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Literature summary extracted from
- Identification and characterization of bifunctional proline racemase/hydroxyproline epimerase from archaea: discrimination of substrates and molecular evolution (2015), PLoS One, 10, e0120349.
Cloned(Commentary)
| EC Number | Cloned (Comment) | Organism |
|---|---|---|
| 5.1.1.4 | expression in Escherichia coli | Clostridioides difficile |
| 5.1.1.4 | expression in Escherichia coli | Thermococcus litoralis |
| 5.1.1.4 | expression in Escherichia coli | Haloarcula japonica |
| 5.1.1.4 | expression in Escherichia coli | Ferroplasma acidarmanus |
| 5.1.1.8 | expression in Escherichia coli | Thermococcus litoralis |
| 5.1.1.8 | expression in Escherichia coli | Ferroplasma acidarmanus |
Protein Variants
| EC Number | Protein Variants | Comment | Organism |
|---|---|---|---|
| 5.1.1.4 | R240W | mutant enzyme shows similar kinetic constants for proline and hydroxyproline as compared to the wild-type enzyme | Ferroplasma acidarmanus |
| 5.1.1.4 | W241F the mutant enzyme | shows 5.3fold, 430fold, and 5.8fold lower kcat/Km values for trans-4-hydroxy-L-proline, trans-3-hydroxy-L-proline, and cis-4-hydroxy-D-proline respectively, mainly due to a marked decrease in kcat values, whereas no significant effects are found in the kinetic constants of proline, suggesting that this (hydrophobic and bulky) tryptophan residue plays an importance role in the recognition of hydroxyproline (more hydrophilic and bulky than proline) | Thermococcus litoralis |
| 5.1.1.8 | F240W | mutant enzyme shows similar kinetic constants for proline and hydroxyproline as compared to the wild-type enzyme | Ferroplasma acidarmanus |
| 5.1.1.8 | W241F the mutant enzyme | shows 5.3fold, 430fold, and 5.8fold lower kcat/Km values for trans-4-hydroxy-L-proline, trans-3-hydroxy-L-proline, and cis-4-hydroxy-D-proline respectively, mainly due to a marked decrease in kcat values, whereas no significant effects were found in the kinetic constants of proline, suggesting that this (hydrophobic and bulky) tryptophan residue plays an importance role in the recognition of hydroxyproline (more hydrophilic and bulky than proline) | Thermococcus litoralis |
Inhibitors
| EC Number | Inhibitors | Comment | Organism | Structure |
|---|---|---|---|---|
| 5.1.1.4 | pyrrole-2-carboxylate | - |
Clostridioides difficile |  |
| 5.1.1.4 | pyrrole-2-carboxylate | - |
Ferroplasma acidarmanus | |
| 5.1.1.4 | pyrrole-2-carboxylate | - |
Haloarcula japonica | |
| 5.1.1.4 | pyrrole-2-carboxylate | - |
Thermococcus litoralis | |
| 5.1.1.8 | pyrrole-2-carboxylate | - |
Ferroplasma acidarmanus | |
| 5.1.1.8 | pyrrole-2-carboxylate | - |
Thermococcus litoralis | |
KM Value [mM]
| EC Number | KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|---|
| 5.1.1.4 | 0.092 | - |
D-proline | pH 8.0, 50°C, wild-type enzyme | Thermococcus litoralis | |
| 5.1.1.4 | 0.156 | - |
D-proline | pH 8.0, 50°C, mutant enzyme F62V | Thermococcus litoralis | |
| 5.1.1.4 | 0.194 | - |
