EC Number |
Substrates |
Organism |
Products |
Reversibility |
---|
5.1.1.8 | 3-allohydroxy-D-Pro |
- |
Pseudomonas putida |
3-allohydroxy-L-Pro |
- |
r |
5.1.1.8 | 3-allohydroxy-L-Pro |
- |
Pseudomonas putida |
3-allohydroxy-D-Pro |
- |
r |
5.1.1.8 | 3-hydroxy-L-Pro |
- |
Pseudomonas putida |
3-hydroxy-D-Pro |
- |
? |
5.1.1.8 | Allohydroxy-D-Pro |
- |
Pseudomonas putida |
Allohydroxy-L-Pro |
- |
? |
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 | D-Ala |
at 1-2% of the activity relative to allo-D-hydroxy-proline epimerization |
Pseudomonas putida |
L-Ala |
- |
? |
5.1.1.8 | Hydroxy-L-Pro |
- |
Pseudomonas putida |
? |
- |
? |
5.1.1.8 | Hydroxy-L-Pro |
trans-hydroxy-L-Pro or cis-hydroxy-L-Pro, initial reaction of the pathway of hydroxyproline metabolism |
Pseudomonas putida |
? |
- |
? |