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Literature summary for 5.3.1.1 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)

Crystallization (Comment) Organism
-
Oryctolagus cuniculus

Inhibitors

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

Molecular Weight [Da]

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

Organism

Organism UniProt Comment Textmining
Oryctolagus cuniculus
-
-
-

Purification (Commentary)

Purification (Comment) Organism
-
Oryctolagus cuniculus

Source Tissue

Source Tissue Comment Organism Textmining
muscle
-
Oryctolagus cuniculus
-

Specific Activity [micromol/min/mg]

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

Substrates and Products (Substrate)

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

Subunits

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

Turnover Number [1/s]

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