Description
Triose-phosphate isomerase (TPI or TIM) is an enzyme (EC 5.3.1.1) that catalyzes the reversible interconversion of the triose phosphate isomers dihydroxyacetone phosphate and D-glyceraldehyde 3-phosphate. TPI plays an important role in glycolysis and is essential for efficient energy production. TPI has been found in nearly every organism searched for the enzyme, including animals such as mammals and insects as well as in fungi, plants, and bacteria. However, some bacteria that do not perform glycolysis, like ureaplasmas, lack TPI.
Abbr
TPI, Native (Baker's Yeast (S. cerevisiae))
Source
Baker's yeast (S. cerevisiae)
Applications
Triosephosphate isomerase has been used in a study to assess differential expression of fourteen proteins of uveal melanoma. Triosephosphate isomerase has also been used in a study to investigate the use of sigmoid pH gradients in free-flow isoelectric f ocusing of human endothelial cell proteins.
Form
ammonium sulfate suspension; Crystalline suspension in 2.7 M (NH4)2SO4, 0.5 mM EDTA, pH 6.5
Enzyme Commission Number
EC 5.3.1.1
Activity
~10,000 units/mg protein
Unit Definition
One unit will convert 1.0 μmole D-glyceraldehyde 3-phosphate to dihydroxyacetone phosphate per min at pH 7.6 at 25°C.
Warnings
Protein determined by biuret. Since the assay of this enzyme seems to be sensitive to minor variables, packages are dispensed per mg protein rather than in units.
Synonyms
Triose-phosphate isomerase; phosphotriose isomerase; triose phosphoisomerase; triose phosphate mutase; D-glyceraldehyde-3-phosphate ketol-isomerase; TPI; TIM; EC 5.3.1.1; 9023-78-3
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