EC Number |
General Information |
Reference |
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1.14.99.29 | evolution |
hypusine occurs only in eukaryotes and certain archaea, but not in eubacteria |
716821 |
1.14.99.29 | evolution |
Plasmodium falciparum DOHH arose from an originally from an EF/type cyanobacterial phycobilin lyase by loss of function. It has a low FASTA score of 27 to its human counterpart |
713727 |
1.14.99.29 | evolution |
the deoxyhypusine/hypusine synthetic pathway has evolved in archaea and eukaryotes, evolution of eIF5A and the hypusine pathway, overview |
701650 |
1.14.99.29 | malfunction |
a mutated deoxyhypusine hydroxylase gene nero affects cell and organ size. However, nero is not required for cell viability. Loss of eIF5A causes phenotypes highly similar to nero but more severe than nero. Inhibition of Nero or eIF5A by RNAi causes a similar impairment in translation elongation |
713727 |
1.14.99.29 | malfunction |
a mutation in the dohh gene causes defects in mitochondrial morphology, distribution and displayed synthetic defects in growth |
713727 |
1.14.99.29 | malfunction |
inactivation of DOHH is recessively lethal |
701650 |
1.14.99.29 | malfunction |
inactivation of DOHH is recessively lethal, phenotypes resulting from depletion of DOHH and hypusine-modified eIF5A, overview |
701650 |
1.14.99.29 | metabolism |
biosynthesis of hypusine occurs in two consecutive steps. In the first step, deoxyhypusine synthase transfers the 4-aminobutyl moiety to a specific lysine residue in eIF5A, while in the second step of hypusine biosynthesis, deoxyhypusine hydroxylase completes this posttranslational modification by hydroxylation |
713727 |
1.14.99.29 | metabolism |
eukaryotic translation initiation factor 5A, eIF5A, is the only cellular protein that contains the polyamine-modified lysine, hypusine, i.e. N6-(4-amino-2-hydroxybutyl)lysine, which is formed post-translationally by two consecutive enzymatic reactions catalyzed by deoxyhypusine synthase, DHS, and deoxyhypusine hydroxylase, DOHH |
716821 |
1.14.99.29 | metabolism |
hypusine is synthesized exclusively in the eukaryotic translation initiation factor 5A, eIF5A, by two sequential enzymatic steps involving deoxyhypusine synthase, DHS, and deoxyhypusine hydroxylase, DOHH. The polyamine spermidine has an independent and specific function as the source of the 4-aminobutyl portion of hypusine, N6-(4-amino-2-hydroxybutyl)-lysine, in the essential cellular protein eIF5A |
701650 |