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Literature summary extracted from
- Crystal structure of a novel prolidase from Deinococcus radiodurans identifies new subfamily of bacterial prolidases (2017), Proteins, 85, 2239-2251 .
Cloned(Commentary)
| EC Number | Cloned (Comment) | Organism |
|---|---|---|
| 3.4.13.9 | - |
Deinococcus radiodurans |
Crystallization (Commentary)
| EC Number | Crystallization (Comment) | Organism |
|---|---|---|
| 3.4.13.9 | to 1.4 A resolution. XPP forms a dimeric structure via unique dimer stabilization loops of N-terminal domains such that their C-terminal domains are placed far apart from each other | Deinococcus radiodurans |
Protein Variants
| EC Number | Protein Variants | Comment | Organism |
|---|---|---|---|
| 3.4.13.9 | R46A | two orders of magnitude loss in the enzymatic activity for all the dipeptides attempted. The Glu340 side-chain interacts with Arg46 and stabilizes its side-chain conformation that is appropriate for substrate binding | Deinococcus radiodurans |
KM Value [mM]
| EC Number | KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|---|
| 3.4.13.9 | 1.3 | - |
Phe-Pro | pH 8.0, 55°C | Deinococcus radiodurans |  |
| 3.4.13.9 | 1.5 | - |
Lys-Pro | pH 8.0, 55°C | Deinococcus radiodurans | |
| 3.4.13.9 | 1.7 | - |
Met-Pro | pH 8.0, 55°C | Deinococcus radiodurans | |
Metals/Ions
| EC Number | Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|---|
| 3.4.13.9 | Mn2+ | presence of 1 mM in the assay | Deinococcus radiodurans | |
Organism
| EC Number | Organism | UniProt | Comment | Textmining |
|---|---|---|---|---|
| 3.4.13.9 | Deinococcus radiodurans | - |
- |
- |
Substrates and Products (Substrate)
| EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 3.4.13.9 | Lys-Pro + H2O | - |
Deinococcus radiodurans | Lys + Pro | - |
? | |
| 3.4.13.9 | Met-Pro + H2O | - |
Deinococcus radiodurans | Met + Pro | - |
? | |
| 3.4.13.9 | additional information | the decreasing order of preference for the P1 residue in the Xaa-Pro dipeptides is Ala, Ser, Phe=Lys, Met, Leu, Gly, Arg, Pro, Val, Tyr, Ile, His, Asp | Deinococcus radiodurans | ? | - |
? | |
| 3.4.13.9 | Phe-Pro + H2O | - |
Deinococcus radiodurans | Phe + Pro | - |
? | |
Synonyms
| EC Number | Synonyms | Comment | Organism |
|---|---|---|---|
| 3.4.13.9 | XPP | - |
Deinococcus radiodurans |
Turnover Number [1/s]
| EC Number | Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|---|
| 3.4.13.9 | 178 | - |
Met-Pro | pH 8.0, 55°C | Deinococcus radiodurans | |
| 3.4.13.9 | 256 | - |
Phe-Pro | pH 8.0, 55°C | Deinococcus radiodurans | |
| 3.4.13.9 | 349 | - |
Lys-Pro | pH 8.0, 55°C | Deinococcus radiodurans | |
kcat/KM [mM/s]
| EC Number | kcat/KM Value [1/mMs-1] | kcat/KM Value Maximum [1/mMs-1] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|---|
| 3.4.13.9 | 102 | - |
Met-Pro | pH 8.0, 55°C | Deinococcus radiodurans | |
| 3.4.13.9 | 201 | - |
Phe-Pro | pH 8.0, 55°C | Deinococcus radiodurans | |
| 3.4.13.9 | 233 | - |
Lys-Pro | pH 8.0, 55°C | Deinococcus radiodurans | |
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Release 2023.1 (January 2023)
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