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Literature summary extracted from
- Purification and characterization of a cobalt-activated carboxypeptidase from the hyperthermophilic archaeon Pyrococcus furiosus (1999), Protein Sci., 8, 2474-2486.
Inhibitors
| EC Number | Inhibitors | Comment | Organism | Structure |
|---|---|---|---|---|
| 3.4.17.B5 | DTT | 2 mM, complete inhibition | Pyrococcus furiosus |  |
| 3.4.17.B5 | EDTA | 1 mM, complete inhibition. Inhibition is fully reversible upon 50fold dilution and re-activation by Co2+ | Pyrococcus furiosus | |
| 3.4.17.B5 | additional information | the serine protease inhibitor phenylmethylsulfonyl fluoride has no effect on the activity | Pyrococcus furiosus |
KM Value [mM]
| EC Number | KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|---|
| 3.4.17.B5 | 0.9 | - |
N-carboxybenzoyl-Ala-Arg | 80°C, pH 6.5, 0.4 mM CoCl2 | Pyrococcus furiosus | |
Metals/Ions
| EC Number | Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|---|
| 3.4.17.B5 | Co2+ | purified in its inactive state by the addition of EDTA and dithiothreitol to purification buffers, and the activity is restored by the addition of Co2+. No activation by Zn2+ | Pyrococcus furiosus | |
Molecular Weight [Da]
| EC Number | Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
|---|---|---|---|---|
| 3.4.17.B5 | 58000 | - |
2 * 58000, SDS-PAGE | Pyrococcus furiosus |
| 3.4.17.B5 | 59000 | - |
2 * 59000, matrix-assisted laser desorption ionization time-of flight mass spectrometry | Pyrococcus furiosus |
| 3.4.17.B5 | 128000 | - |
gel filtration | Pyrococcus furiosus |
Natural Substrates/ Products (Substrates)
| EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 3.4.17.B5 | additional information | Pyrococcus furiosus | the enzyme is involved in digestion and protein turnover | ? | - |
? | |
Organism
| EC Number | Organism | UniProt | Comment | Textmining |
|---|---|---|---|---|
| 3.4.17.B5 | Pyrococcus furiosus | Q8U3L0 | - |
- |
Purification (Commentary)
| EC Number | Purification (Comment) | Organism |
|---|---|---|
| 3.4.17.B5 | purified in its inactive state by the addition of EDTA and dithiothreitol to purification buffers, and the activity is restored by the addition of Co2+ | Pyrococcus furiosus |
Specific Activity [micromol/min/mg]
| EC Number | Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
|---|---|---|---|---|
| 3.4.17.B5 | 1391 | - |
substrate: N-carboxybenzoyl-Ala-Arg, 80°C, pH 6.5, 0.4 mM CoCl2 | Pyrococcus furiosus |
Substrates and Products (Substrate)
| EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 3.4.17.B5 | Ac-Asp-Arg-Val-Tyr-Ile-His-Pro-Phe + H2O | - |
Pyrococcus furiosus | Ac-Asp-Arg-Val-Tyr-Ile-His-Pro + L-phenylalanine | - |
? | |
| 3.4.17.B5 | Ac-Asp-Arg-Val-Tyr-Ile-His-Pro-Phe-His + H2O | - |
Pyrococcus furiosus | Ac-Asp-Arg-Val-Tyr-Ile-His-Pro-Phe + L-histidine | - |
? | |
| 3.4.17.B5 | Ac-Asp-Arg-Val-Tyr-Ile-His-Pro-Phe-His-Leu + H2O | - |
Pyrococcus furiosus | Ac-Asp-Arg-Val-Tyr-Ile-His-Pro-Phe-His + L-leucine | - |
? | |
| 3.4.17.B5 | Ac-Asp-Arg-Val-Tyr-Ile-His-Pro-Phe-His-Leu-Leu + H2O | - |
Pyrococcus furiosus | Ac-Asp-Arg-Val-Tyr-Ile-His-Pro-Phe-His-Leu + L-leucine | - |
? | |
| 3.4.17.B5 | Ac-Asp-Arg-Val-Tyr-Ile-His-Pro-Phe-His-Leu-Leu-Val + H2O | - |
Pyrococcus furiosus | Ac-Asp-Arg-Val-Tyr-Ile-His-Pro-Phe-His-Leu-Leu + L-valine | - |
? | |
| 3.4.17.B5 | Ac-Asp-Arg-Val-Tyr-Ile-His-Pro-Phe-His-Leu-Leu-Val-Tyr + H2O | - |
Pyrococcus furiosus | Ac-Asp-Arg-Val-Tyr-Ile-His-Pro-Phe-His-Leu-Leu-Val + L-tyrosine | - |
? | |
