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1-ethylspermidine + putrescine
homospermidine + ?
-
-
-
?
1-ethylspermidine + [eIF5A-precursor]-lysine
[eIF5A-precursor]-deoxyhypusine + ?
-
-
-
?
1-methylspermidine + putrescine
homospermidine + ?
-
-
-
?
1-methylspermidine + [eIF5A-precursor]-lysine
[eIF5A-precursor]-deoxyhypusine + ?
-
-
-
?
8-ethylspermidine + putrescine
ethylhomospermidine + ?
-
-
-
?
8-ethylspermidine + [eIF5A-precursor]-lysine
[eIF5A-precursor]-ethyldeoxyhypusine + ?
-
-
-
?
8-methylspermidine + putrescine
methylhomospermidine + ?
-
-
-
?
8-methylspermidine + [eIF5A-precursor]-lysine
[eIF5A-precursor]-methyldeoxyhypusine + ?
-
-
-
?
aminopropylcadaverine + [eIF5A-precursor]-lysine
[eIF5A-precursor]-homodeoxyhypusine + ?
-
-
-
?
caldine + putrescine
spermidine + ?
-
-
-
?
homospermidine + putrescine
homospermidine + ?
homospermidine + [eIF5A-precursor]-lysine
[eIF5A-precursor]-deoxyhypusine + ?
-
-
-
?
homospermine + [eIF5A-precursor]-lysine
?
-
-
-
-
?
N-(3-aminopropyl)-1,4-diamino-cis-but-2-ene + putrescine
(1Z)-N4-(4-aminobutyl)but-1-ene-1,4-diamine + 1,3-diaminopropane
-
-
-
?
N-(3-aminopropyl)-1,4-diamino-cis-but-2-ene + [eIF5A-precursor]-lysine
?
-
-
-
?
N-(3-aminopropyl)-1,4-diamino-trans-but-2-ene + putrescine
(1E)-N4-(4-aminobutyl)but-1-ene-1,4-diamine + 1,3-diaminopropane
-
-
-
?
N-(3-aminopropyl)-1,4-diamino-trans-but-2-ene + [eIF5A-precursor]-lysine
?
-
-
-
?
spermidine
1,3-diaminopropane + DELTA1-pyrroline
spermidine + NAD+
dehydrospermidine + NADH
spermidine + putrescine
homospermidine + ?
[eIF5A-1-precursor]-lysine + spermidine
[eIF5A-1-precursor]-deoxyhypusine + propane-1,3-diamine
[eIF5A-2-precursor]-lysine + spermidine
[eIF5A-2-precursor]-deoxyhypusine + propane-1,3-diamine
-
-
-
-
?
[eIF5A-precursor] + spermidine
[eIF5A-precursor]-deoxyhypusine + propane-1,3-diamine
[eIF5A-precursor]-L-lysine + spermidine
[eIF5A-precursor]-deoxyhypusine + propane-1,3-diamine
[eIF5A-precursor]-lysine + (R)-3-methylspermidine
?
[eIF5A-precursor]-lysine + 2-methylspermidine
?
[eIF5A-precursor]-lysine + 3-methylspermidine
?
-
-
-
-
?
[eIF5A-precursor]-lysine + 4-methylspermidine
?
-
-
-
-
?
[eIF5A-precursor]-lysine + homospermidine
[eIF5A-precursor]-deoxyhypusine + putrescine
-
-
?
[eIF5A-precursor]-lysine + spermidine
[eIF5A-precursor]-deoxyhypusine + propane-1,3-diamine
[eIF5A-precursor]-lysine + spermine
?
-
-
-
?
[eIF5A-precursor]-lysine42 + spermidine
[eIF5A-precursor]-lysine42-deoxyhypusine + propane-1,3-diamine
[TveIF-5A-precursor]-lysine + spermidine
[TveIF-5A-precursor]-deoxyhypusine + propane-1,3-diamine
additional information
?
-
homospermidine + putrescine
homospermidine + ?
-
-
-
?
homospermidine + putrescine
homospermidine + ?
-
-
-
?
spermidine
1,3-diaminopropane + DELTA1-pyrroline
-
-
?
spermidine
1,3-diaminopropane + DELTA1-pyrroline
-
reaction in absence of eIF5A-precursor
-
?
spermidine
1,3-diaminopropane + DELTA1-pyrroline
-
reaction in absence of eIF5A-precursor
-
?
spermidine
1,3-diaminopropane + DELTA1-pyrroline
-
reaction in absence of eIF5A-precursor
-
?
spermidine
1,3-diaminopropane + DELTA1-pyrroline
-
reaction in absence of eIF5A-precursor
-
?
spermidine + NAD+
dehydrospermidine + NADH
-
-
-
?
spermidine + NAD+
dehydrospermidine + NADH
-
-
-
?
spermidine + putrescine
homospermidine + ?
-
-
-
?
spermidine + putrescine
homospermidine + ?
-
-
?
spermidine + putrescine
homospermidine + ?
-
-
?
spermidine + putrescine
homospermidine + ?
-
-
?
[eIF5A-1-precursor]-lysine + spermidine
[eIF5A-1-precursor]-deoxyhypusine + propane-1,3-diamine
-
-
-
-
?
[eIF5A-1-precursor]-lysine + spermidine
[eIF5A-1-precursor]-deoxyhypusine + propane-1,3-diamine
-
-
-
-
?
[eIF5A-precursor] + spermidine
[eIF5A-precursor]-deoxyhypusine + propane-1,3-diamine
-
-
-
?
[eIF5A-precursor] + spermidine
[eIF5A-precursor]-deoxyhypusine + propane-1,3-diamine
-
-
-
?
[eIF5A-precursor] + spermidine
[eIF5A-precursor]-deoxyhypusine + propane-1,3-diamine
-
-
-
?
[eIF5A-precursor] + spermidine
[eIF5A-precursor]-deoxyhypusine + propane-1,3-diamine
-
-
-
?
[eIF5A-precursor]-L-lysine + spermidine
[eIF5A-precursor]-deoxyhypusine + propane-1,3-diamine
-
-
-
?
[eIF5A-precursor]-L-lysine + spermidine
[eIF5A-precursor]-deoxyhypusine + propane-1,3-diamine
-
-
-
?
[eIF5A-precursor]-L-lysine + spermidine
[eIF5A-precursor]-deoxyhypusine + propane-1,3-diamine
-
-
-
?
[eIF5A-precursor]-L-lysine + spermidine
[eIF5A-precursor]-deoxyhypusine + propane-1,3-diamine
-
-
-
-
?
[eIF5A-precursor]-L-lysine + spermidine
[eIF5A-precursor]-deoxyhypusine + propane-1,3-diamine
-
-
-
?
[eIF5A-precursor]-lysine + (R)-3-methylspermidine
?
enzyme DHS prefers the (R)- over the (S)-enantiomer as a substrate
-
-
?
[eIF5A-precursor]-lysine + (R)-3-methylspermidine
?
no activity with the (S)-enantiomer
-
-
?
[eIF5A-precursor]-lysine + 2-methylspermidine
?
-
-
-
-
?
[eIF5A-precursor]-lysine + 2-methylspermidine
?
-
the S-enantiomer of 2-MeSpd, which supports long-term growth, is a good substrate for DHS in vitro, whereas the R isomer is not
-
-
?
[eIF5A-precursor]-lysine + spermidine
[eIF5A-precursor]-deoxyhypusine + propane-1,3-diamine
-
-
-
-
?
[eIF5A-precursor]-lysine + spermidine
[eIF5A-precursor]-deoxyhypusine + propane-1,3-diamine
-
-
-
?
[eIF5A-precursor]-lysine + spermidine
[eIF5A-precursor]-deoxyhypusine + propane-1,3-diamine
transfer of a 4-aminobutyl moiety group
-
-
?
[eIF5A-precursor]-lysine + spermidine
[eIF5A-precursor]-deoxyhypusine + propane-1,3-diamine
-
-
-
?
[eIF5A-precursor]-lysine + spermidine
[eIF5A-precursor]-deoxyhypusine + propane-1,3-diamine
transfer of a 4-aminobutyl moiety group
-
-
?
[eIF5A-precursor]-lysine + spermidine
[eIF5A-precursor]-deoxyhypusine + propane-1,3-diamine
deoxyhypusine synthase is the first of the two enzymes that catalyze the maturation of eukaryotic initiation factor 5A. Synthesis of hypusine is essential for the function of eIF5A in eukaryotic cell proliferation and survival
-
-
?
[eIF5A-precursor]-lysine + spermidine
[eIF5A-precursor]-deoxyhypusine + propane-1,3-diamine
bovine enzyme is approximately 26times as effective as the human enzyme in catalyzing the reaction
-
-
?
[eIF5A-precursor]-lysine + spermidine
[eIF5A-precursor]-deoxyhypusine + propane-1,3-diamine
-
-
-
-
?
[eIF5A-precursor]-lysine + spermidine
[eIF5A-precursor]-deoxyhypusine + propane-1,3-diamine
-
-
-
-
?
[eIF5A-precursor]-lysine + spermidine
[eIF5A-precursor]-deoxyhypusine + propane-1,3-diamine
-
-
-
-
?
[eIF5A-precursor]-lysine + spermidine
[eIF5A-precursor]-deoxyhypusine + propane-1,3-diamine
-
the enzyme catalyzes the first reaction in a two-step conversion of inactive eIF-5A to its active form
-
-
?
[eIF5A-precursor]-lysine + spermidine
[eIF5A-precursor]-deoxyhypusine + propane-1,3-diamine
-
-
-
?
[eIF5A-precursor]-lysine + spermidine
[eIF5A-precursor]-deoxyhypusine + propane-1,3-diamine
-
-
-
-
?
[eIF5A-precursor]-lysine + spermidine
[eIF5A-precursor]-deoxyhypusine + propane-1,3-diamine
-
-
-
-
?
[eIF5A-precursor]-lysine + spermidine
[eIF5A-precursor]-deoxyhypusine + propane-1,3-diamine
hypusination of Lys56
-
-
?
