|PROSITE documentation PDOC00155|
Triosephosphate isomerase (EC 184.108.40.206) (TIM)  is the glycolytic enzyme that catalyzes the reversible interconversion of glyceraldehyde 3-phosphate and dihydroxyacetone phosphate. TIM plays an important role in several metabolic pathways and is essential for efficient energy production. It is present in eukaryotes as well as in prokaryotes. TIM is a dimer of identical subunits, each of which is made up of about 250 amino-acid residues. A glutamic acid and a histidine residue are involved in the catalytic mechanism [2,3].
The tertiary structure of TIM has eight β/α motifs folded into a barrel structure (see <PDB:1NEY>). The TIM barrel fold occurs ubiquitously and is found in numerous other enzymes that can be involved in energy metabolism, macromolecule metabolism, or small molecule metabolism .
The sequence around the active site residue is strongly conserved in all known TIM's and can be used as a signature pattern for this type of enzyme. We also developed a profile that covers the entire TIM structure.Last update:
March 2009 / Text revised; profile added.
PROSITE methods (with tools and information) covered by this documentation:
|1||Authors||Lolis E., Alber T., Davenport R.C., Rose D., Hartman F.C., Petsko G.A.|
|Title||Structure of yeast triosephosphate isomerase at 1.9-A resolution.|
|Title||Enzyme catalysis: not different, just better.|
|3||Authors||Jogl G., Rozovsky S., McDermott A.E., Tong L.|
|Title||Optimal alignment for enzymatic proton transfer: structure of the Michaelis complex of triosephosphate isomerase at 1.2-A resolution.|
|Source||Proc. Natl. Acad. Sci. U.S.A. 100:50-55(2003).|
|4||Authors||Nagano N., Orengo C.A., Thornton J.M.|
|Title||One fold with many functions: the evolutionary relationships between TIM barrel families based on their sequences, structures and functions.|
|Source||J. Mol. Biol. 321:741-765(2002).|