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Hypusine is an unusual amino acid found in all eukaryotes and in some archaebacteria, but not in eubacteria. The only known protein containing hypusine is eukaryotic translation initiation factor 5A (eIF-5A) and a similar protein found in archaebacteria. In human, two isoforms of eIF-5A have been described: eIF-5A-1 and eIF-5A-2. They are coded by two different genes. This protein is involved in protein biosynthesis and promotes the formation of the first peptide bond. The region surrounding the hypusine residue is highly conserved among the eukaryotes and is essential to the function of eIF-5A. Thus, hypusine and eIF-5A appear to be vital for the viability and proliferation of eukaryotic cells.
Additional recommended knowledge
Hypusine is formed in eIF-5A by post-translational modification of one of the lysyl residues. There are two reactions and two enzymes involved:
An excess of hypusine was found in the urine of children and patients with familial hyperlysinemia.
Hypusine was first isolated from bovine brain by Japanese scientists Shiba et all. in 1971. The name hypusine indicates that the molecule comprises moieties of hydroxyputrescine and lysine.
|This article is licensed under the GNU Free Documentation License. It uses material from the Wikipedia article "Hypusine". A list of authors is available in Wikipedia.|