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


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.

SUBMITTER: Bruce NC 

PROVIDER: S-EPMC1138092 | biostudies-other | 1994 May

REPOSITORIES: biostudies-other

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