D-proline | pH 8.0, 50°C, mutant enzyme W241F | Thermococcus litoralis | |
| 5.1.1.4 | 0.612 | - |
D-proline | pH 8.0, 50°C, wild-type enzyme | Clostridioides difficile | |
| 5.1.1.4 | 1.17 | - |
D-proline | pH 8.0, 50°C, wild-type enzyme | Ferroplasma acidarmanus | |
| 5.1.1.4 | 1.21 | - |
L-proline | pH 8.0, 50°C, wild-type enzyme | Thermococcus litoralis | |
| 5.1.1.4 | 1.29 | - |
L-proline | pH 8.0, 50°C, mutant enzyme W241F | Thermococcus litoralis | |
| 5.1.1.4 | 1.93 | - |
L-proline | pH 8.0, 50°C, mutant enzyme F62V | Thermococcus litoralis | |
| 5.1.1.4 | 2.54 | - |
D-proline | pH 8.0, 50°C, mutant enzyme L221H | Thermococcus litoralis | |
| 5.1.1.4 | 4 | - |
D-proline | pH 8.0, 50°C, mutant enzyme F62S | Thermococcus litoralis | |
| 5.1.1.4 | 8.53 | - |
L-proline | pH 8.0, 50°C, wild-type enzyme | Clostridioides difficile | |
| 5.1.1.4 | 20.5 | - |
L-proline | pH 8.0, 50°C, mutant enzyme L221H | Thermococcus litoralis | |
| 5.1.1.4 | 31.6 | - |
L-proline | pH 8.0, 50°C, wild-type enzyme | Ferroplasma acidarmanus | |
| 5.1.1.4 | 53 | - |
L-proline | pH 8.0, 50°C, mutant enzyme F240W | Ferroplasma acidarmanus | |
| 5.1.1.4 | 154 | - |
L-proline | pH 8.0, 50°C, mutant enzyme F62S | Thermococcus litoralis | |
| 5.1.1.8 | 0.502 | - |
trans-3-hydroxy-L-proline | pH 8.0, 50°C, wild-type enzyme | Thermococcus litoralis | |
| 5.1.1.8 | 0.905 | - |
trans-4-hydroxy-L-proline | pH 8.0, 50°C, mutant enzyme F62V | Thermococcus litoralis | |
| 5.1.1.8 | 2.17 | - |
trans-4-hydroxy-L-proline | pH 8.0, 50°C, mutant enzyme F420W | Ferroplasma acidarmanus | |
| 5.1.1.8 | 3.14 | - |
cis-4-hydroxy-D-proline | pH 8.0, 50°C, mutant enzyme F62S | Thermococcus litoralis | |
| 5.1.1.8 | 4.18 | - |
cis-4-hydroxy-D-proline | pH 8.0, 50°C, mutant enzyme L221H | Thermococcus litoralis | |
| 5.1.1.8 | 4.28 | - |
trans-4-hydroxy-L-proline | pH 8.0, 50°C, mutant enzyme W241F | Thermococcus litoralis | |
| 5.1.1.8 | 6.08 | - |
trans-4-hydroxy-L-proline | pH 8.0, 50°C, wild-type enzyme | Thermococcus litoralis | |
| 5.1.1.8 | 6.12 | - |
trans-4-hydroxy-L-proline | pH 8.0, 50°C, wild-type enzyme | Ferroplasma acidarmanus | |
| 5.1.1.8 | 6.22 | - |
trans-4-hydroxy-L-proline | pH 8.0, 50°C, mutant enzyme F62S | Thermococcus litoralis | |
| 5.1.1.8 | 6.5 | - |
trans-4-hydroxy-L-proline | pH 8.0, 50°C, mutant enzyme L221H | Thermococcus litoralis | |
| 5.1.1.8 | 6.65 | - |
cis-4-hydroxy-D-proline | pH 8.0, 50°C, wild-type enzyme | Thermococcus litoralis | |
| 5.1.1.8 | 6.7 | - |
cis-4-hydroxy-D-proline | pH 8.0, 50°C, mutant enzyme W241F | Thermococcus litoralis | |
| 5.1.1.8 | 16.4 | - |
trans-3-hydroxy-L-proline | pH 8.0, 50°C, mutant enzyme W241F | Thermococcus litoralis | |
Molecular Weight [Da]
| EC Number | Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
|---|---|---|---|---|
| 5.1.1.4 | 40000 | - |
x * 40000, SDS-PAGE | Clostridioides difficile |
| 5.1.1.4 | 40000 | - |
x * 40000, SDS-PAGE | Thermococcus litoralis |
| 5.1.1.4 | 40000 | - |
x * 40000, SDS-PAGE | Ferroplasma acidarmanus |
