Looking at the incorporation of selenium in proteins like glutathione peroxidases, thioredoxin reductases, formate dehydrogenases, and 20 other proteins it is inquisitive to find out if increased catalysis, stability of intermediates and better leaving groups in selenocysteine over cysteines explain what nature is doing or it has to deal with something else. Can I get views from selenium biologists here?
Hi Abbas. Two interesting things in selenocysteine enzymes are that they can be found in both prokaryotes and eukaryiotes, and that most or all have redox activity, probably to get advantage of a higher reduction potential than cysteine. The form of using the selenocysteine codon is different in bacteria and eukaryotes. So it seems to be "found and maintained" by natural selection for its specific functional properties.
This link may be of help:
http://jnci.oxfordjournals.org/content/96/7/504.full
Greetings.
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