FeII/α-ketoglutarate hydroxylases involved in nucleobase, nucleoside, nucleotide, and chromatin metabolism
| Autor: | Tina A. Müller, Jana M. Simmons, Robert P. Hausinger |
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| Jazyk: | angličtina |
| Rok vydání: | 2008 |
| Předmět: |
Models
Molecular Stereochemistry Iron Polynucleotides Article Nucleobase Dioxygenases Mixed Function Oxygenases Inorganic Chemistry Hydroxylation Fungal Proteins chemistry.chemical_compound Animals Humans Nucleotide chemistry.chemical_classification Nucleotides Nucleosides Chromatin chemistry Biochemistry Polynucleotide Nucleoside DNA |
| Popis: | Fe(II)/alpha-ketoglutarate-dependent hydroxylases uniformly possess a double-stranded beta-helix fold with two conserved histidines and one carboxylate coordinating their mononuclear ferrous ions. Oxidative decomposition of the alpha-keto acid is proposed to generate a ferryl-oxo intermediate capable of hydroxylating unactivated carbon atoms in a myriad of substrates. This Perspective focuses on a subgroup of these enzymes that are involved in pyrimidine salvage, purine decomposition, nucleoside and nucleotide hydroxylation, DNA/RNA repair, and chromatin modification. The varied reaction schemes are presented, and selected structural and kinetic information is summarized. |
| Databáze: | OpenAIRE |
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