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Literature summary for 5.3.1.1 extracted from

  • Amyes, T.L.; Richard, J.P.
    Enzymatic catalysis of proton transfer at carbon: activation of triosephosphate isomerase by phosphite dianion (2007), Biochemistry, 46, 5841-5854.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 5.3.1.1

Organism

Organism UniProt Comment Textmining
Oryctolagus cuniculus
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 commercial preparation
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Reaction

Reaction Comment Organism Reaction ID
D-Glyceraldehyde 3-phosphate = glycerone phosphate intrinsic binding energy of the substrate phosphodianion group is utilized to drive closing of the mobile loop and a protein conformational change that leads to formation of an active site environment that is optimally organized for stabilization of the transition state for proton transfer from R-carbonyl carbon Oryctolagus cuniculus
a

Source Tissue

Source Tissue Comment Organism Textmining
muscle
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 Oryctolagus cuniculus
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Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information formation of a two-part substrate by carving up D-glyceraldehyde 3-phosphate into the minimal neutral two-carbon sugar glycolaldehyde and phosphite dianion pieces. Enzyme catalyzes proton transfer from glycolaldehyde in D2O with a ratio of kcat to Km of 0.26 per M and s. Addition of exogenous phosphite dianion results in a large increase in the observed second-order rate constant for turnover of glycolaldehyde. Binding of phosphite dianion to the free enzyme is 700fold weaker than its binding to the fleeting complex of the enzyme with the altered substrate in the transition state Oryctolagus cuniculus ?
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