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Literature summary extracted from

  • Hartman, F.C.; Norton, I.L.
    Triosephosphate isomerase from rabbit muscle (1975), Methods Enzymol., 41B, 447-453.
    View publication on PubMed

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
5.3.1.1
-
 Oryctolagus cuniculus

Inhibitors

EC Number Inhibitors Comment Organism Structure
5.3.1.1 D-alpha-glycerophosphate competitive Oryctolagus cuniculus
5.3.1.1 Phosphoglycolate and its corresponding hydroxamate; competitive Oryctolagus cuniculus

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
5.3.1.1 53260
-
 calculation from primary structure Oryctolagus cuniculus

Organism

EC Number Organism UniProt Comment Textmining
5.3.1.1 Oryctolagus cuniculus
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
5.3.1.1
-
 Oryctolagus cuniculus

Source Tissue

EC Number Source Tissue Comment Organism Textmining
5.3.1.1 muscle
-
 Oryctolagus cuniculus
-

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
5.3.1.1 7800
-
-
 Oryctolagus cuniculus

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
5.3.1.1 D-Glyceraldehyde 3-phosphate
-
 Oryctolagus cuniculus Glycerone phosphate
-
 ?

Subunits

EC Number Subunits Comment Organism
5.3.1.1 dimer each subunit contains an active site Oryctolagus cuniculus

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
5.3.1.1 additional information
-
 additional information
-
 Oryctolagus cuniculus