Bioinformatic study of genetic variability of superoxide dismutase isoforms

conference paper

English

Superoxide dismutases (SODs) represent ubiquitous enzymes that catalytically convert superoxide anion radical, which is created in many biological processes, to oxygen (O2) and hydrogen peroxide (H2O2)1. Many targets of superoxide anion radical have been identified; it is relatively unreactive with some amino acids excepting sulfur-containing amino acids, but it is strongly reactive with some transition metals and complexes, especially copper, iron, and manganese2. Several forms of superoxide dismutase have been described. Classification of SODs according to presence of cofactors - metal ions – is generally accepted: Cu/ZnSODs (in humans referred as SOD1 and SOD3; they bind copper and zinc ions), Fe and Mn types (Mn/FeSODs, in humans referred as SOD2; they bind either iron or manganese), and Ni (NiSODs; they bind nickel). Whereas Cu/Zn SODs are commonly present in cytosol of eukaryotic cells, Fe and Mn SODs are in some protists, relatively primitive eukaryotic cells, and prokaryotes; mitochondrial and plastid SODs are usually Mn and Fe forms, respectively. NiSODs that were originally identified in Streptomyces are typically prokaryotic3, 4. Despite the significant differences between structures of individual SODs, all crucially provide electrostatic guidance for the superoxide substrate and alter the metal ion redox potential to a range suitable for superoxide disproportionation5. In our work, we compare sequences of vertebrate SODs to identify similarities and phylogenetic relationships.

superoxide dismutase, isoform, multiple sequence alignment, sequence logo,

ŠKUTKOVÁ, H.; BABULA, P.; PROVAZNÍK, I.

2014

7. 4. 2014

Mikulov

978-80-86238-61-6

2. mezinárodní chemicko-technologická konference, SBORNÍK ABSTRAKT A PLNÝCH TEXTŮ

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