1.1.1.B20	evolution	Bdh enzymes can be classified into R-acting or S-acting depending on the chirality of the chiral center introduced by the enzyme at the acetoin C2 atom. Whereas the preference for (3R)-acetoin or (3S)-acetoin is imprinted in the geometry of the substrate-binding pocket, R-acting and S-acting Bdh enzymes belong to different protein families and possess different architectures	-, 760761	
1.1.1.B20	evolution	enzyme BDH belongs to the SDR family, of enzymes	741710	
1.1.1.B20	evolution	enzyme BtBDH contains a GroES-like domain at the N terminus and a NAD(P)-binding domain at the C-terminus. Phylogenetic tree analysis reveals that BtBDH is a member ofthe (2R,3R)-2,3-BDH group. BtBDH has the typical (2R,3R)-2,3-butanediol dehydrogenase properties and belongs to the MDR superfamily. According to previous reports, (2R,3R)-2,3-BDH generally belongs to the MDR family, while meso-2,3-BDH is commonly clustered in the SDR (short chain dehydrogenase/reductase) family	-, 760463	
1.1.1.B20	evolution	phylogenetic analysis	702809	
1.1.1.B20	evolution	the enzyme belongs to the NADH-dependent metal-independent short-chain dehydrogenases/reductase (SDR) family of oxidoreductases	-, 760817	
1.1.1.B20	evolution	the enzyme belongs to the short chain dehydrogenase/reductase family	-, 721906	
1.1.1.B20	evolution	the enzyme belongs to the short-chain dehydrogenases/reductases	761081	
1.1.1.B20	evolution	the enzyme belongs to the shortchain dehydrogenase/reductase superfamily	-, 721397	
1.1.1.B20	malfunction	deletion of bdhA gene successfully blocks the reversible transformation between acetoin and 2,3-butanediol and eliminates the effect of dissolved oxygen on the transformation	-, 762259	
1.1.1.B20	malfunction	deletion of budC causes redox imbalance towards NADH	-, 761003