23
Version 1 2016-10-27, 19:38
Posted on 2017-10-21 - 13:13
Primary deuterium
kinetic isotope effects (1°DKIE) on (kcat/KGA, M–1 s–1) for dianion (X2–) activated
hydride transfer from NADL to glycolaldehyde (GA) catalyzed by glycerol-3-phosphate
dehydrogenase were determined over a 2100-fold range of enzyme reactivity:
(X2–, 1°DKIE); FPO32–, 2.8 ± 0.1; HPO32–, 2.5 ±
0.1; SO42–, 2.8 ± 0.2; HOPO32–, 2.5 ± 0.1; S2O32–, 2.9 ± 0.1; unactivated; 2.4 ± 0.2.
Similar 1°DKIEs were determined for kcat. The observed 1°DKIEs are essentially independent of changes
in enzyme reactivity with changing dianion activator. The results
are consistent with (i) fast and reversible ligand binding; (ii) the
conclusion that the observed 1°DKIEs are equal to the intrinsic
1°DKIE on hydride transfer from NADL to GA; (iii) similar intrinsic
1°DKIEs on GPDH-catalyzed reduction of the substrate pieces and
the whole physiological substrate dihydroxyacetone phosphate. The
ground-state binding interactions for different X2– are similar, but there are large differences in the transition state
interactions for different X2–. The changes in transition
state binding interactions are expressed as changes in kcat and are proposed to represent changes in stabilization
of the active closed form of GPDH. The 1°DKIEs are much smaller
than observed for enzyme-catalyzed hydrogen transfer that occurs mainly
by quantum-mechanical tunneling.
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Reyes, Archie
C.; Amyes, Tina L.; Richard, John P. (2016). Structure–Reactivity
Effects on Intrinsic Primary
Kinetic Isotope Effects for Hydride Transfer Catalyzed by Glycerol-3-phosphate
Dehydrogenase. ACS Publications. Collection. https://doi.org/10.1021/jacs.6b07028
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AUTHORS (3)
AR
Archie
C. Reyes
TA
Tina L. Amyes
JR
John P. Richard
KEYWORDS
enzyme reactivityGAGlycerol -3-phosphate DehydrogenaseKinetic Isotope Effectsglycerol -3-phosphate dehydrogenasetransition state interactionsHOPONADLDKIEground-state binding interactionsk catenzyme-catalyzed hydrogen transferGPDHsubstrate dihydroxyacetone phosphatetransition state binding interactionsFPOHPOhydride transferHydride Transfer Catalyzed