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.[1][2]
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.[2]
References
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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.
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.
Andersson B, Wentland MA, Ricafrente JY, et al. (1996). "A "double adaptor" method for improved shotgun library construction". Anal. Biochem. 236 (1): 107–13. doi:10.1006/abio.1996.0138. PMID8619474.
Jones T, Sheer D, Kapetanopoulos A, et al. (1996). "The gene coding for human deoxyhypusine synthase (DHPS) maps to chromosome 19p13.11-p13.12". Genomics. 35 (3): 635–7. doi:10.1006/geno.1996.0416. PMID8812510.
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.
Mantuano E, Trettel F, Olsen AS, et al. (1998). "Localization and genomic structure of human deoxyhypusine synthase gene on chromosome 19p13.2-distal 19p13.1". Gene. 215 (1): 153–7. doi:10.1016/S0378-1119(98)00254-6. PMID9666110.
Ober D, Harms R, Witte L, Hartmann T (2003). "Molecular evolution by change of function. Alkaloid-specific homospermidine synthase retained all properties of deoxyhypusine synthase except binding the eIF5A precursor protein". J. Biol. Chem. 278 (15): 12805–12. doi:10.1074/jbc.M207112200. PMID12562768.
Park JH, Wolff EC, Folk JE, Park MH (2003). "Reversal of the deoxyhypusine synthesis reaction. Generation of spermidine or homospermidine from deoxyhypusine by deoxyhypusine synthase". J. Biol. Chem. 278 (35): 32683–91. doi:10.1074/jbc.M304247200. PMID12788913.
Kang KR, Chung SI (2004). "Protein kinase CK2 phosphorylates and interacts with deoxyhypusine synthase in HeLa cells". Exp. Mol. Med. 35 (6): 556–64. doi:10.1038/emm.2003.73. PMID14749535.
Umland TC, Wolff EC, Park MH, Davies DR (2004). "A new crystal structure of deoxyhypusine synthase reveals the configuration of the active enzyme and of an enzyme.NAD.inhibitor ternary complex". J. Biol. Chem. 279 (27): 28697–705. doi:10.1074/jbc.M404095200. PMID15100216.
Rual JF, Venkatesan K, Hao T, et al. (2005). "Towards a proteome-scale map of the human protein-protein interaction network". Nature. 437 (7062): 1173–8. doi:10.1038/nature04209. PMID16189514.