| 3.4.17.B5 | Ac-Asp-Arg-Val-Tyr-Ile-His-Pro-Phe-His-Leu-Leu-Val-Tyr-Ser + H2O | stepwise hydrolysis of up to seven residues from the C-terminus | Pyrococcus furiosus | Ac-Asp-Arg-Val-Tyr-Ile-His-Pro-Phe-His-Leu-Leu-Val-Tyr + L-serine | - |
? | |
| 3.4.17.B5 | additional information | the enzyme is involved in digestion and protein turnover | Pyrococcus furiosus | ? | - |
? | |
| 3.4.17.B5 | additional information | no activity with N-carboxybenzoyl-Ala-Gly, N-carboxybenzoyl-Ala-Pro, N-carboxybenzoyl-Ala-Asp, N-carboxybenzoyl-Ala-Glu | Pyrococcus furiosus | ? | - |
? | |
| 3.4.17.B5 | N-carboxybenzoyl-Ala-Ala + H2O | - |
Pyrococcus furiosus | N-carboxybenzoyl-Ala + L-alanine | - |
? | |
| 3.4.17.B5 | N-carboxybenzoyl-Ala-Arg + H2O | - |
Pyrococcus furiosus | N-carboxybenzoyl-Ala + L-arginine | - |
? | |
| 3.4.17.B5 | N-carboxybenzoyl-Ala-Ile + H2O | - |
Pyrococcus furiosus | N-carboxybenzoyl-Ala + L-isoleucine | - |
? | |
| 3.4.17.B5 | N-carboxybenzoyl-Ala-Leu + H2O | - |
Pyrococcus furiosus | N-carboxybenzoyl-Ala + L-leucine | - |
? | |
| 3.4.17.B5 | N-carboxybenzoyl-Ala-Lys + H2O | - |
Pyrococcus furiosus | N-carboxybenzoyl-Ala + L-lysine | - |
? | |
| 3.4.17.B5 | N-carboxybenzoyl-Ala-Met + H2O | - |
Pyrococcus furiosus | N-carboxybenzoyl-Ala + L-methionine | - |
? | |
| 3.4.17.B5 | N-carboxybenzoyl-Ala-Phe + H2O | - |
Pyrococcus furiosus | N-carboxybenzoyl-Ala + L-phenylalanine | - |
? | |
| 3.4.17.B5 | N-carboxybenzoyl-Ala-Trp + H2O | - |
Pyrococcus furiosus | N-carboxybenzoyl-Ala + L-tryptophan | - |
? | |
| 3.4.17.B5 | N-carboxybenzoyl-Ala-Tyr + H2O | - |
Pyrococcus furiosus | N-carboxybenzoyl-Ala + L-tyrosine | - |
? | |
| 3.4.17.B5 | N-carboxybenzoyl-Ala-Val + H2O | - |
Pyrococcus furiosus | N-carboxybenzoyl-Ala + L-valine | - |
? | |
Subunits
| EC Number | Subunits | Comment | Organism |
|---|---|---|---|
| 3.4.17.B5 | homodimer | 2 * 58000, SDS-PAGE | Pyrococcus furiosus |
| 3.4.17.B5 | homodimer | 2 * 59000, matrix-assisted laser desorption ionization time-of flight mass spectrometry | Pyrococcus furiosus |
Synonyms
| EC Number | Synonyms | Comment | Organism |
|---|---|---|---|
| 3.4.17.B5 | PfuCP | - |
Pyrococcus furiosus |
Temperature Optimum [°C]
| EC Number | Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|---|
| 3.4.17.B5 | 90 | - |
- |
Pyrococcus furiosus |
Temperature Stability [°C]
| EC Number | Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
|---|---|---|---|---|
| 3.4.17.B5 | 80 | - |
the overall structure of the holoenzyme is extremely thermostable. The activities of both the apo and holo enzyme exhibit a similar second-order decay over time, with 50% activity remaining after 40 min at 80°C | Pyrococcus furiosus |
Turnover Number [1/s]
| EC Number | Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|---|
| 3.4.17.B5 | 600 | - |
N-carboxybenzoyl-Ala-Arg | 80°C, pH 6.5, 0.4 mM CoCl2 | Pyrococcus furiosus | |
pH Optimum
| EC Number | pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|---|
| 3.4.17.B5 | 6.2 | 6.6 | - |
Pyrococcus furiosus |
pH Range
| EC Number | pH Minimum | pH Maximum | Comment | Organism |
|---|---|---|---|---|
| 3.4.17.B5 | 5.3 | 7.3 | pH 5.3: about 50% of maximal activity, pH 7.3: about 50% of maximal activity | Pyrococcus furiosus |
kcat/KM [mM/s]
| EC Number | kcat/KM Value [1/mMs-1] | kcat/KM Value Maximum [1/mMs-1] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|---|
| 3.4.17.B5 | 667 | - |
N-carboxybenzoyl-Ala-Arg | 80°C, pH 6.5, 0.4 mM CoCl2 | Pyrococcus furiosus | |
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