[eIF5A-precursor]-lysine + spermidine
[eIF5A-precursor]-deoxyhypusine + propane-1,3-diamine
-
-
-
-
?
[eIF5A-precursor]-lysine + spermidine
[eIF5A-precursor]-deoxyhypusine + propane-1,3-diamine
-
-
-
-
?
[eIF5A-precursor]-lysine + spermidine
[eIF5A-precursor]-deoxyhypusine + propane-1,3-diamine
-
the enzyme catalyzes the first reaction in a two-step conversion of inactive eIF-5A to its active form
-
-
?
[eIF5A-precursor]-lysine + spermidine
[eIF5A-precursor]-deoxyhypusine + propane-1,3-diamine
-
-
-
-
?
[eIF5A-precursor]-lysine + spermidine
[eIF5A-precursor]-deoxyhypusine + propane-1,3-diamine
-
-
-
-
ir
[eIF5A-precursor]-lysine + spermidine
[eIF5A-precursor]-deoxyhypusine + propane-1,3-diamine
-
-
-
?
[eIF5A-precursor]-lysine + spermidine
[eIF5A-precursor]-deoxyhypusine + propane-1,3-diamine
-
-
-
-
?
[eIF5A-precursor]-lysine + spermidine
[eIF5A-precursor]-deoxyhypusine + propane-1,3-diamine
-
-
-
?
[eIF5A-precursor]-lysine + spermidine
[eIF5A-precursor]-deoxyhypusine + propane-1,3-diamine
-
-
i.e. [eIF5A-precursor]-N6-(4-aminobutyl)lysine
?
[eIF5A-precursor]-lysine + spermidine
[eIF5A-precursor]-deoxyhypusine + propane-1,3-diamine
-
-
i.e. [eIF5A-precursor]-N6-(4-aminobutyl)lysine
?
[eIF5A-precursor]-lysine + spermidine
[eIF5A-precursor]-deoxyhypusine + propane-1,3-diamine
-
-
i.e. [eIF5A-precursor]-N6-(4-aminobutyl)lysine
?
[eIF5A-precursor]-lysine + spermidine
[eIF5A-precursor]-deoxyhypusine + propane-1,3-diamine
-
-
i.e. [eIF5A-precursor]-N6-(4-aminobutyl)lysine
?
[eIF5A-precursor]-lysine + spermidine
[eIF5A-precursor]-deoxyhypusine + propane-1,3-diamine
-
-
i.e. [eIF5A-precursor]-N6-(4-aminobutyl)lysine
?
[eIF5A-precursor]-lysine + spermidine
[eIF5A-precursor]-deoxyhypusine + propane-1,3-diamine
-
-
i.e. [eIF5A-precursor]-N6-(4-aminobutyl)lysine
?
[eIF5A-precursor]-lysine + spermidine
[eIF5A-precursor]-deoxyhypusine + propane-1,3-diamine
-
-
i.e. [eIF5A-precursor]-N6-(4-aminobutyl)lysine
?
[eIF5A-precursor]-lysine + spermidine
[eIF5A-precursor]-deoxyhypusine + propane-1,3-diamine
-
-
i.e. [eIF5A-precursor]-N6-(4-aminobutyl)lysine
?
[eIF5A-precursor]-lysine + spermidine
[eIF5A-precursor]-deoxyhypusine + propane-1,3-diamine
-
-
i.e. [eIF5A-precursor]-N6-(4-aminobutyl)lysine
?
[eIF5A-precursor]-lysine + spermidine
[eIF5A-precursor]-deoxyhypusine + propane-1,3-diamine
-
-
i.e. [eIF5A-precursor]-N6-(4-aminobutyl)lysine
?
[eIF5A-precursor]-lysine + spermidine
[eIF5A-precursor]-deoxyhypusine + propane-1,3-diamine
-
i.e. [eIF5A-precursor]-N6-(4-aminobutyl)lysine
?
[eIF5A-precursor]-lysine + spermidine
[eIF5A-precursor]-deoxyhypusine + propane-1,3-diamine
-
reversal of reaction in presence of NAD+
i.e. [eIF5A-precursor]-N6-(4-aminobutyl)lysine
r
[eIF5A-precursor]-lysine + spermidine
[eIF5A-precursor]-deoxyhypusine + propane-1,3-diamine
-
first step in the biosynthesis of hypusine
-
-
?
[eIF5A-precursor]-lysine + spermidine
[eIF5A-precursor]-deoxyhypusine + propane-1,3-diamine
first step in the biosynthesis of hypusine
-
-
?
[eIF5A-precursor]-lysine + spermidine
[eIF5A-precursor]-deoxyhypusine + propane-1,3-diamine
-
posttranslational activation of eIF-5A which has a specialized role in proliferation and in serum starvation-induced apoptosis in endothelial cells
-
-
?
[eIF5A-precursor]-lysine + spermidine
[eIF5A-precursor]-deoxyhypusine + propane-1,3-diamine
overall reaction
-
-
?
[eIF5A-precursor]-lysine + spermidine
[eIF5A-precursor]-deoxyhypusine + propane-1,3-diamine
-
bovine enzyme is approximately 26times as effective as the human enzyme in catalyzing the reaction
-
-
?
[eIF5A-precursor]-lysine + spermidine
[eIF5A-precursor]-deoxyhypusine + propane-1,3-diamine
-
DHS catalyzes a NAD-dependent cleavage between N4 and C5 of spermidine and the transfer of the butylamine moiety to the ?-amino group of a specific lysine residue of the eIF5A precursor, eIF5A(Lys), to form the deoxyhypusine residue. The enzyme is modification is strictly specific for one single lysine residue of the cellular protein eukaryotic initiation factor 5A (eIF5A) and does not work on short peptides
1,3-diaminopropane is released as a byproduct from spermidine cleavage
-
?
[eIF5A-precursor]-lysine + spermidine
[eIF5A-precursor]-deoxyhypusine + propane-1,3-diamine
formation of [N(epsilon)-(4-amino-2-hydroxybutyl)lysine]
-
-
?
[eIF5A-precursor]-lysine + spermidine
[eIF5A-precursor]-deoxyhypusine + propane-1,3-diamine
-
-
-
-
?
[eIF5A-precursor]-lysine + spermidine
[eIF5A-precursor]-deoxyhypusine + propane-1,3-diamine
-
-
-
-
?
[eIF5A-precursor]-lysine + spermidine
[eIF5A-precursor]-deoxyhypusine + propane-1,3-diamine
-
-
-
-
?
[eIF5A-precursor]-lysine + spermidine
[eIF5A-precursor]-deoxyhypusine + propane-1,3-diamine
-
-
-
-
?
[eIF5A-precursor]-lysine + spermidine
[eIF5A-precursor]-deoxyhypusine + propane-1,3-diamine
-
-
-
?
[eIF5A-precursor]-lysine + spermidine
[eIF5A-precursor]-deoxyhypusine + propane-1,3-diamine
-
-
-
?
[eIF5A-precursor]-lysine + spermidine
[eIF5A-precursor]-deoxyhypusine + propane-1,3-diamine
-
-
-
-
?
[eIF5A-precursor]-lysine + spermidine
[eIF5A-precursor]-deoxyhypusine + propane-1,3-diamine
-
-
-
-
?
[eIF5A-precursor]-lysine + spermidine
[eIF5A-precursor]-deoxyhypusine + propane-1,3-diamine
-
-
-
?
[eIF5A-precursor]-lysine + spermidine
[eIF5A-precursor]-deoxyhypusine + propane-1,3-diamine
-
i.e. [eIF5A-precursor]-N6-(4-aminobutyl)lysine
?
[eIF5A-precursor]-lysine + spermidine
[eIF5A-precursor]-deoxyhypusine + propane-1,3-diamine
-
-
-
?
[eIF5A-precursor]-lysine + spermidine
[eIF5A-precursor]-deoxyhypusine + propane-1,3-diamine
-
i.e. [eIF5A-precursor]-N6-(4-aminobutyl)lysine
?
[eIF5A-precursor]-lysine + spermidine
[eIF5A-precursor]-deoxyhypusine + propane-1,3-diamine
overall reaction
-
-
?
[eIF5A-precursor]-lysine + spermidine
[eIF5A-precursor]-deoxyhypusine + propane-1,3-diamine
the enzyme is involved in synthesis of synthesis of homospermidine
-
-
?
[eIF5A-precursor]-lysine + spermidine
[eIF5A-precursor]-deoxyhypusine + propane-1,3-diamine
-
-
-
-
?
[eIF5A-precursor]-lysine + spermidine
[eIF5A-precursor]-deoxyhypusine + propane-1,3-diamine
-
-
i.e. [eIF5A-precursor]-N6-(4-aminobutyl)lysine
?
[eIF5A-precursor]-lysine + spermidine
[eIF5A-precursor]-deoxyhypusine + propane-1,3-diamine
-
-
i.e. [eIF5A-precursor]-N6-(4-aminobutyl)lysine
?
[eIF5A-precursor]-lysine + spermidine
[eIF5A-precursor]-deoxyhypusine + propane-1,3-diamine
-
-
i.e. [eIF5A-precursor]-N6-(4-aminobutyl)lysine
?
[eIF5A-precursor]-lysine + spermidine
[eIF5A-precursor]-deoxyhypusine + propane-1,3-diamine
-
-
-
-
?
[eIF5A-precursor]-lysine + spermidine
[eIF5A-precursor]-deoxyhypusine + propane-1,3-diamine
-
-
i.e. [eIF5A-precursor]-N6-(4-aminobutyl)lysine
?
[eIF5A-precursor]-lysine + spermidine
[eIF5A-precursor]-deoxyhypusine + propane-1,3-diamine
-
-
i.e. [eIF5A-precursor]-N6-(4-aminobutyl)lysine
?
[eIF5A-precursor]-lysine + spermidine
[eIF5A-precursor]-deoxyhypusine + propane-1,3-diamine
-
-
i.e. [eIF5A-precursor]-N6-(4-aminobutyl)lysine
?
[eIF5A-precursor]-lysine + spermidine
[eIF5A-precursor]-deoxyhypusine + propane-1,3-diamine
-
-
i.e. [eIF5A-precursor]-N6-(4-aminobutyl)lysine
?
