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Purification and characterization of human deoxyhypusine synthase from HeLa cells
Author(s) -
H Klier,
R Csonga,
A Steinkasserer,
T Wöhl,
F Lottspeich,
J Eder
Publication year - 1995
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(95)00394-o
Subject(s) - biochemistry , enzyme , saccharomyces cerevisiae , biology , hela , amino acid , lysine , peptide sequence , atp synthase , peptide , yeast , cell , gene
Post‐translational modification of a specific lysine residue in eukaryotic initiation factor 5A is essential for cell viability. The amino acid hypusine, which is the product of this modification, is derived in two subsequent enzyme‐catalyzed reactions. We have purified and characterized the enzyme responsible for the first step in hypusine modification, deoxyhypusine synthase, from HeLa cells. The human enzyme is multimeric with a native apparent molecular weight of 150,000 consisting of subunits of 41,000. The amino acid sequences of its peptide fragments share high sequence identity with a hypothetical protein (YHRO68w) on chromosome VIII of Saccharomyces cerevisiae . This protein appears to be the deoxyhypusine synthase of yeast.