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Evolution of cytochrome P-450 proteins
1Department of Biochemistry and Molecular Biology, University of Texas Medical School, Houston 77225.
Molecular Biology and Evolution
|November 1, 1987
Summary
This study reveals the evolutionary history of cytochrome P-450 proteins, identifying eight families and 16 gene duplications. Early duplications led to organelle-specific enzymes, while later ones specialized in drug metabolism.
Area of Science:
- Biochemistry
- Evolutionary Biology
- Genomics
Background:
- Cytochrome P-450 proteins are crucial enzymes involved in metabolizing diverse compounds.
- Understanding their evolutionary history provides insights into their functional diversification.
Purpose of the Study:
- To reconstruct the evolutionary relationships and identify gene duplication events within the cytochrome P-450 superfamily.
- To infer the ancestral functions and evolutionary timeline of different cytochrome P-450 families.
Main Methods:
- Alignment of 34 cytochrome P-450 sequences from bacterial and vertebrate species using a computer algorithm.
- Construction of phylogenetic trees using unweighted-pair-group and neighbor-joining methods.
Main Results:
- Phylogenetic analysis revealed eight distinct cytochrome P-450 families with 16 identified gene duplication events.
- The earliest duplication (~1,360 Mybp) separated mitochondrial and endoplasmic reticulum P-450s, both utilizing cholesterol.
- A significant duplication (~900 Mybp) led to drug-metabolizing P-450s, followed by 11 further duplications in this lineage.
Conclusions:
- The cytochrome P-450 superfamily evolved through extensive gene duplication, leading to specialized functions in metabolism and detoxification.
- The evolution of drug-metabolizing P-450s is a key event, with accelerated evolution noted in avian-mammalian lineages.