| 5.1.1.4 | 42000 | - |
x * 42000, SDS-PAGE | Haloarcula japonica |
| 5.1.1.4 | 80000 | - |
gel filtration | Clostridioides difficile |
| 5.1.1.4 | 80000 | - |
gel filtration | Thermococcus litoralis |
| 5.1.1.4 | 80000 | - |
gel filtration | Haloarcula japonica |
| 5.1.1.4 | 80000 | - |
gel filtration | Ferroplasma acidarmanus |
| 5.1.1.8 | 40000 | - |
x * 40000, SDS-PAGE | Thermococcus litoralis |
| 5.1.1.8 | 40000 | - |
x * 40000, SDS-PAGE | Ferroplasma acidarmanus |
| 5.1.1.8 | 80000 | - |
gel filtration | Thermococcus litoralis |
| 5.1.1.8 | 80000 | - |
gel filtration | Ferroplasma acidarmanus |
Organism
| EC Number | Organism | UniProt | Comment | Textmining |
|---|---|---|---|---|
| 5.1.1.4 | Clostridioides difficile | Q17ZY4 | - |
- |
| 5.1.1.4 | Ferroplasma acidarmanus | S0APF4 | - |
- |
| 5.1.1.4 | Haloarcula japonica | M0LMI3 | - |
- |
| 5.1.1.4 | Haloarcula japonica DSM 6131 | M0LMI3 | - |
- |
| 5.1.1.4 | Thermococcus litoralis | H3ZMH5 | - |
- |
| 5.1.1.4 | Thermococcus litoralis DSM 5473 | H3ZMH5 | - |
- |
| 5.1.1.8 | Ferroplasma acidarmanus | S0APF4 | - |
- |
| 5.1.1.8 | Thermococcus litoralis | H3ZMH5 | - |
- |
| 5.1.1.8 | Thermococcus litoralis DSM 5473 | H3ZMH5 | - |
- |
Purification (Commentary)
| EC Number | Purification (Comment) | Organism |
|---|---|---|
| 5.1.1.4 | - |
Clostridioides difficile |
| 5.1.1.4 | - |
Thermococcus litoralis |
| 5.1.1.4 | - |
Haloarcula japonica |
| 5.1.1.4 | - |
Ferroplasma acidarmanus |
| 5.1.1.8 | - |
Thermococcus litoralis |
| 5.1.1.8 | - |
Ferroplasma acidarmanus |
Substrates and Products (Substrate)
| EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 5.1.1.4 | D-proline | the reaction is completely bi-directional, and the reverse reactions. The specific activity with D-proline is 130% compared to the L-enantiomer. The bifunctional enzyme reversibly catalyzes the racemization of proline and the epimerization of 4-hydroxyproline and 3-hydroxyproline with similar kinetic constants. Catalysis is based on the same 1,1-proton transfer mechanism using two general acidic/basic cysteine residues located on opposite faces of the active site | Thermococcus litoralis | L-proline | - |
? | |
| 5.1.1.4 | D-proline | the reaction is completely bi-directional, and the reverse reactions. The specific activity with D-proline is 130% compared to the L-enantiomer. The bifunctional enzyme reversibly catalyzes the racemization of proline and the epimerization of 4-hydroxyproline and 3-hydroxyproline with similar kinetic constants. Catalysis is based on the same 1,1-proton transfer mechanism using two general acidic/basic cysteine residues located on opposite faces of the active site | Thermococcus litoralis DSM 5473 | L-proline | - |
? | |
| 5.1.1.4 | L-azetidine-2-carboxylate | low activity | Thermococcus litoralis | D-azetidine-2-carboxylate | - |
? | |
| 5.1.1.4 | L-azetidine-2-carboxylate | low activity | Thermococcus litoralis DSM 5473 | D-azetidine-2-carboxylate | - |
? | |
