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Results 1 - 8 of 8
EC Number Natural Substrates Commentary (Nat. Sub.)
Show all pathways known for 1.1.99.21Display the word mapDisplay the reaction diagram Show all sequences 1.1.99.21D-glucitol + NAD+ -
Show all pathways known for 1.1.99.21Display the word mapDisplay the reaction diagram Show all sequences 1.1.99.21D-sorbitol + acceptor -
Show all pathways known for 1.1.99.21Display the word mapDisplay the reaction diagram Show all sequences 1.1.99.21D-sorbitol + acceptor high specificity
Show all pathways known for 1.1.99.21Display the word mapDisplay the reaction diagram Show all sequences 1.1.99.21D-sorbitol + acceptor D-sorbitol is oxidized in the periplasm in a chemo-, regio-, and stereoselective manner to L-sorbose by the membrane-bound dehydrogenase
Show all pathways known for 1.1.99.21Display the word mapDisplay the reaction diagram Show all sequences 1.1.99.21D-sorbitol + NADP+ -
Show all pathways known for 1.1.99.21Display the word mapDisplay the reaction diagram Show all sequences 1.1.99.21L-glucitol + NAD+ 90% conversion
Show all pathways known for 1.1.99.21Display the word mapDisplay the reaction diagram Show all sequences 1.1.99.21more production of 5-keto-D-gluconate is solely dependent on enzyme
Show all pathways known for 1.1.99.21Display the word mapDisplay the reaction diagram Show all sequences 1.1.99.21more this SLDH is distinguished from other L-sorbose-producing enzymes by its high activity and substrate specificity. Isothermal titration calorimetry shows that the protein binds more strongly to D-sorbitol than other L-sorbose-producing enzymes, and substrate docking analysis confirms a higher turnover rate
Results 1 - 8 of 8