Crystallization (Comment) | Organism |
---|---|
crystal structure analysis, overview | Plasmodium falciparum |
Protein Variants | Comment | Organism |
---|---|---|
Y74G | site-directed mutagenesis, the mutation Tyr74Gly significantly reduces the stability of the dimer, mutation-induced alteration in the backbone conformation of Lys12, structure comparison to the wild-type enzyme | Plasmodium falciparum |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
D-Glyceraldehyde 3-phosphate | Plasmodium falciparum | - |
Glycerone phosphate | - |
r |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Plasmodium falciparum | Q07412 | - |
- |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
D-Glyceraldehyde 3-phosphate | - |
Plasmodium falciparum | Glycerone phosphate | - |
r |
Subunits | Comment | Organism |
---|---|---|
dimer | TIM is functional only as a homodimer, the interface Cys13 plays a major role in the stability of the dimer, Cys13 forms favorable interactions with loop 3 and Lys12. Structurally conserved Tyr74 may be essential for the stability, it is necessary to preserve the collective motions in the dimer that contribute to the catalytic efficiency of the TIM dimer. Tyr74 is a ready-made recognition motif for TIM homodimerization | Plasmodium falciparum |
More | simulation of the dynamics of monomeric TIM subunit A, molecular dynamics simulations, disulfide cross-linking at the interface is required for stability, the absence of a disulfide bond between Cys13 and Cys74 produces a dramatic shift in the conformation of Lys12, overview | Plasmodium falciparum |
Synonyms | Comment | Organism |
---|---|---|
TIM | - |
Plasmodium falciparum |
Triosephosphate isomerase | - |
Plasmodium falciparum |