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J Biol Chem, Vol. 274, Issue 45, 32040-32047, November 5, 1999
From the Institut für Pharmazeutische Biologie der
Technischen Universität Braunschweig, Mendelssohnstraße 1, D-38106 Braunschweig, Germany
Deoxyhypusine synthase catalyzes the formation of
a deoxyhypusine residue in the translation eukaryotic initiation factor 5A (eIF5A) precursor protein by transferring an aminobutyl moiety from
spermidine onto a conserved lysine residue within the eIF5A polypeptide
chain. This reaction commences the activation of the initiation factor
in fungi and vertebrates. A mechanistically identical reaction is known
in the biosynthetic pathway leading to pyrrolizidine alkaloids in
plants. Deoxyhypusine synthase from tobacco was cloned and expressed in
active form in Escherichia coli. It catalyzes the formation
of a deoxyhypusine residue in the tobacco eIF5A substrate as shown by
gas chromatography coupled with a mass spectrometer. The enzyme also
accepts free putrescine as the aminobutyl acceptor, instead of lysine
bound in the eIF5A polypeptide chain, yielding homospermidine.
Conversely, it accepts homospermidine instead of spermidine as the
aminobutyl donor, whereby the reactions with putrescine and
homospermidine proceed at the same rate as those involving the
authentic substrates. The conversion of deoxyhypusine
synthase-catalyzed eIF5A deoxyhypusinylation pinpoints a function for
spermidine in plant metabolism. Furthermore, and quite unexpectedly,
the substrate spectrum of deoxyhypusine synthase hints at a biochemical
basis behind the sparse and skew occurrence of both homospermidine and
its pyrrolizidine derivatives across distantly related plant taxa.
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