6C2G
Human triosephosphate isomerase mutant V231M
Summary for 6C2G
| Entry DOI | 10.2210/pdb6c2g/pdb |
| Descriptor | Triosephosphate isomerase (2 entities in total) |
| Functional Keywords | isomerase |
| Biological source | Homo sapiens (Human) |
| Total number of polymer chains | 4 |
| Total formula weight | 106934.12 |
| Authors | Torres, L.A.,Enriquez, F.S. (deposition date: 2018-01-08, release date: 2018-03-21, Last modification date: 2023-10-04) |
| Primary citation | Cabrera, N.,Torres-Larios, A.,Garcia-Torres, I.,Enriquez-Flores, S.,Perez-Montfort, R. Differential effects on enzyme stability and kinetic parameters of mutants related to human triosephosphate isomerase deficiency. Biochim. Biophys. Acta, 1862:1401-1409, 2018 Cited by PubMed Abstract: Human triosephosphate isomerase (TIM) deficiency is a very rare disease, but there are several mutations reported to be causing the illness. In this work, we produced nine recombinant human triosephosphate isomerases which have the mutations reported to produce TIM deficiency. These enzymes were characterized biophysically and biochemically to determine their kinetic and stability parameters, and also to substitute TIM activity in supporting the growth of an Escherichia coli strain lacking the tim gene. Our results allowed us to rate the deleteriousness of the human TIM mutants based on the type and severity of the alterations observed, to classify four "unknown severity mutants" with altered residues in positions 62, 72, 122 and 154 and to explain in structural terms the mutation V231M, the most affected mutant from the kinetic point of view and the only homozygous mutation reported besides E104D. PubMed: 29571745DOI: 10.1016/j.bbagen.2018.03.019 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.3 Å) |
Structure validation
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