EC Number   |
General Information |
Reference |
|---|
  1.1.1.422 | evolution |
ephedrine dehydrogenase (EDH) from Arthrobacter sp. TS-15 is an NADH-dependent member of the oxidoreductase superfamily of short-chain dehydrogenases/reductases (SDRs) |
752351 |
| 1.1.1.422 | evolution |
the enzyme belongs to the superfamily of short-chain dehydrogenases |
755862 |
| 1.1.1.422 | metabolism |
the enzyme is involved in the ephedrine metabolism, overview |
755862 |
| 1.1.1.422 | more |
a model of the active site in complex with NAD+ and 1-phenyl-1,2-propanedione suggests key roles for S143 and W152 in recognition of the substrate and positioning for the reduction reaction. The typical catalytic tetrad of the superfamily SDR consisting of N113, S141, Y155, and K159 residues. K159 interacts with the nicotinamide ribose of the cofactor and decreases the pKa of the -OH group of Y155 initiating the hydrogen transfer. Y155 acts as catalytic base, and S141 stabilizes the substrate. N113 interacts with K159 via a water molecule to create a network of hydrogen bonds between cofactor, catalytic side chains, and water molecules |
752351 |
| 1.1.1.422 | physiological function |
Arthrobacter sp. TS-15 is capable of metabolizing all isomers of ephedrine as a sole source of carbon and energy. Enantioselective oxidation of (-)-(R,N)-(pseudo)ephedrine and (+)-(S,N)-(pseudo)ephedrine catalyzed by PseDH and EDH, respectively, overview |
755862 |
