F
IPR000652

Triosephosphate isomerase

InterPro entry
Short nameTriosephosphate_isomerase
Overlapping
homologous
superfamilies
 
family relationships

Description

Triosephosphate isomerase (
5.3.1.1
) (TIM)
[1]
is the glycolytic enzyme that catalyses 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, highly conserved in prokaryotes and eukaryotes. In pathogenic organisms, this enzyme plays a crucial role obtaining energy for infection and survival. TIM is a dimer of identical subunits, each of which is made up of about 250 amino-acid residues. A glutamic acid residue is involved in the catalytic mechanism
[3, 2, 6]
.

The tertiary structure of TIM has eight β/α motifs folded into a barrel structure. 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
[5]
.

The sequence around the active site residue is perfectly conserved in all known TIM's. Deficiencies in TIM are associated with haemolytic anaemia coupled with a progressive, severe neurological disorder
[4]
.

References

1.Structure of yeast triosephosphate isomerase at 1.9-A resolution. Lolis E, Alber T, Davenport RC, Rose D, Hartman FC, Petsko GA. Biochemistry 29, 6609-18, (1990). View articlePMID: 2204417

2.Optimal alignment for enzymatic proton transfer: structure of the Michaelis complex of triosephosphate isomerase at 1.2-A resolution. Jogl G, Rozovsky S, McDermott AE, Tong L. Proc. Natl. Acad. Sci. U.S.A. 100, 50-5, (2003). View articlePMID: 12509510

3.Enzyme catalysis: not different, just better. Knowles JR. Nature 350, 121-4, (1991). View articlePMID: 2005961

4.Triosephosphate isomerase deficiency: a neurodegenerative misfolding disease. Olah J, Orosz F, Keseru GM, Kovari Z, Kovacs J, Hollan S, Ovadi J. Biochem. Soc. Trans. 30, 30-8, (2002). View articlePMID: 12023819

5.One fold with many functions: the evolutionary relationships between TIM barrel families based on their sequences, structures and functions. Nagano N, Orengo CA, Thornton JM. J. Mol. Biol. 321, 741-65, (2002). View articlePMID: 12206759

6.Gene Cloning, Recombinant Expression, Characterization, and Molecular Modeling of the Glycolytic Enzyme Triosephosphate Isomerase from Fusarium oxysporum. Hernandez-Ochoa B, Gomez-Manzo S, Alcaraz-Carmona E, Serrano-Posada H, Centeno-Leija S, Arreguin-Espinosa R, Cuevas-Cruz M, Gonzalez-Valdez A, Mendoza-Espinoza JA, Acosta Ramos M, Cortes-Maldonado L, Montiel-Gonzalez AM, Perez de la Cruz V, Rocha-Ramirez LM, Marcial-Quino J, Sierra-Palacios E. Microorganisms 8, (2019). PMID: 31878282

GO terms

biological process

  • None

cellular component

  • None

Cross References

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