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alcohol dehydrogenase catalytic domain-containing protein
This is the catalytic domain of alcohol dehydrogenases. Many of them contain an inserted zinc binding domain. This domain has a GroES-like structure [1-2]. [1]. 8804825. Structural classification of proteins: new superfamilies. Murzin AG;. Curr Opin Struct Biol 1996;6:386-394. [2]. 10556240. Conserved structural features and sequence patterns in the GroES fold family. Taneja B, Mande SC;. Protein Eng 1999;12:815-818. (from Pfam)
zinc-binding dehydrogenase
glutathione-independent formaldehyde dehydrogenase
glutathione-independent formaldehyde dehydrogenase is a zinc-dependent/medium chain alcohol dehydrogenase family protein that catalyzes the NAD(+)-dependent oxidation of formaldehyde and acetoaldehyde, and to a lesser extent, long-chain alcohols, and the dismutation of a wide range of aldehydes such as formaldehyde
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