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Results 1 - 7 of 7
EC Number General Information Commentary Reference
Display the word mapDisplay the reaction diagram Show all sequences 5.4.99.11evolution the enzyme belongs to the glycoside hydrolase family 13 (GH13) in the CAZy classification 726588
Display the word mapDisplay the reaction diagram Show all sequences 5.4.99.11more active site structure and substrate and ligand binding structures, overview 726588
Display the word mapDisplay the reaction diagram Show all sequences 5.4.99.11more enzyme-substrate complex, docking study with sucrose and fructose -, 727307
Display the word mapDisplay the reaction diagram Show all sequences 5.4.99.11more proteins AS9 PalI and SmuA differ in only one amino acid, structure of the wild-type sucrose isomerases is obtained by single point mutation through pymol using the crystal structure of SmuA from Protaminobacter rubrum strain CBS 547.77 (PDB ID 3GBD). Homology models of structures of the mutant sucrose isomerases are constructed based on the crystal structure of SmuA, using the EMBL-EBI server -, 749077
Display the word mapDisplay the reaction diagram Show all sequences 5.4.99.11more structural basis for the product specificity of NX-5, docking of fructofuranose and fructopyranose into the active site of the enzyme mutant D241A-glucose complex, molecular dynamics simulations, molecular mechanism controlling sucrose isomer formation, overview. Phe297 and Phe321 in enzyme NX-5 form an aromatic clamp near the entrance of the active pocket. Residues Asp102, His145, Arg239, His368, Asp369, Glu428, and Arg456 are responsible for sucrose binding and residues Asp241 (the nucleophile) and Glu295 (the acid catalyst) are crucial for sucrose hydrolysis. The active site pocket is stabilized by the salt bridge interactions between Arg239-Asp241, Asp102-Arg456 and Asp369-Arg456. Residues Arg325 and Arg328 are located in the325RLDRD329 motif and play roles in the product specificity -, 728625
Display the word mapDisplay the reaction diagram Show all sequences 5.4.99.11more the unique RLDRD motif is located in a loop adjacent to the active site cleft and is determined to play an important role in the isomerization process and in the control of product specificity -, 746878
Display the word mapDisplay the reaction diagram Show all sequences 5.4.99.11physiological function physiological functions of isomaltulose and biochemical properties of sucrose isomerases, as well as biological isomaltulose production from sucrose using sucrose isomerase, overview -, 746878
Results 1 - 7 of 7