[eIF5A-precursor]-lysine + spermidine
[eIF5A-precursor]-deoxyhypusine + propane-1,3-diamine
-
-
i.e. [eIF5A-precursor]-N6-(4-aminobutyl)lysine
?
[eIF5A-precursor]-lysine + spermidine
[eIF5A-precursor]-deoxyhypusine + propane-1,3-diamine
-
-
i.e. [eIF5A-precursor]-N6-(4-aminobutyl)lysine
?
[eIF5A-precursor]-lysine + spermidine
[eIF5A-precursor]-deoxyhypusine + propane-1,3-diamine
-
the enzyme catalyzes the first reaction in a two-step conversion of inactive eIF-5A to its active form
-
-
?
[eIF5A-precursor]-lysine + spermidine
[eIF5A-precursor]-deoxyhypusine + propane-1,3-diamine
-
-
-
-
?
[eIF5A-precursor]-lysine + spermidine
[eIF5A-precursor]-deoxyhypusine + propane-1,3-diamine
-
-
-
?
[eIF5A-precursor]-lysine + spermidine
[eIF5A-precursor]-deoxyhypusine + propane-1,3-diamine
-
i.e. [eIF5A-precursor]-N6-(4-aminobutyl)lysine
?
[eIF5A-precursor]-lysine + spermidine
[eIF5A-precursor]-deoxyhypusine + propane-1,3-diamine
-
i.e. [eIF5A-precursor]-N6-(4-aminobutyl)lysine
?
[eIF5A-precursor]-lysine + spermidine
[eIF5A-precursor]-deoxyhypusine + propane-1,3-diamine
posttranslational activation of the initiation factor 5A
-
-
?
[eIF5A-precursor]-lysine + spermidine
[eIF5A-precursor]-deoxyhypusine + propane-1,3-diamine
-
i.e. [eIF5A-precursor]-N6-(4-aminobutyl)lysine
?
[eIF5A-precursor]-lysine + spermidine
[eIF5A-precursor]-deoxyhypusine + propane-1,3-diamine
-
-
-
?
[eIF5A-precursor]-lysine + spermidine
[eIF5A-precursor]-deoxyhypusine + propane-1,3-diamine
-
-
-
?
[eIF5A-precursor]-lysine + spermidine
[eIF5A-precursor]-deoxyhypusine + propane-1,3-diamine
-
-
-
-
?
[eIF5A-precursor]-lysine + spermidine
[eIF5A-precursor]-deoxyhypusine + propane-1,3-diamine
-
-
-
?
[eIF5A-precursor]-lysine + spermidine
[eIF5A-precursor]-deoxyhypusine + propane-1,3-diamine
Trypanosoma brucei brucei 927 / 4 GUTat10.1 / TREU927
-
-
-
?
[eIF5A-precursor]-lysine + spermidine
[eIF5A-precursor]-deoxyhypusine + propane-1,3-diamine
-
-
-
-
?
[eIF5A-precursor]-lysine42 + spermidine
[eIF5A-precursor]-lysine42-deoxyhypusine + propane-1,3-diamine
-
substrate [eIF5A-precursor]-lysine42 of Haloferax volcanii
overall reaction
-
?
[eIF5A-precursor]-lysine42 + spermidine
[eIF5A-precursor]-lysine42-deoxyhypusine + propane-1,3-diamine
-
substrate [eIF5A-precursor]-lysine42 of Haloferax volcanii
overall reaction
-
?
[TveIF-5A-precursor]-lysine + spermidine
[TveIF-5A-precursor]-deoxyhypusine + propane-1,3-diamine
-
-
-
?
[TveIF-5A-precursor]-lysine + spermidine
[TveIF-5A-precursor]-deoxyhypusine + propane-1,3-diamine
transfer of 4-amino-2-hydroxybutyl side chain, MS/MS analysis for determination of the hypusine residue
-
-
?
[TveIF-5A-precursor]-lysine + spermidine
[TveIF-5A-precursor]-deoxyhypusine + propane-1,3-diamine
-
-
-
?
[TveIF-5A-precursor]-lysine + spermidine
[TveIF-5A-precursor]-deoxyhypusine + propane-1,3-diamine
transfer of 4-amino-2-hydroxybutyl side chain, MS/MS analysis for determination of the hypusine residue
-
-
?
additional information
?
-
-
deoxyhypusine synthase-suppressed Brassica napus plants have larger leaves as well as enhanced seed yield, this appears to reflect increased tolerance to chronic sublethal stress
-
-
?
additional information
?
-
-
recombinant deoxyhypusine synthase from Haloferax volcanii does not show any activity under varying aIF5A concentration and substrate concentration unsing spermidine, agmatine, cadaverine, and putrescine. In vivo, the eIF5A-precursor in Haloferax volcanii is shown to be deoxyhypusinylated
-
-
?
additional information
?
-
-
recombinant deoxyhypusine synthase from Haloferax volcanii does not show any activity under varying aIF5A concentration and substrate concentration unsing spermidine, agmatine, cadaverine, and putrescine. In vivo, the eIF5A-precursor in Haloferax volcanii is shown to be deoxyhypusinylated
-
-
?
additional information
?
-
-
as racemic mixtures, only 2-MeSpd and 3-MeSpd support long-term growth (9-18 days) of spermidine-depleted DU-145 cells, whereas gamma-MeSpd and omega-MeSpd do not
-
-
?
additional information
?
-
-
development of a radioactive assay method for detection of spermidine incorporation into eIF5A, overview
-
-
?
additional information
?
-
(R)-3-methylspermidine competes with spermidine for cellular uptake less efficiently than the (S)-3-methylspermidine
-
-
?
additional information
?
-
(R)-3-methylspermidine competes with spermidine for cellular uptake less efficiently than the (S)-3-methylspermidine
-
-
?
additional information
?
-
no substrates: putrecine, lysine
-
-
-
additional information
?
-
-
no substrates: putrecine, lysine
-
-
-
additional information
?
-
-
the DHSL20 protein lacks a critical lysine residue, and the recombinant protein shows no DHS activity in vitro, while DHS34 contains the critical lysine residue, and the recombinant DHS34 effectively catalyzes deoxyhypusine synthesis
-
-
?
additional information
?
-
the DHSL20 protein lacks a critical lysine residue, and the recombinant protein shows no DHS activity in vitro, while DHS34 contains the critical lysine residue, and the recombinant DHS34 effectively catalyzes deoxyhypusine synthesis
-
-
?
additional information
?
-
the DHSL20 protein lacks a critical lysine residue, and the recombinant protein shows no DHS activity in vitro, while DHS34 contains the critical lysine residue, and the recombinant DHS34 effectively catalyzes deoxyhypusine synthesis
-
-
?
additional information
?
-
no synthesis of [eIF5A-precursor]-hypusine
-
-
?
additional information
?
-
-
no synthesis of [eIF5A-precursor]-hypusine
-
-
?
additional information
?
-
no synthesis of [eIF5A-precursor]-hypusine
-
-
?
additional information
?
-
-
mutants of substrate [eIF5A-1-precursor]-lysine with changes in residue K50, and mutants G52A and K55A are no substrates. The hypusine site loop has critical importance in eIF5A function and hypusine modification
-
-
?
additional information
?
-
the rTvDHS enzyme is bifunctional and is also involved in the hydroxylation of deoxyhypusine-containing rTveIF-5A, cf. EC 1.14.99.29
-
-
?
additional information
?
-
-
the rTvDHS enzyme is bifunctional and is also involved in the hydroxylation of deoxyhypusine-containing rTveIF-5A, cf. EC 1.14.99.29
-
-
?
additional information
?
-
formation of a TvDHS-TveIF-5A complex
-
-
?
additional information
?
-
-
formation of a TvDHS-TveIF-5A complex
-
-
?
additional information
?
-
the rTvDHS enzyme is bifunctional and is also involved in the hydroxylation of deoxyhypusine-containing rTveIF-5A, cf. EC 1.14.99.29
-
-
?
additional information
?
-
formation of a TvDHS-TveIF-5A complex
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
[eIF5A-precursor]-lysine + 2-methylspermidine
?
-
-
-
-
?
[eIF5A-precursor]-lysine + 3-methylspermidine
?
-
-
-
-
?
[eIF5A-precursor]-lysine + spermidine
[eIF5A-precursor]-deoxyhypusine + propane-1,3-diamine
[TveIF-5A-precursor]-lysine + spermidine
[TveIF-5A-precursor]-deoxyhypusine + propane-1,3-diamine
additional information
?
-
[eIF5A-precursor]-lysine + spermidine
[eIF5A-precursor]-deoxyhypusine + propane-1,3-diamine
-
-
-
?
[eIF5A-precursor]-lysine + spermidine
[eIF5A-precursor]-deoxyhypusine + propane-1,3-diamine
-
-
-
?
[eIF5A-precursor]-lysine + spermidine
[eIF5A-precursor]-deoxyhypusine + propane-1,3-diamine
deoxyhypusine synthase is the first of the two enzymes that catalyze the maturation of eukaryotic initiation factor 5A. Synthesis of hypusine is essential for the function of eIF5A in eukaryotic cell proliferation and survival
-
-
?
[eIF5A-precursor]-lysine + spermidine
[eIF5A-precursor]-deoxyhypusine + propane-1,3-diamine
-
-
-
-
?
[eIF5A-precursor]-lysine + spermidine
[eIF5A-precursor]-deoxyhypusine + propane-1,3-diamine
-
-
-
-
?
[eIF5A-precursor]-lysine + spermidine
[eIF5A-precursor]-deoxyhypusine + propane-1,3-diamine
-
the enzyme catalyzes the first reaction in a two-step conversion of inactive eIF-5A to its active form
-
-
?
[eIF5A-precursor]-lysine + spermidine
[eIF5A-precursor]-deoxyhypusine + propane-1,3-diamine
-
-
-
?
[eIF5A-precursor]-lysine + spermidine
[eIF5A-precursor]-deoxyhypusine + propane-1,3-diamine
-
-
-
-
?
