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.
Bacterial morphine dehydrogenase further defines a distinct superfamily of oxidoreductases with diverse functional activities.
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N C Bruce, D L Willey, A F Coulson, J Jeffery; Bacterial morphine dehydrogenase further defines a distinct superfamily of oxidoreductases with diverse functional activities.. Biochem J 1 May 1994; 299 (3): 805–811. doi: https://doi.org/10.1042/bj2990805
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