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This research investigates the capability of native amine dehydrogenases (nat-AmDHs) to directly reduce carbonyl compounds to alcohols without ammonia, revealing significant ketoreductase (KRED) activity under these conditions. The study highlights the structural features influencing this activity and demonstrates the heterogeneity of KRED performance across various enzyme-substrate pairs. Kinetic analyses indicate that while nat-AmDHs exhibit notable KRED activity, their reverse reaction of alcohol oxidati

Author

shajutirahman60

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EN