Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 5.3.1.1 extracted from

  • ODonoghue, A.C.; Amyes, T.L.; Richard, J.P.
    Slow proton transfer from the hydrogen-labelled carboxylic acid side chain (Glu-165) of triosephosphate isomerase to imidazole buffer in D2O (2008), Org. Biomol. Chem., 6, 391-396.
    View publication on PubMed
Search for more literature for 5.3.1.1

Organism

Organism UniProt Comment Textmining
Oryctolagus cuniculus
-
-
-

Reaction

Reaction Comment Organism Reaction ID
D-Glyceraldehyde 3-phosphate = glycerone phosphate the active site of free enzyme, which has an open conformation needed to allow substrate binding, adopts a closed conformation at the enediolate-complex intermediate where the catalytic side chain is sequestered from interaction with imidazole dissolved in D2O Oryctolagus cuniculus
a

Source Tissue

Source Tissue Comment Organism Textmining
muscle
-
 Oryctolagus cuniculus
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
D-glyceraldehyde 3-phosphate the active site of free enzyme, which has an open conformation needed to allow substrate binding, adopts a closed conformation at the enediolate-complex intermediate where the catalytic side chain is sequestered from interaction with imidazole dissolved in D2O Oryctolagus cuniculus dihydroxyacetone phosphate
-
 ?