[eIF5A-precursor]-lysine + spermidine
[eIF5A-precursor]-deoxyhypusine + propane-1,3-diamine
-
-
-
-
?
[eIF5A-precursor]-lysine + spermidine
[eIF5A-precursor]-deoxyhypusine + propane-1,3-diamine
hypusination of Lys56
-
-
?
[eIF5A-precursor]-lysine + spermidine
[eIF5A-precursor]-deoxyhypusine + propane-1,3-diamine
-
-
-
-
?
[eIF5A-precursor]-lysine + spermidine
[eIF5A-precursor]-deoxyhypusine + propane-1,3-diamine
-
the enzyme catalyzes the first reaction in a two-step conversion of inactive eIF-5A to its active form
-
-
?
[eIF5A-precursor]-lysine + spermidine
[eIF5A-precursor]-deoxyhypusine + propane-1,3-diamine
-
-
-
-
?
[eIF5A-precursor]-lysine + spermidine
[eIF5A-precursor]-deoxyhypusine + propane-1,3-diamine
-
-
-
-
ir
[eIF5A-precursor]-lysine + spermidine
[eIF5A-precursor]-deoxyhypusine + propane-1,3-diamine
-
-
-
?
[eIF5A-precursor]-lysine + spermidine
[eIF5A-precursor]-deoxyhypusine + propane-1,3-diamine
-
-
-
-
?
[eIF5A-precursor]-lysine + spermidine
[eIF5A-precursor]-deoxyhypusine + propane-1,3-diamine
-
-
-
?
[eIF5A-precursor]-lysine + spermidine
[eIF5A-precursor]-deoxyhypusine + propane-1,3-diamine
-
first step in the biosynthesis of hypusine
-
-
?
[eIF5A-precursor]-lysine + spermidine
[eIF5A-precursor]-deoxyhypusine + propane-1,3-diamine
first step in the biosynthesis of hypusine
-
-
?
[eIF5A-precursor]-lysine + spermidine
[eIF5A-precursor]-deoxyhypusine + propane-1,3-diamine
-
posttranslational activation of eIF-5A which has a specialized role in proliferation and in serum starvation-induced apoptosis in endothelial cells
-
-
?
[eIF5A-precursor]-lysine + spermidine
[eIF5A-precursor]-deoxyhypusine + propane-1,3-diamine
-
-
-
-
?
[eIF5A-precursor]-lysine + spermidine
[eIF5A-precursor]-deoxyhypusine + propane-1,3-diamine
-
-
-
-
?
[eIF5A-precursor]-lysine + spermidine
[eIF5A-precursor]-deoxyhypusine + propane-1,3-diamine
-
-
-
-
?
[eIF5A-precursor]-lysine + spermidine
[eIF5A-precursor]-deoxyhypusine + propane-1,3-diamine
-
-
-
-
?
[eIF5A-precursor]-lysine + spermidine
[eIF5A-precursor]-deoxyhypusine + propane-1,3-diamine
-
-
-
?
[eIF5A-precursor]-lysine + spermidine
[eIF5A-precursor]-deoxyhypusine + propane-1,3-diamine
-
-
-
?
[eIF5A-precursor]-lysine + spermidine
[eIF5A-precursor]-deoxyhypusine + propane-1,3-diamine
-
-
-
-
?
[eIF5A-precursor]-lysine + spermidine
[eIF5A-precursor]-deoxyhypusine + propane-1,3-diamine
-
-
-
-
?
[eIF5A-precursor]-lysine + spermidine
[eIF5A-precursor]-deoxyhypusine + propane-1,3-diamine
-
-
-
?
[eIF5A-precursor]-lysine + spermidine
[eIF5A-precursor]-deoxyhypusine + propane-1,3-diamine
-
-
-
?
[eIF5A-precursor]-lysine + spermidine
[eIF5A-precursor]-deoxyhypusine + propane-1,3-diamine
the enzyme is involved in synthesis of synthesis of homospermidine
-
-
?
[eIF5A-precursor]-lysine + spermidine
[eIF5A-precursor]-deoxyhypusine + propane-1,3-diamine
-
-
-
-
?
[eIF5A-precursor]-lysine + spermidine
[eIF5A-precursor]-deoxyhypusine + propane-1,3-diamine
-
-
-
-
?
[eIF5A-precursor]-lysine + spermidine
[eIF5A-precursor]-deoxyhypusine + propane-1,3-diamine
-
the enzyme catalyzes the first reaction in a two-step conversion of inactive eIF-5A to its active form
-
-
?
[eIF5A-precursor]-lysine + spermidine
[eIF5A-precursor]-deoxyhypusine + propane-1,3-diamine
-
-
-
?
[eIF5A-precursor]-lysine + spermidine
[eIF5A-precursor]-deoxyhypusine + propane-1,3-diamine
posttranslational activation of the initiation factor 5A
-
-
?
[eIF5A-precursor]-lysine + spermidine
[eIF5A-precursor]-deoxyhypusine + propane-1,3-diamine
-
-
-
?
[eIF5A-precursor]-lysine + spermidine
[eIF5A-precursor]-deoxyhypusine + propane-1,3-diamine
-
-
-
?
[eIF5A-precursor]-lysine + spermidine
[eIF5A-precursor]-deoxyhypusine + propane-1,3-diamine
-
-
-
-
?
[eIF5A-precursor]-lysine + spermidine
[eIF5A-precursor]-deoxyhypusine + propane-1,3-diamine
-
-
-
?
[eIF5A-precursor]-lysine + spermidine
[eIF5A-precursor]-deoxyhypusine + propane-1,3-diamine
Trypanosoma brucei brucei 927 / 4 GUTat10.1 / TREU927
-
-
-
?
[eIF5A-precursor]-lysine + spermidine
[eIF5A-precursor]-deoxyhypusine + propane-1,3-diamine
-
-
-
-
?
[TveIF-5A-precursor]-lysine + spermidine
[TveIF-5A-precursor]-deoxyhypusine + propane-1,3-diamine
-
-
-
?
[TveIF-5A-precursor]-lysine + spermidine
[TveIF-5A-precursor]-deoxyhypusine + propane-1,3-diamine
-
-
-
?
additional information
?
-
-
deoxyhypusine synthase-suppressed Brassica napus plants have larger leaves as well as enhanced seed yield, this appears to reflect increased tolerance to chronic sublethal stress
-
-
?
additional information
?
-
-
as racemic mixtures, only 2-MeSpd and 3-MeSpd support long-term growth (9-18 days) of spermidine-depleted DU-145 cells, whereas gamma-MeSpd and omega-MeSpd do not
-
-
?
additional information
?
-
the rTvDHS enzyme is bifunctional and is also involved in the hydroxylation of deoxyhypusine-containing rTveIF-5A, cf. EC 1.14.99.29
-
-
?
additional information
?
-
-
the rTvDHS enzyme is bifunctional and is also involved in the hydroxylation of deoxyhypusine-containing rTveIF-5A, cf. EC 1.14.99.29
-
-
?
additional information
?
-
the rTvDHS enzyme is bifunctional and is also involved in the hydroxylation of deoxyhypusine-containing rTveIF-5A, cf. EC 1.14.99.29
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
(4-[[2-(1H-benzimidazol-2-yl)hydrazinylidene]methyl]phenyl)(hydroxy)oxoammonium
55% inhibition
(R)-3-methylspermidine
competitive inhibition versus spermidine
(S)-3-methylspermidine
competitive inhibition versus spermidine
1-(3-aminopropyl)-4-aminomethylpiperidine
-
1 mM, less than 50% inhibition
1-amino-7-guanidinoheptane
-
competitive, inhibits binding of spermidine to the enzyme
1-aminooctane
-
1 mM, less than 50% inhibition
1-methylspermidine
-
0.184 mM, 50% inhibition
6-bromo-N-(1H-indol-4-yl)-1-benzothiophene-2-carboxamide
the 6'-bromo substituent is necessary for binding to DHPS
6-fluorospermidine
-
0.048 mM, 50% inhibition
7,7-Difluorospermidine
-
1 mM, less than 50% inhibition
8-fluoro-N-[3-(morpholin-4-yl)propyl]-5H-pyrimido[5,4-b]indol-4-amine
23.6% inhibition
aminopropylcadaverine
-
inhibition of deoxyhypusine synthesis
diaminononane
weaker inhibition
GC7
-
a specific DHS-inhibitor, inhibits DHS by competitive replacement of its native spermidine substrate. Inhibition of DHS by GC7 induces antiproliferative effects in vitro. The compound shows a strong antiproliferative effect in glioblastoma cell lines in vitro, while normal human astrocytes are not affected, and it causes p53 dependent premature senescence, a permanent cell cycle arrestin U-MG 87 cells
Homospermidine
-
inhibition of deoxyhypusine synthesis
N''-guanyl-1,7-diaminoheptane
N,N'-bis-benzyldiaminooctane
-
1 mM, less than 50% inhibition
N,N'-bis[3,5-bis[1(aminoiminomethyl)-hydrazoethyl]phenyl]decanediamide-tetrahydrochloride
N,N'-bis[3,5-bis[1(aminoiminomethyl)-hydrazoethyl]phenyl]dodecanediamide-tetrahydrochloride
N-(2-cyanoethyl)-1,3-diaminopropane
-
1 mM, less than 50% inhibition
N-(3-aminopropyl)-1,3-diaminopropane
-
1 mM, less than 50% inhibition
N-(3-aminopropyl)-1,4-diamino-cis-but-2-ene
-
-
N-(3-aminopropyl)-1,4-diamino-trans-but-2-ene
-
-
N-(3-aminopropyl)-cadaverine
-
-
N-(3-aminopropyl)-cis-1,4-diaminocyclohexane
-
1 mM, less than 50% inhibition
N-(3-aminopropyl)-N'-methylbutane-1,4-diamine
-
-
N-(3-aminopropyl)-trans-1,4-diaminocyclohexane
-
1 mM, less than 50% inhibition
N-(3-cyanopropyl)-1,3-diaminopropane
-
1 mM, less than 50% inhibition
N-(7-chloroquinolin-4-yl)-N'-methylpropane-1,3-diamine
12.45% inhibition
N-butyl-1,3-diaminopropane
-
1 mM, less than 50% inhibition
N-guanyl-1,7-diaminoheptane
shows only little inhibitory effect on the leishmanial recombinant DHS34
N1,N3-bis-guanyl-1,3-diaminopropane
-
1 mM, less than 50% inhibition
N1,N3-bis-tert-butyloxycarbonylspermidine
-
1 mM, less than 50% inhibition
N1,N6-bis-guanyl-1,6-diaminohexane
-
-
N1,N7-bis-allylcaldine
-
1 mM, less than 50% inhibition
N1,N7-bis-benzylcaldine
-
1 mM, less than 50% inhibition
N1,N7-bis-dimethylcaldine
-
1 mM, less than 50% inhibition
N1,N7-bis-guanyl-1,7-diaminoheptane
-
-
N1,N7-bis-guanylcaldine
-
-
N1,N8-bis-guanyl-1,8-diaminooctane
-
-
N1-acetylspermidine
-
1 mM, less than 50% inhibition
N1-guanyl-1,3-diaminopropane
-
1 mM, less than 50% inhibition
N1-guanyl-1,7-diaminoheptane
N1-guanyl-1,8-diaminooctane
-
-
N1-methylspermidine
-
inhibits generation of spermidine from [eIF5A-precursor]-deoxyhypusine
N3-ethylspermidine
-
1 mM, less than 50% inhibition
N4-(3-aminopropyl)-4-methylpentane-1,4-diamine
-
1 mM, less than 50% inhibition
N4-acetylspermidine
-
1 mM, less than 50% inhibition
N4-benzoylspermidine
-
1 mM, less than 50% inhibition
N4-benzylspermidine
-
1 mM, less than 50% inhibition
N4-bromoacetylspermidine
-
1 mM, less than 50% inhibition
N4-methylcaldine
-
1 mM, less than 50% inhibition
paromomycin
inhibits oocysts formation
putrescine
-
1 mM, less than 50% inhibition
1,3-diaminopropane
-
-
1,7-Diaminoheptane
-
inhibits generation of spermidine from [eIF5A-precursor]-deoxyhypusine
1,8-diaminooctane
weaker inhibition
6,6'-difluorospermidine
-
inhibition of deoxyhypusine synthesis
6,6'-difluorospermidine
-
0.014 mM, 50% inhibition
caldine
-
inhibition of deoxyhypusine synthesis
CNI-1493
-
inhibition in vitro and in vivo, inhibits germination conidia. Although DHS of wheat, fungus, and human can be equally inhibited by the inhibitor CNI-1493 in vitro, application during infection of wheat and maize flowers results in strong inhibition of the pathogen without interference with kernel development, providing the possibiity to selectively inhibit fungal growth without affecting plant growth
CNI-1493
a compound that inhibits fungal DHS activity without affecting grain development
CNI-1493
-
