Any feedback?
Literature summary for 3.4.17.18 extracted from
- Crystal structures of carboxypeptidase T complexes with transition-state analogs (2018), J. Biomol. Struct. Dyn., 36, 3958-3966 .
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| expression in the Escherichia coli BL21(DE3)pLysS cells | Thermoactinomyces vulgaris |
Crystallization (Commentary)
| Crystallization (Comment) | Organism |
|---|---|
| crystals of carboxypeptidase T complexes with the transition-state analogs N-sulfamoyl-L-arginine and N-sulfamoyl-L-phenylalanine are grown in microgravity in a capillary using the counter-diffusion technique. Conformation of the transition state analogue of the hydrophobic substrate in the complex with carboxypeptidase T is similar to that of the ground state analogue | Thermoactinomyces vulgaris |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Thermoactinomyces vulgaris | P29068 | - |
- |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
- |
Thermoactinomyces vulgaris |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| additional information | broad, predominantly hydrophobic substrate selectivity of this enzyme | Thermoactinomyces vulgaris | ? | - |
? |  |
Temperature Optimum [°C]
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 25 | - |
assay at | Thermoactinomyces vulgaris |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 7.5 | - |
assay at | Thermoactinomyces vulgaris |
Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.
Release 2023.1 (January 2023)
Legal
Curated at
Member of
