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Literature summary for 5.3.1.1 extracted from

  • Kulkarni, Y.S.; Liao, Q.; Bylehn, F.; Amyes, T.L.; Richard, J.P.; Kamerlin, S.C.L.
    Role of ligand-driven conformational changes in enzyme catalysis Modeling the reactivity of the catalytic cage of triosephosphate isomerase (2018), J. Am. Chem. Soc., 140, 3854-3857 .
    View publication on PubMedView publication on EuropePMC
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Organism

Organism UniProt Comment Textmining
Saccharomyces cerevisiae P00942
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Saccharomyces cerevisiae 288c P00942
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Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information the effect of bound phosphite dianion on the activation barrier is small, in comparison to the much larger intrinsic phosphodianion and phosphite dianion binding energy utilized to stabilize the transition states for TIM-catalyzed deprotonation of glyceraldehyde-3-phosphate and glyceraldehyde-phosphite dianion complex, respectively Saccharomyces cerevisiae ?
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additional information the effect of bound phosphite dianion on the activation barrier is small, in comparison to the much larger intrinsic phosphodianion and phosphite dianion binding energy utilized to stabilize the transition states for TIM-catalyzed deprotonation of glyceraldehyde-3-phosphate and glyceraldehyde-phosphite dianion complex, respectively Saccharomyces cerevisiae 288c ?
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 ?