inhibition in vitro. Although DHS of wheat, fungus, and human can be equally inhibited by the inhibitor CNI-1493 in vitro, application during infection of wheat and maize flowers results in strong inhibition of the pathogen without interference with kernel development, providing the possibiity to selectively inhibit fungal growth without affecting plant growth
CNI-1493
-
inhibition in vitro. Although DHS of wheat, fungus, and human can be equally inhibited by the inhibitor CNI-1493 in vitro, application during infection of wheat and maize flowers results in strong inhibition of the pathogen without interference with kernel development, providing the possibiity to selectively inhibit fungal growth without affecting plant growth
deoxyspergualin
-
-
N''-guanyl-1,7-diaminoheptane
i.e. GC7, almost complete inhibition at 20 microM in both one-step and two-step assays
N''-guanyl-1,7-diaminoheptane
i.e. GC7. Downregulation of eIF5A through inhibition of deoxyhypusine synthase favors the reversal of the Th1 mediated cellular processes but minimally affects CD8 T-cells. Inhibition of elF5A increases the Treg/Th17 ratio, reduces anti-GAD65 antibody production and islet/beta-cell ER stress that leads to improvement in the endocrine pancreas functionality in a humanized model of T1D. Diabetes onset is delayed
N''-guanyl-1,7-diaminoheptane
GC7, a spermidine analogue
N,N'-bis[3,5-bis[1(aminoiminomethyl)-hydrazoethyl]phenyl]decanediamide-tetrahydrochloride
-
i.e. CNI-1493
N,N'-bis[3,5-bis[1(aminoiminomethyl)-hydrazoethyl]phenyl]decanediamide-tetrahydrochloride
-
i.e. CNI-1493
N,N'-bis[3,5-bis[1(aminoiminomethyl)-hydrazoethyl]phenyl]dodecanediamide-tetrahydrochloride
-
i.e. DHSI-15
N,N'-bis[3,5-bis[1(aminoiminomethyl)-hydrazoethyl]phenyl]dodecanediamide-tetrahydrochloride
-
i.e. DHSI-15
N1-ethylspermidine
-
inhibits generation of spermidine from [eIF5A-precursor]-deoxyhypusine
N1-ethylspermidine
-
1 mM, less than 50% inhibition
N1-guanyl-1,7-diaminoheptane
GC7, a potent competitive inhibitor of DHS, causes an effective inhibition of infection and growth of Cryptosporidium parvum in human HCT-8 adenocarcinoma cells. Complete inhibition at 0.01 mM
N1-guanyl-1,7-diaminoheptane
-
-
N1-guanyl-1,7-diaminoheptane
-
inhibits generation of spermidine from [eIF5A-precursor]-deoxyhypusine
N1-guanyl-1,7-diaminoheptane
competitive
N1-guanyl-1,7-diaminoheptane
-
N1-guanyl-1,7-diaminoheptane
-
i.e. GC7
N1-guanyl-1,7-diaminoheptane
-
-
N1-guanyl-1,7-diaminoheptane
GC7, inhibits the activity of TbDHSc-TbDBHSp heterotetrameric complex; GC7, inhibits the activity of TbDHSc-TbDBHSp heterotetrameric complex
spermidine
-
inhibits generation of spermidine from [eIF5A-precursor]-deoxyhypusine
additional information
no growth inhibition by alpha-difluoromethylornithine, an inhibitor of polyamine biosynthesis, and (R)-3-methylspermidine, while the the combination of alpha-difluoromethylornithine with a racemate or (S)-3-methylspermidine causes cessation of cell growth. Cells treated with racemic 3-MeSpd accumulat intracellularly mainly (S)-3-methylspermidine, but not DHS substrate (R)-3-methylspermidine, explaining the inability of the racemate to support long-term growth
-
additional information
inhibitor screning in an anti-malaria compound collection, a guanyl residue seems to be an important lead structure for inhibition of Theileria parva DHS enzyme
-
additional information
-
inhibitor screning in an anti-malaria compound collection, a guanyl residue seems to be an important lead structure for inhibition of Theileria parva DHS enzyme
-
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evolution
CpDHS is more closely related to apicomplexan and human DHS than to kinetoplast DHS
evolution
-
homospermidine synthase, HSS, EC 2.5.1.44/45, evolved from the gene encoding deoxyhypusine synthase, DHS, by gene duplication. HSS and deoxyhypusine synthase have also diverged with respect to their regulation
evolution
-
homospermidine synthase, HSS, EC 2.5.1.44/45, evolved from the gene encoding deoxyhypusine synthase, DHS, by gene duplication. HSS and deoxyhypusine synthase have also diverged with respect to their regulation
evolution
-
homospermidine synthase, HSS, EC 2.5.1.44/45, evolved from the gene encoding deoxyhypusine synthase, DHS, by gene duplication. HSS and deoxyhypusine synthase have also diverged with respect to their regulation
evolution
-
homospermidine synthase, HSS, EC 2.5.1.44/45, evolved from the gene encoding deoxyhypusine synthase, DHS, by gene duplication. HSS and deoxyhypusine synthase have also diverged with respect to their regulation
evolution
-
homospermidine synthase, HSS, EC 2.5.1.44/45, evolved from the gene encoding deoxyhypusine synthase, DHS, by gene duplication. HSS and deoxyhypusine synthase have also diverged with respect to their regulation
evolution
-
homospermidine synthase, HSS, EC 2.5.1.44/45, evolved from the gene encoding deoxyhypusine synthase, DHS, by gene duplication. HSS and deoxyhypusine synthase have also diverged with respect to their regulation
evolution
-
homospermidine synthase, HSS, EC 2.5.1.44/45, evolved from the gene encoding deoxyhypusine synthase, DHS, by gene duplication. HSS and deoxyhypusine synthase have also diverged with respect to their regulation
malfunction
-
a haploid Saccharomyces cerevisiae strain with disruption of the DHS gene is not viable, and can be rescued by a plasmid encoding the wild type DHS. When examined under the microscope, a non-viable DHS-disrupted ascus from a tetrad dissection grows several generations to a colony of 100-200 enlarged cells before growth arrest
malfunction
-
Dhps+/- mice appear normal and do not show any growth defects or phenotypes. When the heterozygous male and female mice are crossed, no pups are born with the genotype of Dhps-/- homozygous deletion, indicating that DHS is vital for growth and survival
malfunction
DHSL20 lacks the catalytic lysine residue at residue 344, which is indispensable for the enzymatic reaction and is present in the active center for catalysis, and contains leucine instead
malfunction
gene deletion mutations are attempted via targeted gene replacement. Chromosomal null mutants of DHS34 could only be obtained in the presence of a DHS34-containing episome, indicating that DHS34 is an essential gene
malfunction
-
deoxyhypusine synthase haploinsufficiency attenuates acute cytokine signaling, overview. DHS dysfunction in the setting of diabetes mellitus, overview
malfunction
-
inhibition of DHS by GC7 induces antiproliferative effects in vitro. GC7 treatment induces premature senescence in U87-MG cells, co-treatment of glioblastoma cells with TMZ/BCNU and GC7 has an additive antiproliferative effect
malfunction
-
inhibition of proliferation of BA/F3 p210 cells including the imatinib resistant mutants M351T, E255K, and T315I by deoxyhypusine synthase inhibitors
malfunction
-
severe effects of knockout of Eif5a gene or Dhps gene in mice in cell lines RRE174 with Eif5a disruption and RRM039 with Dhps disruption, Eif5a heterozygous knockout mice and Dhps heterozygous knockout mice are viable and fertile, but, homozygous Eif5a1gt/gt embryos and Dhpsgt/gt embryos die early in embryonic development. Upon transfer to in vitro culture, homozygous Eif5agt/gt or Dhpsgt/gt blastocysts at E3.5 show growth defects when compared to heterozygous or wild-type blastocysts
malfunction
DHS enzyme inhibition by N1-guanyl-1,7-diaminoheptane results in a significant decrease in tumor formation in vivo. In patients with esophageal squamous cell carcinoma, overexpression of gene DHPS in ESCC tumors is significantly associated with worse recurrence-free survival, and correlated with distant metastasis. Although the mRNA levels of RhoA in DHPS-knockdown cells do not change, RhoA protein levels significantly decrease compared with control
malfunction
early flowering phenotype of dexamethasone-treated siDHS knockout transgenic plants, hypersensitivityof siDHS transgenic plants to osmotic stressors and abscisic acid. The sensitivity of transgenic siDHS plantsto abscisic acid in the absence of the silencing drug dexamethasone probably reflects that the genetic inactivation system is slightly leaky and that minor inactivation of the eIF5A pathway is very sensitive to alterations in abscisic acid homeostasis. Non-silenced siDHS plants display partial growth inhibition under salt treatment. Alterations in root cell expansion and root hair phenotypes caused by DHS silencing, overview
malfunction
importance of imbalances in eIF5A hypusination in Fusarium graminearum: overexpression of gene DHS leads to increased virulence in Triticum aestivum, elevated production of the mycotoxin deoxynivalenol, more infection structures, faster Triticum aestivum tissue invasion in plants and increases vegetatively produced conidia. Overexpression of the enzyme DOHH completely prevents infection structure formation, pathogenicity in Triticum aestivum and Zea mays, leads to overproduction of reactive oxygen species, reduced DON mycotoxin production and increased sexual reproduction. Simultaneous overexpression of both genes restores wild type-like phenotypes, strongly increased hypusinated eIF5A in DOHH overexpression mutant in comparison to wild-type, and the DHS overexpression mutants
malfunction
-
the dys1-1 mutant shows a strong depletion of mutated Dys1 protein, resulting in more than 2fold decrease in hypusine levels relative to the wild type. he growth phenotype of dys1-1 mutant is severe, growing only in the presence of 1 M sorbitol, an osmotic stabilizer, the sorbitol requirement from dys1-1 is not associated with cell lysis. The dys1-1 mutant genetically interacts with the sole yeast protein kinase C (Pkc1) and Asc1, a component of the 40S ribosomal subunit. The dys1-1 mutant is synthetically lethal in combination with asc1DELTA and overexpression of TIF51A (eIF5A) or DYS1 is toxic for an asc1DELTA strain. Inactive Pkc1 (K853R) form does not affect the dys1-1 mutant. Dys1-1 mutant phenotype, overview
