Cloned (Comment) | Organism |
---|---|
recombinant expression of wild-type and mutant enzymes | Homo sapiens |
Protein Variants | Comment | Organism |
---|---|---|
V55R | site-directed mutagenesis, the mutation increases the PPIase activity by a factor of 11 | Homo sapiens |
Y82K | site-directed mutagenesis, the mutation decreases the PPIase activity by a factor of 7 | Homo sapiens |
Inhibitors | Comment | Organism | Structure |
---|---|---|---|
FK506 | - |
Homo sapiens |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Homo sapiens | - |
- |
- |
Synonyms | Comment | Organism |
---|---|---|
FK506 binding protein 12 | - |
Homo sapiens |
FKBP 12 | - |
Homo sapiens |
peptidyl-prolyl isomerase | - |
Homo sapiens |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
25 | - |
assay at | Homo sapiens |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
8 | - |
assay at | Homo sapiens |
General Information | Comment | Organism |
---|---|---|
physiological function | peptidyl-prolyl isomerase activity of FKBP12 is essential for prevention of aggregation of tau, an Alzheimer's disease-related protein. Tau aggregates into neurofibrillary tangles when it is hyperphosphorylated, only the cis-isomer can aggregate. FKBP12 catalyzes isomerization of the tau R3 peptide peptide in both the monomeric and aggregative states, once the cis-isomer is converted into the trans-isomer in the aggregative state, the trans-isomer is quickly released from the aggregation because the trans-isomer cannot aggregate, inhibitory mechanism of R3 peptide aggregation by simple binding of FKBP12, overview. IC50 of FKBP12 is 0.003 mM. The aggregation inhibitory activity of FKBP12 is independent of the affinity between FKBP12 and the R3 peptide. Therefore, the aggregation inhibitory activity of FKBP12 depends only on the PPIase activity of FKBP12 | Homo sapiens |