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. 1994 May 1;299(Pt 3):805–811. doi: 10.1042/bj2990805

Bacterial morphine dehydrogenase further defines a distinct superfamily of oxidoreductases with diverse functional activities.

N C Bruce 1, D L Willey 1, A F Coulson 1, J Jeffery 1
PMCID: PMC1138092  PMID: 8192670

Abstract

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.

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Selected References

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