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Literature summary for 5.3.1.1 extracted from

  • Kulkarni, Y.S.; Liao, Q.; Petrovi?, D.; Krueger, D.M.; Strodel, B.; Amyes, T.L.; Richard, J.P.; Kamerlin, S.C.L.
    Enzyme architecture Modeling the operation of a hydrophobic clamp in catalysis by triosephosphate isomerase (2017), J. Am. Chem. Soc., 139, 10514-10525 .
    View publication on PubMedView publication on EuropePMC
Search for more literature for 5.3.1.1

Cloned(Commentary)

Cloned (Comment) Organism
-
 Saccharomyces cerevisiae

Protein Variants

Protein Variants Comment Organism
I170A effect of the mutation on the relative electrostatic contribution of the residue is negligible. Mutation results in increases in the activation barriers for deprotonation of substrate Saccharomyces cerevisiae
I170A/L230A effect of the mutation on the relative electrostatic contribution of the residue is negligible. Mutation results in increases in the activation barriers for deprotonation of substrate Saccharomyces cerevisiae
L230A effect of the mutation on the relative electrostatic contribution of the residue is negligible. Mutation results in increases in the activation barriers for deprotonation of substrate Saccharomyces cerevisiae

Organism

Organism UniProt Comment Textmining
Saccharomyces cerevisiae P00942
-
-
Saccharomyces cerevisiae 288c P00942
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information the substrate is locked in a protein cage with the phosphodianion occluded from interaction with solvent water, and ion-paired to the surface alkyl ammonium side chain of residue K12. The neutral imidazole side chain of H95 interacts with the carbonyl oxygen of dihydroxyacetone phosphate and glyceraldehyde 3-phosphate Saccharomyces cerevisiae ?
-
 ?
additional information the substrate is locked in a protein cage with the phosphodianion occluded from interaction with solvent water, and ion-paired to the surface alkyl ammonium side chain of residue K12. The neutral imidazole side chain of H95 interacts with the carbonyl oxygen of dihydroxyacetone phosphate and glyceraldehyde 3-phosphate Saccharomyces cerevisiae 288c ?
-
 ?

Synonyms

Synonyms Comment Organism
TPI1
-
 Saccharomyces cerevisiae