| 5.1.1.4 | L-pipecolate | low activity | Thermococcus litoralis | D-pipecolate | - |
? | |
| 5.1.1.4 | L-pipecolate | low activity | Thermococcus litoralis DSM 5473 | D-pipecolate | - |
? | |
| 5.1.1.4 | L-proline | - |
Clostridioides difficile | D-proline | - |
r | |
| 5.1.1.4 | L-proline | kcat/Km value for trans-4-hydroxy-L-proline is about 3fold lower than that for L-proline, which is attributed to a 17fold lower kcat value. The kinetic parameters of the epimerization of cis-4-hydroxy-D-proline can not be determined | Ferroplasma acidarmanus | D-proline | - |
r | |
| 5.1.1.4 | L-proline | the enzyme can utilize both proline and hydroxyprolines as substrate | Haloarcula japonica | D-proline | - |
r | |
| 5.1.1.4 | L-proline | the reaction is completely bi-directional, and the reverse reactions. The specific activity with D-proline is 130% compared to the L-enantiomer. The bifunctional enzyme reversibly catalyzes the racemization of proline and the epimerization of 4-hydroxyproline and 3-hydroxyproline with similar kinetic constants. Catalysis is based on the same 1,1-proton transfer mechanism using two general acidic/basic cysteine residues located on opposite faces of the active site | Thermococcus litoralis | D-proline | - |
r | |
| 5.1.1.4 | L-proline | the reaction is completely bi-directional, and the reverse reactions. The specific activity with D-proline is 130% compared to the L-enantiomer. The bifunctional enzyme reversibly catalyzes the racemization of proline and the epimerization of 4-hydroxyproline and 3-hydroxyproline with similar kinetic constants. Catalysis is based on the same 1,1-proton transfer mechanism using two general acidic/basic cysteine residues located on opposite faces of the active site | Thermococcus litoralis DSM 5473 | D-proline | - |
r | |
| 5.1.1.4 | L-proline | the enzyme can utilize both proline and hydroxyprolines as substrate | Haloarcula japonica DSM 6131 | D-proline | - |
r | |
| 5.1.1.8 | cis-3-hydroxy-L-proline | - |
Thermococcus litoralis | trans-3-hydroxy-D-proline | - |
? | |
| 5.1.1.8 | cis-4-hydroxy-D-proline | the reaction is completely bi-directional. The specific activity with cis-4-hydroxy-D-proline is 160% compared to the L-enantiomer. The bifunctional enzyme reversibly catalyzes the racemization of proline and the epimerization of 4-hydroxyproline and 3-hydroxyproline with similar kinetic constants. The catalytic efficiency (kcat/Km) values for L-proline and trans-4-hydroxy-D-proline are similar, whereas a preference for D-proline over cis-4-hydroxy-D-proline (45fold) is identified and is caused by a 75fold lower Km for D-proline. Catalysis is based on the same 1,1-proton transfer mechanism using two general acidic/basic cysteine residues located on opposite faces of the active site | Thermococcus litoralis | trans-4-hydroxy-L-proline | - |
r | |
