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Results 1 - 6 of 6
EC Number Protein Variants Commentary Reference
Display the word mapDisplay the reaction diagram Show all sequences 5.1.1.8C236S radical loss of OH-L/D-Pro epimerization 676749
Display the word mapDisplay the reaction diagram Show all sequences 5.1.1.8C88S radical loss of OH-L/D-Pro epimerization 676749
Display the word mapDisplay the reaction diagram Show all sequences 5.1.1.8F240W mutant enzyme shows similar kinetic constants for proline and hydroxyproline as compared to the wild-type enzyme 730678
Display the word mapDisplay the reaction diagram Show all sequences 5.1.1.8V60F radical loss of OH-L/D-Pro epimerization. V60 residue accounts for OH-Pro ligand specificity 676749
Display the word mapDisplay the reaction diagram Show all sequences 5.1.1.8V60G almost complete loss of epimerization of trans-4-hydroxy-L-Pro, some residual activity on trans-4-hydroxy-D-Pro. V60 residue accounts for OH-Pro ligand specificity 676749
Display the word mapDisplay the reaction diagram Show all sequences 5.1.1.8W241F 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) -, 730678
Results 1 - 6 of 6