PROSITE documentation PDOC00155

Triosephosphate isomerase (TIM) family signature and profile




Description

Triosephosphate isomerase (EC 5.3.1.1) (TIM) [1] 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 [4].

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.

Technical section

PROSITE methods (with tools and information) covered by this documentation:

TIM_2, PS51440; Triosephosphate isomerase (TIM) family profile  (MATRIX)

TIM_1, PS00171; Triosephosphate isomerase active site  (PATTERN)


References

1AuthorsLolis E., Alber T., Davenport R.C., Rose D., Hartman F.C., Petsko G.A.
TitleStructure of yeast triosephosphate isomerase at 1.9-A resolution.
SourceBiochemistry 29:6609-6618(1990).
PubMed ID2204417

2AuthorsKnowles J.R.
TitleEnzyme catalysis: not different, just better.
SourceNature 350:121-124(1991).
PubMed ID2005961
DOI10.1038/350121a0

3AuthorsJogl G., Rozovsky S., McDermott A.E., Tong L.
TitleOptimal alignment for enzymatic proton transfer: structure of the Michaelis complex of triosephosphate isomerase at 1.2-A resolution.
SourceProc. Natl. Acad. Sci. U.S.A. 100:50-55(2003).
PubMed ID12509510
DOI10.1073/pnas.0233793100

4AuthorsNagano N., Orengo C.A., Thornton J.M.
TitleOne fold with many functions: the evolutionary relationships between TIM barrel families based on their sequences, structures and functions.
SourceJ. Mol. Biol. 321:741-765(2002).
PubMed ID12206759



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