Triosephosphateisomerase
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| Triosephosphate isomerase 1 | |
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| Symbol(s): | TPI1 TIM |
| Genetic data | |
| Locus: | Chr. 12 p13 |
| Database Links | |
| EC number: | 5.3.1.1 |
| Entrez: | 7167 |
| OMIM: | 190450 |
| RefSeq: | NM_000365 |
| UniProt: | P60174 |
Triose-phosphate isomerase (TPI), is an enzyme (EC 5.3.1.1) that catalyzes the reversible interconvertion of triose phosphates isomers dihydroxyacetone phosphate and D-glyceraldehyde 3-phosphate.
| Dihydroxyacetone phosphate | triose phosphate isomerase | D-glyceraldehyde 3-phosphate | |
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| triose phosphate isomerase | |||
Compound C00111 at KEGG Pathway Database.Enzyme 5.3.1.1 at KEGG Pathway Database.Compound C00118 at KEGG Pathway Database.
Triose phosphate isomerase (TPI) plays an important role in glycolysis and is essential for efficient energy production. TPI has been found in every organism searched for the enzyme, from humans and chickens to trypanosoma brucei the parasitic protozoan that causes sleeping sickness and the intestinal bacterium E. coli.
Deficiencies in TPI are associated with haemolytic anaemia coupled with a progressive, severe neurological disorder.
Triose phosphate isomerase is a massively efficient enzyme, performing the reaction billions of times faster than it would naturally in solution. The reaction is so efficient it is limited by the rate the substrate can diffuse into the enzyme's active site.
[edit] Structure
Triose phosphate isomerase is a dimer of identical subunits, each of which is made up of about 250 amino acid residues. The three-dimensional structure of a subunit contains eight α-helices (blue and red) on the outside and eight parallel β-strands on the inside (violet and yellow). This structural motif is called an αβ-barrel, or a TIM-barrel, and is by far the most commonly observed protein fold. The active site of this enzyme is in the center of the barrel. A glutamic acid residue is involved in the catalytic mechanism. The sequence around the active site residue is conserved in all known triose phosphate isomerases.
[edit] See also
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[edit] References
http://pdbdev.sdsc.edu:48346/pdb/molecules/pdb50_6.html
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