Autor: |
Jillian Hagel, Peter Facchini |
Jazyk: |
angličtina |
Rok vydání: |
2010 |
Předmět: |
|
Zdroj: |
Frontiers in Physiology, Vol 1 (2010) |
Druh dokumentu: |
article |
ISSN: |
1664-042X |
DOI: |
10.3389/fphys.2010.00014 |
Popis: |
Demethylases play a pivitol role in numerous biological processes from covalent histone modification and DNA repair to specialized metabolism in plants and microorganisms. Enzymes that catalyze O- and N-demethylation include 2-oxoglutarate (2OG)/Fe(II)-dependent dioxygenases, cytochromes P450, Rieske-domain proteins and flavin adenine dinucleotide (FAD)-dependent oxidases. Proposed mechanisms for demethylation by 2OG/Fe(II)-dependent enzymes involve hydroxylation at the O- or N-linked methyl group followed by formaldehyde elimination. Members of this enzyme family catalyze a wide variety of reactions in diverse plant metabolic pathways. Recently, we showed that 2OG/Fe(II)-dependent dioxygenases catalyze the unique O-demethylation steps of morphine biosynthesis in opium poppy, which provides a rational basis for the widespread occurrence of demethylases in benzylisoquinoline alkaloid metabolism. |
Databáze: |
Directory of Open Access Journals |
Externí odkaz: |
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