malfunction
-
gene deletion mutations are attempted via targeted gene replacement. Chromosomal null mutants of DHS34 could only be obtained in the presence of a DHS34-containing episome, indicating that DHS34 is an essential gene
-
malfunction
-
deoxyhypusine synthase haploinsufficiency attenuates acute cytokine signaling, overview. DHS dysfunction in the setting of diabetes mellitus, overview
-
malfunction
-
severe effects of knockout of Eif5a gene or Dhps gene in mice in cell lines RRE174 with Eif5a disruption and RRM039 with Dhps disruption, Eif5a heterozygous knockout mice and Dhps heterozygous knockout mice are viable and fertile, but, homozygous Eif5a1gt/gt embryos and Dhpsgt/gt embryos die early in embryonic development. Upon transfer to in vitro culture, homozygous Eif5agt/gt or Dhpsgt/gt blastocysts at E3.5 show growth defects when compared to heterozygous or wild-type blastocysts
-
malfunction
-
early flowering phenotype of dexamethasone-treated siDHS knockout transgenic plants, hypersensitivityof siDHS transgenic plants to osmotic stressors and abscisic acid. The sensitivity of transgenic siDHS plantsto abscisic acid in the absence of the silencing drug dexamethasone probably reflects that the genetic inactivation system is slightly leaky and that minor inactivation of the eIF5A pathway is very sensitive to alterations in abscisic acid homeostasis. Non-silenced siDHS plants display partial growth inhibition under salt treatment. Alterations in root cell expansion and root hair phenotypes caused by DHS silencing, overview
-
metabolism
-
deoxyhypusine synthase catalyzes a step in hypusine sythesis, a unique mmoified lysine derivative of eukaryotic translation initiation factor 5A, eIF5A
metabolism
first enzyme of the hypusine pathway
metabolism
-
the functions of Asc1 associated with protein synthesis are necessary in the absence of wild type levels of hypusine-containing eIF5A in the cell
metabolism
the enzyme is involved in synthesis of synthesis homospermidine
metabolism
-
first enzyme of the hypusine pathway
-
physiological function
-
deoxyhypusine synthase catalyzes the synthesis of deoxyhypusine [N?-(4-aminobutyl)-lysine], the first step in the post-translational synthesis of an unusual amino acid hypusine [N?-(4-amino-2-hydroxybutyl)-lysine]
physiological function
deoxyhypusine synthase, an NAD+-dependent enzyme, catalyzes the first step in the post-translational synthesis of an unusual amino acid, hypusine (N-(4-amino-2-hydroxybutyl)lysine), in the eukaryotic initiation factor 5A precursor protein, DHS34 is essential for Leishmania donovani
physiological function
-
deoxyhypusine synthase, DHS, catalyzes the post-translational formation of the amino acid hypusine. Hypusine is unique to the eukaryotic translational initiation factor 5A (eIF5A), and is required for its functions in mRNA shuttling, translational elongation and stress granule formation. DHS promotes cytokine and ER stress signaling in the islet beta cell and thereby contributes to its dysfunction in the setting of diabetes mellitus
physiological function
-
eukaryotic translation initiation factor 5A, eIF5A, is a small acidic protein and the only cellular protein that contains the unique modified lysine, hypusine [N1-(4-amino-2-hydroxybutyl)lysine]. Hypusine is formed by the post-translational modification of one specific lysine residue of the eIF5A precursor, eIF5A(Lys), in two consecutive enzymatic steps. The first enzyme, deoxyhypusine synthase, DHS, catalyzes the transfer of the aminobutyl moiety from the polyamine spermidine to form an intermediate, deoxyhypusine [N1-(4-aminobutyl)lysine] residue, which is subsequently hydroxylated by deoxyhypusine hydroxylase
physiological function
-
hypusine is formed posttranslationally by the addition of the 4-aminobutyl moiety from the polyamine spermidine to a specific lysine residue, catalyzed by deoxyhypusine synthase, DHPS, and subsequent hydroxylation by deoxyhypusine hydroxylase, DOHH. Essential role of eIF5A-1 and deoxyhypusine synthase in mouse embryonic development, overview
physiological function
-
hypusine modification is an irreversible protein modification and naturally occurring eIF5A exists predominantly as the hypusinated form. Deoxyhypusine synthase catalyzes the transfer of the aminobutyl moiety from spermidine to a specific lysine of the eIF5A precursor to form the deoxyhypusine [N?-(4-aminobutyl)lysine] intermediate. Hypusine is formed from deoxyhypusine by the action of EC 1.14.99.29, deoxyhypusine monooxygenase
physiological function
activation of eukaryotic translation initiation factor eIF5A requires a posttranslational modification, forming the unique amino acid hypusine. This activation is mediated by two enzymes, deoxyhypusine synthase, DHS, and deoxyhypusine hydroxylase, DOHH. Enzyme DHS catalyzes eIF5A Lys56 hypusination and is essential in Fusarium graminearum
physiological function
hypusination of eIF5A is an important post-translational modification essential for cell proliferation. This modification occurs in a two step processcatalyzed by deoxyhypusine synthase followed by deoxyhypusine hydroxylase
physiological function
hypusine is formed from spermidine, a metabolite of polyamine metabolism, by the sequential action of two catalytic enzymes, deoxyhypusine synthase (DHPS) and deoxyhypusine hydroxylase (DOHH). These enzymes have an important role in post-translational modification of eukaryotic translation factor 5A (eIF5A), which functions in protein synthesis. The hypusine cascade contributes to cell proliferation and embryogenesis by the regulation of translation elongation in healthy cells. DHPS-mediated hypusine-modification of eukaryotic translation factor 5A facilitates the translation of RhoA, resulting in the activation of the RhoA signaling pathway and leading to not only increased cell motility, invasion and metastasis of cancer cells in vitro, but also increased tumor growth in vivo. DHPS regulates the expression and activation of RhoA, DHPS may regulate the organization of F-actin through the increase in RhoA protein level. Hypusinated eIF5A may regulate tumor growth and metastasis via the RhoA signaling pathway
physiological function
the enzyme deoxyhypusine synthase is required for spermidine-dependent hypusine modification of a lysine residue in the essential translation factor eIF5A. Enzyme DHS is essential for infectivity of Trypanosoma brucei in mice
physiological function
the enzyme is required for spermidine-mediated activation of eIF5A by hypusination. Activated elF5A is involved in several aspects of plant biology such as the control of flowering time, the aerial and root architecture, and root hair growth. In addition, the pathway is required for adaptation to challenging growth conditions such as high salt and high glucose medium and to elevated concentrations of the plant hormone abscisic acid
physiological function
the eukaryotic translation initiation factor 5A (eIF5A) is essential for cell proliferation, becoming functionally active only after post-translational conversion of a specific Lys to hypusine catalyzed by deoxyhypusine synthase, the rate-limiting enzyme of this two-step process
physiological function
the plant stress hormone abscisic acid causes a reduction in the hypusination of eIF5A1 probably through the post-transcriptional alteration of DHS activity
physiological function
-
translation factor eIF5A undergoes an essential and conserved posttranslational modification at a specific lysine, K51, to generate the residue hypusine. The enzymes deoxyhypusine synthase (Dys1) and deoxyhypusine hydroxylase (Lia1) catalyze this two-step modification process. Correlated role for eIF5A and Asc1 in coordinating the translational control of a subset of mRNAs associated with cell integrity
physiological function
translation elongation factor aIF5A is hypusinated and also forms a stable complex with deoxyhypusine synthase
physiological function
clonal transgenic parasites with integration of glmS riboswitch downstream of the DHS gene show DHS protein in the cytoplasm of in asexual stages. The DHS protein can be attenuated fivefold in transgenic parasites with an active riboswitch. Attenuation of DHS expression for 72 h leads to a significant reduction of hypusinated protein, while global protein synthesis is unaffected. Parasites with attenuated DHS expression show a significant growth defect. DHS-attenuated parasites show increased sensitivity to inhibitor N1-guanyl-1,7-diaminoheptane
physiological function
in a mouse model that enables the inducible, postnatal deletion of Dhps specifically in postnatal islet beta cells, removal of Dhps does not have an effect under normal physiologic conditions. Upon development of insulin resistance, which induces beta-cell proliferation, Dhps deletion causes alterations in proteins required for mRNA translation and protein secretion, reduced production of the cell cycle molecule cyclin D2, impaired beta-cell proliferation, and induces overt diabetes. Hypusine biosynthesis is downstream of protein kinase C-zeta and is required for c-Myc-induced proliferation
physiological function
-
virus-mediated PhDHS silencing causes a sectored chlorotic leaf phenotype. Chlorophyll levels and photosystem II activity are reduced, and chloroplast development is abnormal in DHS-silenced leaves. Silencing results in extended leaf longevity and thick leaves. 308 proteins are upregulated and 266 proteins are downregulated in DHS-silenced plants compared with control. The mRNA level of eIF5A-1 significantly decreases in DHS-silenced plants, while those of another three eIF5As are not significantly affected
