This article is about the gene coding for the enzyme deoxyhypusine synthase. For another enzyme commonly abbreviated DHPS, see Dihydropteroate synthetase. For other uses, see DHPS (disambiguation).
Deoxyhypusine synthase is an enzyme that in humans is encoded by the DHPSgene.[5][6]
The unusual amino acid hypusine is formed posttranslationally and is only found in a single cellular protein, eukaryotic translation initiation factor 5A. In the first step of hypusine biosynthesis, deoxyhypusine synthase catalyzes the NAD-dependent transfer of the butylamine moiety of spermidine to the epsilon-amino group of a specific lysine residue of the EIF5A precursor protein to form the intermediate deoxyhypusine residue. This gene consists of nine exons spanning 6.6 kb. Three transcript variants have been isolated. However, only transcript variant 1 encodes an active protein. The shorter variants may act as modulating factors of DHPS activity.[6]
Klier H; Csonga R; Steinkasserer A; et al. (1995). "Purification and characterization of human deoxyhypusine synthase from HeLa cells". FEBS Lett. 364 (2): 207–10. doi:10.1016/0014-5793(95)00394-O. PMID7750572. {{cite journal}}: Unknown parameter |name-list-format= ignored (|name-list-style= suggested) (help)
Joe YA, Park MH (1994). "Structural features of the eIF-5A precursor required for posttranslational synthesis of deoxyhypusine". J. Biol. Chem. 269 (41): 25916–21. PMID7929297.
Bevec D; Kappel B; Jaksche H; et al. (1996). "Molecular characterization of a cDNA encoding functional human deoxyhypusine synthase and chromosomal mapping of the corresponding gene locus". FEBS Lett. 378 (2): 195–8. doi:10.1016/0014-5793(95)01456-X. PMID8549832. {{cite journal}}: Unknown parameter |name-list-format= ignored (|name-list-style= suggested) (help)
Liao DI, Wolff EC, Park MH, Davies DR (1998). "Crystal structure of the NAD complex of human deoxyhypusine synthase: an enzyme with a ball-and-chain mechanism for blocking the active site". Structure. 6 (1): 23–32. doi:10.1016/S0969-2126(98)00004-5. PMID9493264.