EC Number |
General Information |
Reference |
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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 |