Bacterial morphine dehydrogenase further defines a distinct superfamily of oxidoreductases with diverse functional activities.
Pseudomonas putida morphine dehydrogenase is shown to be closely homologous to 18 proteins, defining a superfamily within which morphine dehydrogenase particularly resembles two bacterial, 2,5-dioxo-D-gluconic acid reductases, and two eukaryotic proteins of unknown functions. Relationships within the superfamily are extensive and complex. Residue identities between protein pairs range from 29-90%. Three subgroups are proposed. Nevertheless, on the basis of residue conservations/exchanges it is suggested that the nicotinamide coenzyme binding and substrate reduction occur in all the enzymes by broadly analogous mechanisms, among which some probable differences are identified.
Bruce
N C
NC
Institute of Biotechnology, University of Cambridge, U.K.
Willey
D L
DL
Coulson
A F
AF
Jeffery
J
J
D000429:Alcohol Oxidoreductases / Q000737:chemistry / Q000145:classification / Q000378:metabolism*; D000449:Aldehyde Reductase / Q000737:chemistry / Q000378:metabolism; D000595:Amino Acid Sequence; D001483:Base Sequence; D001665:Binding Sites; D003067:Coenzymes / Q000378:metabolism; D018076:DNA, Complementary; D006801:Humans; D006859:Hydrogen / Q000737:chemistry; D008969:Molecular Sequence Data; D064430:NAD (+) and NADP (+) Dependent Alcohol Oxidoreductases; D011451:Prostaglandin-Endoperoxide Synthases / Q000737:chemistry / Q000378:metabolism; D011487:Protein Conformation; D016958:Pseudomonas putida / Q000201:enzymology*; D016415:Sequence Alignment
D003067:Coenzymes; D018076:DNA, Complementary; D006859:Hydrogen; D000429:Alcohol Oxidoreductases; D064430:NAD (+) and NADP (+) Dependent Alcohol Oxidoreductases; D000449:Aldehyde Reductase; C045221:morphine 6-dehydrogenase; C048321:chlordecone reductase; D011451:Prostaglandin-Endoperoxide Synthases