Substrate product equilibrium on a reversible enzyme, triosephosphate isomerase
S Rozovsky, AE McDermott - Proceedings of the National …, 2007 - National Acad Sciences
The highly efficient glycolytic enzyme, triosephosphate isomerase, is expected to
differentially stabilize the proposed stable reaction species: ketone, aldehyde, and enediol …
differentially stabilize the proposed stable reaction species: ketone, aldehyde, and enediol …
[引用][C] Substrate product equilibrium on a reversible enzyme, triosephosphate isomerase
S ROZOVSKY - Proc. Natl Acad. Sci. USA, 2007 - cir.nii.ac.jp
[HTML][HTML] Substrate product equilibrium on a reversible enzyme, triosephosphate isomerase
S Rozovsky, AE McDermott - … of the National Academy of Sciences …, 2007 - ncbi.nlm.nih.gov
The highly efficient glycolytic enzyme, triosephosphate isomerase, is expected to
differentially stabilize the proposed stable reaction species: ketone, aldehyde, and enediol …
differentially stabilize the proposed stable reaction species: ketone, aldehyde, and enediol …
[PDF][PDF] Substrate product equilibrium on a reversible enzyme, triosephosphate isomerase
S Rozovsky, AE McDermott - PNAS, 2007 - researchgate.net
Results We examined the steady-state populations of enzyme-bound triose phosphates by
using a fully 13C-enriched substrate,[13C3] DHAP, prepared by enzymatic synthesis from …
using a fully 13C-enriched substrate,[13C3] DHAP, prepared by enzymatic synthesis from …
Substrate Product Equilibrium on a Reversible Enzyme, Triosephosphate Isomerase
S Rozovsky, AE McDermott - Proceedings of the National Academy of …, 2007 - JSTOR
The highly efficient glycolytic enzyme, triosephosphate isomerase, is expected to
differentially stabilize the proposed stable reaction species: ketone, aldehyde, and enediol …
differentially stabilize the proposed stable reaction species: ketone, aldehyde, and enediol …
Substrate product equilibrium on a reversible enzyme, triosephosphate isomerase.
S Rozovsky, AE McDermott - … of the National Academy of Sciences …, 2007 - europepmc.org
The highly efficient glycolytic enzyme, triosephosphate isomerase, is expected to
differentially stabilize the proposed stable reaction species: ketone, aldehyde, and enediol …
differentially stabilize the proposed stable reaction species: ketone, aldehyde, and enediol …
Substrate product equilibrium on a reversible enzyme, triosephosphate isomerase
S Rozovsky, AE McDermott - Proceedings of the National …, 2007 - ui.adsabs.harvard.edu
The highly efficient glycolytic enzyme, triosephosphate isomerase, is expected to
differentially stabilize the proposed stable reaction species: ketone, aldehyde, and enediol …
differentially stabilize the proposed stable reaction species: ketone, aldehyde, and enediol …
Substrate product equilibrium on a reversible enzyme, triosephosphate isomerase
S Rozovsky, AE McDermott - Proceedings of the National …, 2007 - pubmed.ncbi.nlm.nih.gov
The highly efficient glycolytic enzyme, triosephosphate isomerase, is expected to
differentially stabilize the proposed stable reaction species: ketone, aldehyde, and enediol …
differentially stabilize the proposed stable reaction species: ketone, aldehyde, and enediol …
Substrate product equilibrium on a reversible enzyme, triosephosphate isomerase.
S Rozovsky, AE McDermott - … of the National Academy of Sciences …, 2007 - europepmc.org
The highly efficient glycolytic enzyme, triosephosphate isomerase, is expected to
differentially stabilize the proposed stable reaction species: ketone, aldehyde, and enediol …
differentially stabilize the proposed stable reaction species: ketone, aldehyde, and enediol …