Journal
AMINO ACIDS
Volume 33, Issue 2, Pages 341-350Publisher
SPRINGER WIEN
DOI: 10.1007/s00726-007-0525-0
Keywords
hypusine; eIF5A; posttranslational modification; deoxyhypusine synthase; deoxyhypusine hydroxylase; polyamine
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Funding
- Intramural NIH HHS [Z01 DE000608-14, Z99 DE999999] Funding Source: Medline
- National Research Foundation of Korea [2006-005-J04203] Funding Source: Korea Institute of Science & Technology Information (KISTI), National Science & Technology Information Service (NTIS)
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A naturally occurring unusual amino acid, hypusine [N-epsilon-(4amino-2-hydroxybutyl)-lysine] is a component of a single cellular protein, eukaryotic translation initiation factor 5A (eIF5A). It is a modified lysine with structural contribution from the polyamine spermidine. Hypusine is formed in a novel posttranslational modification that involves two enzymes, deoxyhypusine synthase (DHS) and deoxyhypusine hydroxylase (DOHH). eIF5A and deoxyhypusine/hypusine modification are essential for growth of eukaryotic cells. The hypusine synthetic pathway has evolved in eukar-yotes and eIF5A, DHS and DOHH are highly conserved, suggesting maintenance of a fundamental cellular function of eIF5A through evolution. The unique feature of the hypusine modification is the strict specificity of the enzymes toward its substrate protein, eIF5A. Moreover, DHS exhibits a narrow specificity toward spermidine. In view of the extraordinary specificity and the requirement for hypusine-containing eIF5A for mammalian cell proliferation, eIF5A and the hypusine biosynthetic enzymes present new potential targets for intervention in aberrant cell proliferation.
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