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Literature summary extracted from
- Molecular insights into substrate recognition and catalytic mechanism of the chaperone and FKBP peptidyl-prolyl isomerase SlyD (2016), BMC Biol., 14, 82 .
Cloned(Commentary)
| EC Number | Cloned (Comment) | Organism |
|---|---|---|
| 5.2.1.8 | - |
Thermus thermophilus |
Crystallization (Commentary)
| EC Number | Crystallization (Comment) | Organism |
|---|---|---|
| 5.2.1.8 | crystal structures with the inhibitor FK506 bound to the FK506-binding domain, and with 15-residue-long peptides bound to either one or both domains. Substrates bind in a highly adaptable fashion to the insert-in-flap chaperone domain through beta-strand augmentation, and can bind to the FK506-binding domain | Thermus thermophilus |
Protein Variants
| EC Number | Protein Variants | Comment | Organism |
|---|---|---|---|
| 5.2.1.8 | A78G | 52% of wild-type activity | Thermus thermophilus |
| 5.2.1.8 | D23A | 78% of wild-type activity | Thermus thermophilus |
| 5.2.1.8 | F128A | 35% of wild-type activity | Thermus thermophilus |
| 5.2.1.8 | H119A | 84% of wild-type activity | Thermus thermophilus |
| 5.2.1.8 | I37G | 50% of wild-type activity | Thermus thermophilus |
| 5.2.1.8 | M96A | 39% of wild-type activity | Thermus thermophilus |
| 5.2.1.8 | additional information | a mutant lacking the insert-in-flap chaperone domain shoiws 58% of wild-type activity | Thermus thermophilus |
| 5.2.1.8 | N35A | 71% of wild-type activity | Thermus thermophilus |
| 5.2.1.8 | Q94A | 98% of wild-type activity | Thermus thermophilus |
| 5.2.1.8 | Y13F | 92% of wild-type activity | Thermus thermophilus |
| 5.2.1.8 | Y63A | 21% of wild-type activity | Thermus thermophilus |
| 5.2.1.8 | Y63F | 76% of wild-type activity | Thermus thermophilus |
| 5.2.1.8 | Y92A | 36% of wild-type activity | Thermus thermophilus |
Inhibitors
| EC Number | Inhibitors | Comment | Organism | Structure |
|---|---|---|---|---|
| 5.2.1.8 | FK506 | - |
Thermus thermophilus |  |
KM Value [mM]
| EC Number | KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|---|
| 5.2.1.8 | 2 | - |
TRYWNAKMK-(cis)-PFIFGA | wild-type, pH 7.5, temperature not specified in the publication | Thermus thermophilus | |
Organic Solvent Stability
| EC Number | Organic Solvent | Comment | Organism |
|---|---|---|---|
| 5.2.1.8 | dimethyl sulfoxide | 5%, only minor effects on binding of peptide substrates | Thermus thermophilus |
Organism
| EC Number | Organism | UniProt | Comment | Textmining |
|---|---|---|---|---|
| 5.2.1.8 | Thermus thermophilus | Q5SLE7 | - |
- |
| 5.2.1.8 | Thermus thermophilus DSM 579 | Q5SLE7 | - |
- |
Substrates and Products (Substrate)
| EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 5.2.1.8 | additional information | peptide substrates derived from ribosomal proteins S2 and S3 display a dual binding mode with both a high- and a low-affinity binding site. Peptide TRYWNPKMKPFIFGA from protein S2 binds to both the insert-in-flap and FK506-binding domains | Thermus thermophilus | ? | - |
? | |
| 5.2.1.8 | additional information | peptide substrates derived from ribosomal proteins S2 and S3 display a dual binding mode with both a high- and a low-affinity binding site. Peptide TRYWNPKMKPFIFGA from protein S2 binds to both the insert-in-flap and FK506-binding domains | Thermus thermophilus DSM 579 | ? | - |
? | |
| 5.2.1.8 | N-succinyl-Ala-Leu-(cis)-Pro-Phe-4-nitroanilide | - |
Thermus thermophilus | N-succinyl-Ala-Leu-(trans)-Pro-Phe-4-nitroanilide | - |
r | |
| 5.2.1.8 | N-succinyl-Ala-Leu-(cis)-Pro-Phe-4-nitroanilide | - |
Thermus thermophilus DSM 579 | N-succinyl-Ala-Leu-(trans)-Pro-Phe-4-nitroanilide | - |
r | |
| 5.2.1.8 | TRYWNAKMK-(cis)-PFIFGA | - |
Thermus thermophilus | TRYWNAKMK-(trans)-PFIFGA | - |
r | |
| 5.2.1.8 | TRYWNAKMK-(cis)-PFIFGA | - |
Thermus thermophilus DSM 579 | TRYWNAKMK-(trans)-PFIFGA | - |
r | |
Synonyms
| EC Number | Synonyms | Comment | Organism |
|---|---|---|---|
| 5.2.1.8 | SLyD | - |
Thermus thermophilus |
| 5.2.1.8 | TTHA0346 | - |
Thermus thermophilus |
Turnover Number [1/s]
| EC Number | Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|---|
| 5.2.1.8 | 70000 | - |
TRYWNAKMK-(cis)-PFIFGA | wild-type, pH 7.5, temperature not specified in the publication | Thermus thermophilus | |
kcat/KM [mM/s]
| EC Number | kcat/KM Value [1/mMs-1] | kcat/KM Value Maximum [1/mMs-1] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|---|
| 5.2.1.8 | 850 | - |
N-succinyl-Ala-Leu-(cis)-Pro-Phe-4-nitroanilide | mutant lacking the insert-in-flap domain, pH 7.5, temperature not specified in the publication | Thermus thermophilus | |
| 5.2.1.8 | 1470 | - |
N-succinyl-Ala-Leu-(cis)-Pro-Phe-4-nitroanilide | wild-type, pH 7.5, temperature not specified in the publication | Thermus thermophilus | |
| 5.2.1.8 | 248000 | - |
TRYWNAKMK-(cis)-PFIFGA | mutant lacking the insert-in-flap domain, pH 7.5, temperature not specified in the publication | Thermus thermophilus | |
| 5.2.1.8 | 368000 | - |
TRYWNAKMK-(cis)-PFIFGA | wild-type, pH 7.5, temperature not specified in the publication | Thermus thermophilus | |
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