| 5.1.1.8 | cis-4-hydroxy-L-proline | the reaction is completely bi-directional. The specific activity with trans-4-hydroxy-D-proline is 97% compared to the L-enantiomer. The bifunctional enzyme reversibly catalyzes the racemization of proline and the epimerization of 4-hydroxyproline and 3-hydroxyproline with similar kinetic constants. Catalysis is based on the same 1,1-proton transfer mechanism using two general acidic/basic cysteine residues located on opposite faces of the active site | Thermococcus litoralis | trans-4-hydroxy-D-proline | - |
r | |
| 5.1.1.8 | L-azetidine-2-carboxylate | low activity | Thermococcus litoralis | D-azetidine-2-carboxylate | - |
? | |
| 5.1.1.8 | L-pipecolate | low activity | Thermococcus litoralis | D-pipecolate | - |
? | |
| 5.1.1.8 | trans-3-hydroxy-L-proline | - |
Thermococcus litoralis | trans-3-hydroxy-D-proline | - |
? | |
| 5.1.1.8 | trans-4-hydroxy-D-proline | the reaction is completely bi-directional. The specific activity with trans-4-hydroxy-D-proline is 97% compared to the L-enantiomer. The bifunctional enzyme reversibly catalyzes the racemization of proline and the epimerization of 4-hydroxyproline and 3-hydroxyproline with similar kinetic constants. Catalysis is based on the same 1,1-proton transfer mechanism using two general acidic/basic cysteine residues located on opposite faces of the active site | Thermococcus litoralis | cis-4-hydroxy-L-proline | - |
r | |
| 5.1.1.8 | trans-4-hydroxy-D-proline | the reaction is completely bi-directional. The specific activity with trans-4-hydroxy-D-proline is 97% compared to the L-enantiomer. The bifunctional enzyme reversibly catalyzes the racemization of proline and the epimerization of 4-hydroxyproline and 3-hydroxyproline with similar kinetic constants. Catalysis is based on the same 1,1-proton transfer mechanism using two general acidic/basic cysteine residues located on opposite faces of the active site | Thermococcus litoralis DSM 5473 | cis-4-hydroxy-L-proline | - |
r | |
| 5.1.1.8 | trans-4-hydroxy-L-proline | kcat/Km value for trans-4-hydroxy-L-proline is about 3fold lower than that for L-proline, which is attributed to a 17fold lower kcat value. The kinetic parameters of the epimerization of cis-4-hydroxy-D-proline can not be determined | Ferroplasma acidarmanus | cis-4-hydroxy-D-proline | - |
r | |
| 5.1.1.8 | trans-4-hydroxy-L-proline | the reaction is completely bi-directional. The specific activity with cis-4-hydroxy-D-proline is 160% compared to the L-enantiomer. The bifunctional enzyme reversibly catalyzes the racemization of proline and the epimerization of 4-hydroxyproline and 3-hydroxyproline with similar kinetic constants. The catalytic efficiency (kcat/Km) values for L-proline and trans-4-hydroxy-D-proline are similar, whereas a preference for D-proline over cis-4-hydroxy-D-proline (45fold) is identified and is caused by a 75fold lower Km for D-proline. Catalysis is based on the same 1,1-proton transfer mechanism using two general acidic/basic cysteine residues located on opposite faces of the active site | Thermococcus litoralis | cis-4-hydroxy-D-proline | - |
r | |
Subunits
| EC Number | Subunits | Comment | Organism |
|---|---|---|---|
