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PMID: 8192670 Published · ppublish English Journal Article

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

The Biochemical journal ·Vol. 299 ( Pt 3) ·1994-05-01 ·Pages 805-11

Bruce NC, Willey DL, Coulson AF, Jeffery J

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.

MeSH Terms
Alcohol Oxidoreductases/chemistry,classification,metabolism Aldehyde Reductase/chemistry,metabolism Amino Acid Sequence Base Sequence Binding Sites Coenzymes/metabolism DNA, Complementary Humans Hydrogen/chemistry Molecular Sequence Data NAD (+) and NADP (+) Dependent Alcohol Oxidoreductases Prostaglandin-Endoperoxide Synthases/chemistry,metabolism Protein Conformation Pseudomonas putida/enzymology Sequence Alignment
Chemicals
Coenzymes DNA, Complementary Hydrogen Alcohol Oxidoreductases NAD (+) and NADP (+) Dependent Alcohol Oxidoreductases Aldehyde Reductase morphine 6-dehydrogenase chlordecone reductase Prostaglandin-Endoperoxide Synthases
Authors & Affiliations
4 authors, click to expand affiliations / ORCID
Bruce N C
Institute of Biotechnology, University of Cambridge, U.K.
Willey D L
Coulson A F
Jeffery J
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44 references, click to expand
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Article Info
Journal
The Biochemical journal
Abbr.
Biochem J
ISSN
0264-6021
DOI
10.1042/bj2990805
Published
1994-05-01
Pages
805-11
Language
English
Region
England
NLM ID
2984726R
PMCID
PMC1138092
Subset
IM
External Links
PubMed source DOI: 10.1042/bj2990805 PMC Full Text View journal details
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