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EC Number Substrates Commentary Substrates Organism Products Commentary (Products) Reversibility
Display the word mapDisplay the reaction diagram Show all sequences 5.1.1.83-allohydroxy-D-Pro - Pseudomonas putida 3-allohydroxy-L-Pro - r
Display the word mapDisplay the reaction diagram Show all sequences 5.1.1.83-allohydroxy-L-Pro - Pseudomonas putida 3-allohydroxy-D-Pro - r
Display the word mapDisplay the reaction diagram Show all sequences 5.1.1.83-hydroxy-L-Pro - Pseudomonas putida 3-hydroxy-D-Pro - ?
Display the word mapDisplay the reaction diagram Show all sequences 5.1.1.8Allohydroxy-D-Pro - Pseudomonas putida Allohydroxy-L-Pro - ?
Display the word mapDisplay the reaction diagram Show all sequences 5.1.1.8cis-3-hydroxy-L-proline - Thermococcus litoralis trans-3-hydroxy-D-proline - ?
Display the word mapDisplay the reaction diagram Show all sequences 5.1.1.8cis-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
Display the word mapDisplay the reaction diagram Show all sequences 5.1.1.8cis-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
Display the word mapDisplay the reaction diagram Show all sequences 5.1.1.8D-Ala at 1-2% of the activity relative to allo-D-hydroxy-proline epimerization Pseudomonas putida L-Ala - ?
Display the word mapDisplay the reaction diagram Show all sequences 5.1.1.8Hydroxy-L-Pro - Pseudomonas putida ? - ?
Display the word mapDisplay the reaction diagram Show all sequences 5.1.1.8Hydroxy-L-Pro trans-hydroxy-L-Pro or cis-hydroxy-L-Pro, initial reaction of the pathway of hydroxyproline metabolism Pseudomonas putida ? - ?
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