| 5.1.1.4 | ? | x * 42000, SDS-PAGE | Haloarcula japonica |
| 5.1.1.4 | ? | x * 40000, SDS-PAGE | Clostridioides difficile |
| 5.1.1.4 | ? | x * 40000, SDS-PAGE | Thermococcus litoralis |
| 5.1.1.4 | ? | x * 40000, SDS-PAGE | Ferroplasma acidarmanus |
| 5.1.1.8 | ? | x * 40000, SDS-PAGE | Thermococcus litoralis |
| 5.1.1.8 | ? | x * 40000, SDS-PAGE | Ferroplasma acidarmanus |
Synonyms
| EC Number | Synonyms | Comment | Organism |
|---|---|---|---|
| 5.1.1.4 | CdProR | - |
Clostridioides difficile |
| 5.1.1.4 | FaProR | - |
Ferroplasma acidarmanus |
| 5.1.1.4 | HjProR | - |
Haloarcula japonica |
| 5.1.1.4 | proline racemase/hydroxyproline epimerase | bifunctional enzyme | Thermococcus litoralis |
| 5.1.1.4 | ProR/HypE | bifunctional enzyme | Thermococcus litoralis |
| 5.1.1.8 | FaProR | - |
Ferroplasma acidarmanus |
| 5.1.1.8 | proline racemase/hydroxyproline epimerase | bifunctional enzyme | Thermococcus litoralis |
| 5.1.1.8 | ProR/HypE | bifunctional enzyme | Thermococcus litoralis |
Temperature Optimum [°C]
| EC Number | Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|---|
| 5.1.1.4 | 50 | - |
assay at | Clostridioides difficile |
| 5.1.1.4 | 50 | - |
assay at | Thermococcus litoralis |
| 5.1.1.4 | 50 | - |
assay at | Haloarcula japonica |
| 5.1.1.4 | 50 | - |
assay at | Ferroplasma acidarmanus |
| 5.1.1.4 | 90 | 100 | - |
Clostridioides difficile |
| 5.1.1.4 | 90 | 100 | - |
Thermococcus litoralis |
| 5.1.1.4 | 90 | 100 | - |
Haloarcula japonica |
| 5.1.1.4 | 90 | 100 | - |
Ferroplasma acidarmanus |
| 5.1.1.8 | 50 | - |
assay at | Thermococcus litoralis |
| 5.1.1.8 | 50 | - |
assay at | Ferroplasma acidarmanus |
| 5.1.1.8 | 90 | 100 | - |
Thermococcus litoralis |
| 5.1.1.8 | 90 | 100 | - |
Ferroplasma acidarmanus |
Turnover Number [1/s]
| EC Number | Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|---|
| 5.1.1.4 | 0.0235 | - |
D-proline | pH 8.0, 50°C, mutant enzyme F62V | Thermococcus litoralis | |
| 5.1.1.4 | 0.026 | - |
D-proline | pH 8.0, 50°C, mutant enzyme F62S | Thermococcus litoralis | |
| 5.1.1.4 | 0.092 | - |
L-proline | pH 8.0, 50°C, mutant enzyme F62V | Thermococcus litoralis | |
| 5.1.1.4 | 0.119 | - |
D-proline | pH 8.0, 50°C, wild-type enzyme | Ferroplasma acidarmanus | |
| 5.1.1.4 | 0.2 | - |
L-proline | pH 8.0, 50°C, mutant enzyme F62S | Thermococcus litoralis | |
| 5.1.1.4 | 0.29 | - |
D-proline | pH 8.0, 50°C, mutant enzyme L221H | Thermococcus litoralis | |
| 5.1.1.4 | 0.42 | - |
L-proline | pH 8.0, 50°C, mutant enzyme F240W | Ferroplasma acidarmanus | |
| 5.1.1.4 | 0.6 | - |
L-proline | pH 8.0, 50°C, wild-type enzyme | Ferroplasma acidarmanus | |
| 5.1.1.4 | 0.92 | - |
L-proline | pH 8.0, 50°C, mutant enzyme L221H | Thermococcus litoralis | |
| 5.1.1.4 | 2.22 | - |
D-proline | pH 8.0, 50°C, wild-type enzyme | Thermococcus litoralis | |
| 5.1.1.4 | 2.48 | - |
D-proline | pH 8.0, 50°C, wild-type enzyme | Clostridioides difficile | |
| 5.1.1.4 | 2.78 | - |
L-proline | pH 8.0, 50°C, wild-type enzyme | Thermococcus litoralis | |
| 5.1.1.4 | 3.17 | - |