physiological function
-
deoxyhypusine synthase, an NAD+-dependent enzyme, catalyzes the first step in the post-translational synthesis of an unusual amino acid, hypusine (N-(4-amino-2-hydroxybutyl)lysine), in the eukaryotic initiation factor 5A precursor protein, DHS34 is essential for Leishmania donovani
-
physiological function
-
deoxyhypusine synthase, DHS, catalyzes the post-translational formation of the amino acid hypusine. Hypusine is unique to the eukaryotic translational initiation factor 5A (eIF5A), and is required for its functions in mRNA shuttling, translational elongation and stress granule formation. DHS promotes cytokine and ER stress signaling in the islet beta cell and thereby contributes to its dysfunction in the setting of diabetes mellitus
-
physiological function
-
hypusine is formed posttranslationally by the addition of the 4-aminobutyl moiety from the polyamine spermidine to a specific lysine residue, catalyzed by deoxyhypusine synthase, DHPS, and subsequent hydroxylation by deoxyhypusine hydroxylase, DOHH. Essential role of eIF5A-1 and deoxyhypusine synthase in mouse embryonic development, overview
-
physiological function
-
the plant stress hormone abscisic acid causes a reduction in the hypusination of eIF5A1 probably through the post-transcriptional alteration of DHS activity
-
physiological function
-
the enzyme is required for spermidine-mediated activation of eIF5A by hypusination. Activated elF5A is involved in several aspects of plant biology such as the control of flowering time, the aerial and root architecture, and root hair growth. In addition, the pathway is required for adaptation to challenging growth conditions such as high salt and high glucose medium and to elevated concentrations of the plant hormone abscisic acid
-
physiological function
-
translation elongation factor aIF5A is hypusinated and also forms a stable complex with deoxyhypusine synthase
-
physiological function
Trypanosoma brucei brucei 927 / 4 GUTat10.1 / TREU927
-
the enzyme deoxyhypusine synthase is required for spermidine-dependent hypusine modification of a lysine residue in the essential translation factor eIF5A. Enzyme DHS is essential for infectivity of Trypanosoma brucei in mice
-
additional information
-
Dhps heterozygosity does not lead to significant inhibition of proliferation or cell cycle progression, Dhps heterozygosity does not alter growth or metabolic homeostasis, overview
additional information
-
inhibition of eIF5A by siRNA or DHS-inhibitors in combination with Imatinib exerts synergistic cytotoxic effects on BCR-ABL positive cell lines
additional information
-
structural modeling of DHS34, overview
additional information
structural modeling of DHS34, overview
additional information
enzyme structure modelling, model evaluation and comparative structural analysis, overview
additional information
-
enzyme structure modelling, model evaluation and comparative structural analysis, overview
additional information
structural comparison of the three-dimensional structure of Theileria parva DHS with Homo sapiens DHS
additional information
-
structural comparison of the three-dimensional structure of Theileria parva DHS with Homo sapiens DHS
additional information
-
the Convulvulaceae species Ipomoea hederifolia contains ipanguline- and triangularine-type polyamines
additional information
-
the Convulvulaceae species Ipomoea meyeri contains triangularine-type polyamines
additional information
-
the Convulvulaceae species Ipomoea neei contains ipanguline-type polyamines
additional information
-
the Convulvulaceae species Merremia quinquefolia contains lycopsamine-type polyamines
additional information
the inability of racemic 3-methylspermidine and (S)-3-methylspermidine to support DU-145 cells growth due to the fact that only the (R)-isomer is a substrate of DHS, but this isomer, (R)-3-methylspermidine, competes with spermidine for cellular uptake and is less efficient than the (S)-3-methylspermidine, which results in accumulation of inactive (S)-3-methylspermidine in the cell. Synthesis of (S)-3-methylspermidine and (R)-3-methylspermidine, overview
additional information
Trypanosoma brucei encodes two deoxyhypusine synthase isozymes TbDHSc and TbDHSp that form a functional complex
additional information
Trypanosoma brucei encodes two deoxyhypusine synthase isozymes TbDHSc and TbDHSp that form a functional complex
additional information
Trypanosoma brucei encodes two deoxyhypusine synthase isozymes TbDHSc and TbDHSp that form a functional heterotetrameric complex
additional information
Trypanosoma brucei encodes two deoxyhypusine synthase isozymes TbDHSc and TbDHSp that form a functional heterotetrameric complex
additional information
-
structural modeling of DHS34, overview
-
additional information
-
Dhps heterozygosity does not lead to significant inhibition of proliferation or cell cycle progression, Dhps heterozygosity does not alter growth or metabolic homeostasis, overview
-
additional information
-
structural comparison of the three-dimensional structure of Theileria parva DHS with Homo sapiens DHS
-
additional information
Trypanosoma brucei brucei 927 / 4 GUTat10.1 / TREU927
-
Trypanosoma brucei encodes two deoxyhypusine synthase isozymes TbDHSc and TbDHSp that form a functional heterotetrameric complex
-
additional information
Trypanosoma brucei brucei 927 / 4 GUTat10.1 / TREU927
-
Trypanosoma brucei encodes two deoxyhypusine synthase isozymes TbDHSc and TbDHSp that form a functional complex
-
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D238A
-
NAD-site mutant, less than 5% activity of wild-type
D243A
-
spermidine-site mutant, no spermidine-binding
D313A
-
unable to bind eIF5A-precursor, no synthesis of deoxyhypusine
D316A
-
spermidine-site mutant, no spermidine-binding
D342A
-
NAD-site mutant, less than 5% activity of wild-type
E137A
-
NAD-site mutant, less than 5% activity of wild-type
E323A
-
spermidine-site mutant, no spermidine-binding
G283A
-
NAD-site mutant, activity similar to wild-type
K305A
-
spermidine-site mutant with retained avtivity
K329A
-
spermidine-site mutant, 18-24% spermidine binding capacity
N173S
recurrent missense variant identified with likely gene disrupting variant (c.1014+1G>A, c.912_917delTTACAT [p.Tyr305_Ile306del]), or c.1A>G [p.Met1] in unrelated individuals having similar neurodevelopmental features that include global developmental delay and seizures. Two of four affected females have short stature. The c.1014+1G>A variant causes aberrant splicing. Recombinant p.Asn173Ser or p.Tyr305_Ile306del protein show reduced (20%) or absent in vitro activity, respectively. The p.Tyr305_Ile306del and p.Asn173Ser variants result in reduced hypusination of eIF5A compared to wild-type DHPS enzyme
S317A
-
NAD-site mutant, activity similar to wild-type
T308A
-
NAD-site mutant, activity similar to wild-type
W327A
-
spermidine-site mutant, no spermidine-binding
L344K
mutant enzyme is still devoid of any DHS activity, suggesting that other differences in amino acid sequences also contribute to its inactivity
K308A
-
very low reaction rate
K308R
-
low reaction rate
K308R/K350E
-
no activity
K308R/K350P
-
no activity
K308R/K350R
-
no activity
D314A
site-directed mutagenesis, the mutant is active as deoxyhypusine synthase, but inactive as deoxyhypusine hydroxylase
H313A
site-directed mutagenesis, the mutant is active as deoxyhypusine synthase, but inactive as deoxyhypusine hydroxylase
D314A
-
site-directed mutagenesis, the mutant is active as deoxyhypusine synthase, but inactive as deoxyhypusine hydroxylase
-
H313A
-
site-directed mutagenesis, the mutant is active as deoxyhypusine synthase, but inactive as deoxyhypusine hydroxylase
-
D218A
mutation in catalytic site of subunit DHSp, mutant is unable to catalyze the single-turnover formation of NADH
D405A
mutation in catalytic site of subunit DHSc, impaired in activity
E103A
mutation in catalytic site of subunit DHSp, impaired in activity
E104A
mutation in catalytic site of subunit DHSp, impaired in activity
E166A
mutation in dead site of subunit DHSc, activity is similar to wild-type. The heterotetrameric complex shows a decrease in melting temperature by 4.9 degrees
H266A
mutation in dead site of subunit DHSp, activity is similar to wild-type
D218A
-
mutation in catalytic site of subunit DHSp, mutant is unable to catalyze the single-turnover formation of NADH
-
D405A
-
mutation in catalytic site of subunit DHSc, impaired in activity
-
E103A
-
mutation in catalytic site of subunit DHSp, impaired in activity
-
H266A
-
mutation in dead site of subunit DHSp, activity is similar to wild-type
-
H288A
-
6% of wild-type activity
H288A
-
spermidine-site mutant, no spermidine-binding
additional information
generation of deoxyhypusine synthase knockout mutants using siRNA via Agrobacterium strainGV3101/pMP90 transfection in Arabidopsis thaliana
additional information
-
generation of deoxyhypusine synthase knockout mutants using siRNA via Agrobacterium strainGV3101/pMP90 transfection in Arabidopsis thaliana
additional information
-
generation of deoxyhypusine synthase knockout mutants using siRNA via Agrobacterium strainGV3101/pMP90 transfection in Arabidopsis thaliana
-
additional information
replacement of the endogenous DHS and DOHH genes by homologous recombination with the PgpdA-DHS or Pgpd1-DOHH alleles, excluding any possibility of mutagenic effects by ectopic integration
additional information
-
replacement of the endogenous DHS and DOHH genes by homologous recombination with the PgpdA-DHS or Pgpd1-DOHH alleles, excluding any possibility of mutagenic effects by ectopic integration
additional information
