Protein Family Models

Triosephosphate isomerase (EC: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, present in eukaryotes and prokaryotes. 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 [2,3]. The tertiary structure of TIM has eight beta/alpha motifs folded into a barrel structure [4]. 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 [5]. [1]. 2204417. Structure of yeast triosephosphate isomerase at 1.9-A. resolution.. Lolis E, Alber T, Davenport RC, Rose D, Hartman FC, Petsko GA;. Biochemistry. 1990;29:6609-6618.. [2]. 2005961. Enzyme catalysis: not different, just better.. Knowles JR;. Nature. 1991;350:121-124.. [3]. 12509510. 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. 2003;100:50-55.. [4]. 12206759. 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. 2002;321:741-765.. [5]. 12023819. Triosephosphate isomerase deficiency: a neurodegenerative. misfolding disease.. Olah J, Orosz. TRUNCATED at 1650 bytes (from Pfam)

Date:

2024-08-14

Triosephosphate isomerase (tim/TPIA) is the glycolytic enzyme that catalyzes the reversible interconversion of glyceraldehyde 3-phosphate and dihydroxyacetone phosphate.

Gene:

tpiA

Date:

2021-04-27