L-proline | pH 8.0, 50°C, mutant enzyme W241F | Thermococcus litoralis | |
| 5.1.1.4 | 3.18 | - |
D-proline | pH 8.0, 50°C, mutant enzyme W241F | Thermococcus litoralis | |
| 5.1.1.4 | 14.15 | - |
L-proline | pH 8.0, 50°C, wild-type enzyme | Clostridioides difficile | |
| 5.1.1.8 | 0.012 | - |
trans-4-hydroxy-L-proline | pH 8.0, 50°C, mutant enzyme F420W | Ferroplasma acidarmanus | |
| 5.1.1.8 | 0.014 | - |
cis-4-hydroxy-D-proline | pH 8.0, 50°C, mutant enzyme F62S | Thermococcus litoralis | |
| 5.1.1.8 | 0.039 | - |
trans-4-hydroxy-L-proline | pH 8.0, 50°C, mutant enzyme F62S | Thermococcus litoralis | |
| 5.1.1.8 | 0.0395 | - |
trans-4-hydroxy-L-proline | pH 8.0, 50°C, wild-type enzyme | Ferroplasma acidarmanus | |
| 5.1.1.8 | 0.11 | - |
cis-4-hydroxy-D-proline | pH 8.0, 50°C, mutant enzyme L221H | Thermococcus litoralis | |
| 5.1.1.8 | 0.13 | - |
trans-4-hydroxy-L-proline | pH 8.0, 50°C, mutant enzyme F62V | Thermococcus litoralis | |
| 5.1.1.8 | 0.29 | - |
trans-3-hydroxy-L-proline | pH 8.0, 50°C, mutant enzyme W241F | Thermococcus litoralis | |
| 5.1.1.8 | 0.65 | - |
trans-4-hydroxy-L-proline | pH 8.0, 50°C, mutant enzyme L221H | Thermococcus litoralis | |
| 5.1.1.8 | 0.69 | - |
cis-4-hydroxy-D-proline | pH 8.0, 50°C, mutant enzyme W241F | Thermococcus litoralis | |
| 5.1.1.8 | 1.53 | - |
trans-4-hydroxy-L-proline | pH 8.0, 50°C, mutant enzyme W241F | Thermococcus litoralis | |
| 5.1.1.8 | 3.6 | - |
trans-3-hydroxy-L-proline | pH 8.0, 50°C, wild-type enzyme | Thermococcus litoralis | |
| 5.1.1.8 | 3.83 | - |
cis-4-hydroxy-D-proline | pH 8.0, 50°C, wild-type enzyme | Thermococcus litoralis | |
| 5.1.1.8 | 12.13 | - |
trans-4-hydroxy-L-proline | pH 8.0, 50°C, wild-type enzyme | Thermococcus litoralis | |
pH Optimum
| EC Number | pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|---|
| 5.1.1.4 | 8 | - |
assay at | Clostridioides difficile |
| 5.1.1.4 | 8 | - |
assay at | Thermococcus litoralis |
| 5.1.1.4 | 8 | - |
assay at | Haloarcula japonica |
| 5.1.1.4 | 8 | - |
assay at | Ferroplasma acidarmanus |
| 5.1.1.8 | 8 | - |
assay at | Thermococcus litoralis |
| 5.1.1.8 | 8 | - |
assay at | Ferroplasma acidarmanus |
IC50 Value
| EC Number | IC50 Value | IC50 Value Maximum | Comment | Organism | Inhibitor | Structure |
|---|---|---|---|---|---|---|
| 5.1.1.4 | 0.217 | - |
pH 8.0, 50°C | Thermococcus litoralis | pyrrole-2-carboxylate | |
| 5.1.1.4 | 0.269 | - |
pH 8.0, 50°C | Clostridioides difficile | pyrrole-2-carboxylate | |
| 5.1.1.4 | 0.295 | - |
pH 8.0, 50°C | Haloarcula japonica | pyrrole-2-carboxylate | |
| 5.1.1.4 | 0.58 | - |
pH 8.0, 50°C | Ferroplasma acidarmanus | pyrrole-2-carboxylate | |
| 5.1.1.8 | 0.217 | - |
pH 8.0, 50°C | Thermococcus litoralis | pyrrole-2-carboxylate | |
| 5.1.1.8 | 0.58 | - |
pH 8.0, 50°C | Ferroplasma acidarmanus | pyrrole-2-carboxylate | |
kcat/KM [mM/s]
| EC Number | kcat/KM Value [1/mMs-1] | kcat/KM Value Maximum [1/mMs-1] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|---|
| 5.1.1.4 | 0.0013 | - |
