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Chemistry of Hypusine Formation on Eukaryotic Initiation Factor 5A in Biological Systems
Author(s) -
Chen Kuang Yu,
Jao David L.
Publication year - 1999
Publication title -
journal of the chinese chemical society
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.329
H-Index - 45
eISSN - 2192-6549
pISSN - 0009-4536
DOI - 10.1002/jccs.199900100
Subject(s) - chemistry , biochemistry , spermidine , residue (chemistry) , eukaryotic initiation factor , amino acid , microbiology and biotechnology , enzyme , biology , translation (biology) , gene , messenger rna
Hypusine, an unusual amino acid, is derived from the hydrolysis of eukaryotic initiation factor 5 A (eIF‐5A), the only cellular protein known to contain hypusine residue. Hypusine residue is formed through a spermidine‐dependent posttranslational modification of eIF‐5A at a specific lysine residue. Each mature eIF‐5A molecule contains only one hypusine. Hypusine formation on eIF‐5A is essential for cell survival and proliferation. The biochemistry of hypusine formation has been actively investigated in a number of leading laboratories during the past decade. The precise functional role of eIF‐5A remains a mystery. This paper reviews recent progress in the study of the biochemistry of hypusine formation and offers speculation on the possible function of eIF‐5A.