Ephedrine dehydrogenase
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In enzymology, ephedrine dehydrogenase (EC 1.5.1.18) is an enzyme that catalyzes the chemical reaction
| ephedrine dehydrogenase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 1.5.1.18 | ||||||||
| CAS no. | 73508-06-2 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| Gene Ontology | AmiGO / QuickGO | ||||||||
| |||||||||
The two substrates of this enzyme are ephedrine and oxidised nicotinamide adenine dinucleotide (NAD+). This forms an imine intermediate which spontaneously hydrolyses to give (-)-phenylacetylcarbinol and methylamine.[1] The enzyme was isolated from a strain of the soil bacterium Pseudomonas putida which uses ephedrine as its sole source of carbon.[2]
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-NH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is (-)-ephedrine:NAD+ 2-oxidoreductase.