L-proline | pH 8.0, 50°C, mutant enzyme F62S | Thermococcus litoralis | |
| 5.1.1.4 | 0.0065 | - |
D-proline | pH 8.0, 50°C, mutant enzyme F62S | Thermococcus litoralis | |
| 5.1.1.4 | 0.0079 | - |
L-proline | pH 8.0, 50°C, mutant enzyme F240W | Ferroplasma acidarmanus | |
| 5.1.1.4 | 0.019 | - |
L-proline | pH 8.0, 50°C, wild-type enzyme | Ferroplasma acidarmanus | |
| 5.1.1.4 | 0.045 | - |
L-proline | pH 8.0, 50°C, mutant enzyme L221H | Thermococcus litoralis | |
| 5.1.1.4 | 0.048 | - |
L-proline | pH 8.0, 50°C, mutant enzyme F62V | Thermococcus litoralis | |
| 5.1.1.4 | 0.1 | - |
D-proline | pH 8.0, 50°C, wild-type enzyme | Ferroplasma acidarmanus | |
| 5.1.1.4 | 0.11 | - |
D-proline | pH 8.0, 50°C, mutant enzyme L221H | Thermococcus litoralis | |
| 5.1.1.4 | 0.15 | - |
D-proline | pH 8.0, 50°C, mutant enzyme F62V | Thermococcus litoralis | |
| 5.1.1.4 | 1.65 | - |
L-proline | pH 8.0, 50°C, wild-type enzyme | Clostridioides difficile | |
| 5.1.1.4 | 2.3 | - |
L-proline | pH 8.0, 50°C, wild-type enzyme | Thermococcus litoralis | |
| 5.1.1.4 | 2.45 | - |
L-proline | pH 8.0, 50°C, mutant enzyme W241F | Thermococcus litoralis | |
| 5.1.1.4 | 4.08 | - |
D-proline | pH 8.0, 50°C, wild-type enzyme | Clostridioides difficile | |
| 5.1.1.4 | 16.5 | - |
D-proline | pH 8.0, 50°C, mutant enzyme W241F | Thermococcus litoralis | |
| 5.1.1.4 | 26.2 | - |
D-proline | pH 8.0, 50°C, wild-type enzyme | Thermococcus litoralis | |
| 5.1.1.8 | 0.0046 | - |
cis-4-hydroxy-D-proline | pH 8.0, 50°C, mutant enzyme F62S | Thermococcus litoralis | |
| 5.1.1.8 | 0.0055 | - |
trans-4-hydroxy-L-proline | pH 8.0, 50°C, mutant enzyme F420W | Ferroplasma acidarmanus | |
| 5.1.1.8 | 0.0063 | - |
trans-4-hydroxy-L-proline | pH 8.0, 50°C, mutant enzyme F62S | Thermococcus litoralis | |
| 5.1.1.8 | 0.0065 | - |
trans-4-hydroxy-L-proline | pH 8.0, 50°C, wild-type enzyme | Ferroplasma acidarmanus | |
| 5.1.1.8 | 0.027 | - |
cis-4-hydroxy-D-proline | pH 8.0, 50°C, mutant enzyme L221H | Thermococcus litoralis | |
| 5.1.1.8 | 0.1 | - |
trans-4-hydroxy-L-proline | pH 8.0, 50°C, mutant enzyme L221H | Thermococcus litoralis | |
| 5.1.1.8 | 0.1 | - |
cis-4-hydroxy-D-proline | pH 8.0, 50°C, mutant enzyme W241F | Thermococcus litoralis | |
| 5.1.1.8 | 0.14 | - |
trans-4-hydroxy-L-proline | pH 8.0, 50°C, mutant enzyme F62V | Thermococcus litoralis | |
| 5.1.1.8 | 0.18 | - |
trans-3-hydroxy-L-proline | pH 8.0, 50°C, mutant enzyme W241F | Thermococcus litoralis | |
| 5.1.1.8 | 0.36 | - |
trans-4-hydroxy-L-proline | pH 8.0, 50°C, mutant enzyme W241F | Thermococcus litoralis | |
| 5.1.1.8 | 0.58 | - |
cis-4-hydroxy-D-proline | pH 8.0, 50°C, wild-type enzyme | Thermococcus litoralis | |
| 5.1.1.8 | 2.03 | - |
trans-4-hydroxy-L-proline | pH 8.0, 50°C, wild-type enzyme | Thermococcus litoralis | |
| 5.1.1.8 | 7.2 | - |
trans-3-hydroxy-L-proline | pH 8.0, 50°C, wild-type enzyme | Thermococcus litoralis | |
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Release 2023.1 (January 2023)
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