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Please use this identifier to cite or link to this item: http://ntour.ntou.edu.tw:8080/ir/handle/987654321/27088

Title: Molecular cloning and functional expression of bovine deoxyhypusine hydroxylase cDNA and homologs
Authors: Jenq-Kuen Huang;Yalun Cui;Chieh-Hua Chen;Denae Clampitt;Chi-Tsai Lin;Lisa Wen
Contributors: NTOU:Institute of Bioscience and Biotechnology
國立臺灣海洋大學:生物科技研究所
Keywords: Deoxyhypusine hydroxylase;eIF5A;Hypusine;HEAT-repeat-containing;cDNA cloning
Date: 2007-07-01
Issue Date: 2011-10-21T02:22:37Z
Publisher: Protein Expression and Purification
Abstract: Abstract:Deoxyhypusine hydroxylase is the second of the two enzymes that catalyzes the maturation of eukaryotic initiation factor 5A (eIF5A). The mature eIF5A is the only known protein in eukaryotic cells that contains the unusual amino acid hypusine (Nε-(4-amino-2(R)-hydroxybutyl)lysine). Synthesis of hypusine is essential for the function of eIF5A in eukaryotic cell proliferation and survival. Here, we describe the cloning and characterization of bovine deoxyhypusine hydroxylase cDNA and its homologs. The deduced bovine deoxyhypusine hydroxylase protein is 87% identical to human enzyme and 45% identical to yeast enzyme. The overexpressed enzyme showed activity in catalyzing the hydroxylation of the deoxyhypusine residue in the eIF5A intermediate. An amino acid substitution from Glu 57 to Gly located at one of the four conserved His–Glu (HE) pairs, the potential metal coordination sites, resulted in severe reduction of deoxyhypusine hydroxylase activity. A deletion at the HEAT-repeats 1–3 resulted in complete losses of deoxyhypusine hydroxylase activity.
Relation: 54(1), pp.126–133
URI: http://ntour.ntou.edu.tw/handle/987654321/27088
Appears in Collections:[Department of Bioscience and Biotechnology ] Periodical Articles

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