variant recombinant proteins with i. a truncation of 48 or 97 NH2-terminal amino acids, ii. A truncation of 39 COOH-terminal amino acids, or iii. An internal deletion (ASp262-Ser317) are inactive. A chimeric protein consisting of the complete human sequence and 16 amino acids of the yeast sequence, Gln197-Asn212, not present in the human enzyme, inserted between Glu193 and Gln194 exhibit moderate activity
additional information
-
variant recombinant proteins with i. a truncation of 48 or 97 NH2-terminal amino acids, ii. A truncation of 39 COOH-terminal amino acids, or iii. An internal deletion (ASp262-Ser317) are inactive. A chimeric protein consisting of the complete human sequence and 16 amino acids of the yeast sequence, Gln197-Asn212, not present in the human enzyme, inserted between Glu193 and Gln194 exhibit moderate activity
additional information
-
DHS knock-down by stable lentiviral expression of shRNAs in G55T2 and U87-MG cells
additional information
DHPS gene silencing by transfection of DHPS-specific short hairpin RNA (shRNA) in LM-pGL4.5 cells
additional information
-
DHPS gene silencing by transfection of DHPS-specific short hairpin RNA (shRNA) in LM-pGL4.5 cells
additional information
during purification and crystallization, residue C177 is is covalently modified to a 2-mercaptoethanol adduct
additional information
-
during purification and crystallization, residue C177 is is covalently modified to a 2-mercaptoethanol adduct
additional information
-
DHS34 gene deletion mutations via targeted gene replacement, chromosomal null mutants of DHS34 are only obtained in the presence of a DHS34-containing episome. HYGDELTAdhs34 and PHLEODELLTAdhs34 gene replacement cassettes are individually transfected into wild-type parasites, phenotypes, verview
additional information
DHS34 gene deletion mutations via targeted gene replacement, chromosomal null mutants of DHS34 are only obtained in the presence of a DHS34-containing episome. HYGDELTAdhs34 and PHLEODELLTAdhs34 gene replacement cassettes are individually transfected into wild-type parasites, phenotypes, verview
additional information
-
DHS34 gene deletion mutations via targeted gene replacement, chromosomal null mutants of DHS34 are only obtained in the presence of a DHS34-containing episome. HYGDELTAdhs34 and PHLEODELLTAdhs34 gene replacement cassettes are individually transfected into wild-type parasites, phenotypes, verview
-
additional information
-
construction of heterozygous or homozygous knockout mice via stem cell lines, phenotypes, overview
additional information
-
construction of heterozygous or homozygous knockout mice via stem cell lines, phenotypes, overview
-
additional information
-
generation of the dys1-1 mutant that has a defect in total protein synthesis, a defect in polysome profile indicative of a translation elongation defect and a reduced association of eIF5A with polysomes
additional information
generation of a knockout mutant by gene replacement
additional information
generation of a knockout mutant by gene replacement
additional information
mutation of sets of matched pairs, where the same residue is changed in both the catalytic and dead site, melting temperature of mutants is similar to wild-type
additional information
Trypanosoma brucei brucei 927 / 4 GUTat10.1 / TREU927
-
generation of a knockout mutant by gene replacement
-
additional information
-
mutation of sets of matched pairs, where the same residue is changed in both the catalytic and dead site, melting temperature of mutants is similar to wild-type
-
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Wolff, E.C.; Park, M.H.; Folk, J.E.
Cleavage of spermidine as the first step in deoxyhypusine synthesis. The role of NAD+
J. Biol. Chem.
265
4793-4799
1990
Rattus norvegicus
brenda
Wolff, E.C.; Folk, J.E.; Park, M.H.
Enzyme-substrate intermediate formation at lysine 329 of human deoxyhypusine synthase
J. Biol. Chem.
272
15865-15871
1997
Homo sapiens
brenda
Chen, K.Y.; Liu, A.Y.C.
Biochemistry and function of hypusine formation on eukaryotic initiation factor 5A
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Homo sapiens, Mus musculus
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Homo sapiens (P49366)
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Deciphering the translation initiation factor 5A modification pathway in halophilic Archaea
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Biochimie
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Njuguna, J.T.; von Koschitzky, I.; Gerhardt, H.; Laemmerhofer, M.; Choucry, A.; Pink, M.; Schmitz-Spahnke, S.; Bakheit, M.A.; Strube, C.; Kaiser, A.
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Theileria parva (Q4UDC3), Theileria parva, Theileria parva Muguga (Q4UDC3)
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Arabidopsis thaliana (Q9FI94), Arabidopsis thaliana, Arabidopsis thaliana Col-0 (Q9FI94)
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Nguyen, S.; Jones, D.C.; Wyllie, S.; Fairlamb, A.H.; Phillips, M.A.
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Mittal, N.; Morada, M.; Tripathi, P.; Gowri, V.S.; Mandal, S.; Quirch, A.; Park, M.H.; Yarlett, N.; Madhubala, R.
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Cryptosporidium parvum (A3FQA5), Cryptosporidium parvum
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Muramatsu, T.; Kozaki, K.I.; Imoto, S.; Yamaguchi, R.; Tsuda, H.; Kawano, T.; Fujiwara, N.; Morishita, M.; Miyano, S.; Inazawa, J.
The hypusine cascade promotes cancer progression and metastasis through the regulation of RhoA in squamous cell carcinoma
Oncogene
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Homo sapiens (P49366), Homo sapiens
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Kaltenegger, E.; Eich, E.; Ober, D.
Evolution of homospermidine synthase in the convolvulaceae: a story of gene duplication, gene loss, and periods of various selection pressures
Plant Cell
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Convolvulus arvensis, Ipomoea neei, Ipomoea hederifolia, Ipomoea alba, Ipomoea meyeri, Distimake quinquefolius, Convolvulus tricolor
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Galvao, F.C.; Rossi, D.; Silveira, W.d.a..S.; Valentini, S.R.; Zanelli, C.F.
The deoxyhypusine synthase mutant dys1-1 reveals the association of eIF5A and Asc1 with cell wall integrity
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Saccharomyces cerevisiae
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Homo sapiens (P49366)
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Martinez-Rocha, A.L.; Woriedh, M.; Chemnitz, J.; Willingmann, P.; Kroeger, C.; Hadeler, B.; Hauber, J.; Schaefer, W.
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Fusarium graminearum (D5L6Z2), Fusarium graminearum
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Extremophiles
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Saccharolobus solfataricus (Q97ZF1), Saccharolobus solfataricus, Saccharolobus solfataricus DSM 1617 (Q97ZF1)
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Burnat, M.; Li, B.; Kim, S.; Michael, A.; Flores, E.
Homospermidine biosynthesis in the cyanobacterium Anabaena requires a deoxyhypusine synthase homologue and is essential for normal diazotrophic growth
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Nostoc sp. PCC 7120 = FACHB-418 (Q8YQL7)
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Ganapathi, M.; Padgett, L.R.; Yamada, K.; Devinsky, O.; Willaert, R.; Person, R.; Au, P.B.; Tagoe, J.; McDonald, M.; Karlowicz, D.; Wolf, B.; Lee, J.; Shen, Y.; Okur, V.; Deng, L.; LeDuc, C.A.; Wang, J.; Hanner, A.; Mirmira, R.G.; Park, M.H.; Mastracci, T.L.; Chung, W.K.
Recessive rare variants in deoxyhypusine synthase, an enzyme involved in the synthesis of hypusine, are associated with a neurodevelopmental disorder
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Homo sapiens (P49366)
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A new non-radioactive deoxyhypusine synthase assay adaptable to high throughput screening
Amino Acids
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Homo sapiens (P49366), Homo sapiens
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Schultz, C.R.; Geerts, D.; Mooney, M.; El-Khawaja, R.; Koster, J.; Bachmann, A.S.
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Homo sapiens (P49366)
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Biomolecules
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Homo sapiens (P49366), Homo sapiens
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Liu, J.; Chang, X.; Ding, B.; Zhong, S.; Peng, L.; Wei, Q.; Meng, J.; Yu, Y.
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Homo sapiens (P49366)
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Validation of Plasmodium falciparum deoxyhypusine synthase as an antimalarial target
PeerJ
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Plasmodium falciparum (Q8ILW8), Plasmodium falciparum
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eIF5A inhibition influences T cell dynamics in the pancreatic microenvironment of the humanized mouse model of type 1 diabetes
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Mus musculus (Q3TXU5), Mus musculus
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Mus musculus (Q3TXU5), Mus musculus
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Afanador, G.A.; Tomchick, D.R.; Phillips, M.A.
Trypanosomatid deoxyhypusine synthase activity is dependent on shared active-site complementation between pseudoenzyme paralogs
Structure
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2018
Trypanosoma brucei brucei (Q38BX0 and Q4GZD1), Trypanosoma brucei brucei 927/4 GUTat10.1 (Q38BX0 and Q4GZD1)
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