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6-N-[(R)-4-amino-2-hydroxybutyl]-L-lysine of human translation initiation factor 5A + electron donor + O2
6-N-(4-aminobutyl)-L-lysine of human translation initiation factor 5A + oxidized electron donor + H2O
6-N-[(R)-4-amino-2-hydroxybutyl]-L-lysine of yeast translation initiation factor 5A + electron donor + O2
6-N-(4-aminobutyl)-L-lysine of yeast translation initiation factor 5A + oxidized electron donor + H2O
eIF5A-N6-(4-aminobutyl)-L-lysine + AH2 + O2
eIF5A-N6-(4-amino-2-hydroxybutyl)-L-lysine + A + H2O
eIF5A-Nepsilon-(4-aminobutyl)lysine + AH2 + O2
eIF5A-Nepsilon-(4-amino-2-hydroxybutyl)lysine + A + H2O
eukaryotic translation initiation factor eIF-5A deoxyhypusine + O2 + AH2
eukaryotic translation initiation factor eIF-5A hypusine + H2O + A
N'-(4-aminobutyl)lysine + electron donor + O2
N'-(4-amino-2-hydroxybutyl)lysine + oxidized electron donor + H2O
[eIF5A]-deoxyhypusine + AH2 + O2
[eIF5A]-hypusine + A + H2O
[eIF5A]-deoxyhypusine + NADH + H+ + O2
[eIF5A]-hypusine + NAD+ + H2O
-
-
-
-
?
additional information
?
-
6-N-[(R)-4-amino-2-hydroxybutyl]-L-lysine of human translation initiation factor 5A + electron donor + O2
6-N-(4-aminobutyl)-L-lysine of human translation initiation factor 5A + oxidized electron donor + H2O
-
-
-
-
?
6-N-[(R)-4-amino-2-hydroxybutyl]-L-lysine of human translation initiation factor 5A + electron donor + O2
6-N-(4-aminobutyl)-L-lysine of human translation initiation factor 5A + oxidized electron donor + H2O
-
strong preference of enzyme for binding the 6-N-(4-amino-2-hydroxybutyl)-L-lysine-containing form of translation initiation factor 5A
-
-
?
6-N-[(R)-4-amino-2-hydroxybutyl]-L-lysine of yeast translation initiation factor 5A + electron donor + O2
6-N-(4-aminobutyl)-L-lysine of yeast translation initiation factor 5A + oxidized electron donor + H2O
-
strong preference of enzyme for binding the 6-N-(4-amino-2-hydroxybutyl)-L-lysine-containing form of translation initiation factor 5A
-
-
?
6-N-[(R)-4-amino-2-hydroxybutyl]-L-lysine of yeast translation initiation factor 5A + electron donor + O2
6-N-(4-aminobutyl)-L-lysine of yeast translation initiation factor 5A + oxidized electron donor + H2O
-
-
-
-
?
eIF5A-N6-(4-aminobutyl)-L-lysine + AH2 + O2
eIF5A-N6-(4-amino-2-hydroxybutyl)-L-lysine + A + H2O
-
-
-
-
?
eIF5A-N6-(4-aminobutyl)-L-lysine + AH2 + O2
eIF5A-N6-(4-amino-2-hydroxybutyl)-L-lysine + A + H2O
-
the unique posttranslational modification occurs in only one cellular protein, the eukaryotic translation initiation factor 5A, eIF5A
-
-
?
eIF5A-N6-(4-aminobutyl)-L-lysine + AH2 + O2
eIF5A-N6-(4-amino-2-hydroxybutyl)-L-lysine + A + H2O
-
-
-
-
?
eIF5A-N6-(4-aminobutyl)-L-lysine + AH2 + O2
eIF5A-N6-(4-amino-2-hydroxybutyl)-L-lysine + A + H2O
-
different eIF5A isozymes exist. The unique posttranslational modification occurs in only one cellular protein, the eukaryotic translation initiation factor 5A, eIF5A
-
-
?
eIF5A-N6-(4-aminobutyl)-L-lysine + AH2 + O2
eIF5A-N6-(4-amino-2-hydroxybutyl)-L-lysine + A + H2O
-
-
-
-
?
eIF5A-N6-(4-aminobutyl)-L-lysine + AH2 + O2
eIF5A-N6-(4-amino-2-hydroxybutyl)-L-lysine + A + H2O
-
the unique posttranslational modification occurs in only one cellular protein, the eukaryotic translation initiation factor 5A, eIF5A
-
-
?
eIF5A-N6-(4-aminobutyl)-L-lysine + AH2 + O2
eIF5A-N6-(4-amino-2-hydroxybutyl)-L-lysine + A + H2O
-
-
-
-
?
eIF5A-N6-(4-aminobutyl)-L-lysine + AH2 + O2
eIF5A-N6-(4-amino-2-hydroxybutyl)-L-lysine + A + H2O
-
-
-
-
ir
eIF5A-N6-(4-aminobutyl)-L-lysine + AH2 + O2
eIF5A-N6-(4-amino-2-hydroxybutyl)-L-lysine + A + H2O
-
different eIF5A isozymes exist. The unique posttranslational modification occurs in only one cellular protein, the eukaryotic translation initiation factor 5A, eIF5A
-
-
?
eIF5A-N6-(4-aminobutyl)-L-lysine + AH2 + O2
eIF5A-N6-(4-amino-2-hydroxybutyl)-L-lysine + A + H2O
-
the DOHH reaction is irreversible
-
-
ir
eIF5A-N6-(4-aminobutyl)-L-lysine + AH2 + O2
eIF5A-N6-(4-amino-2-hydroxybutyl)-L-lysine + A + H2O
-
-
-
-
?
eIF5A-N6-(4-aminobutyl)-L-lysine + AH2 + O2
eIF5A-N6-(4-amino-2-hydroxybutyl)-L-lysine + A + H2O
-
-
-
-
?
eIF5A-N6-(4-aminobutyl)-L-lysine + AH2 + O2
eIF5A-N6-(4-amino-2-hydroxybutyl)-L-lysine + A + H2O
-
-
-
-
?
eIF5A-N6-(4-aminobutyl)-L-lysine + AH2 + O2
eIF5A-N6-(4-amino-2-hydroxybutyl)-L-lysine + A + H2O
-
activation of eIF5A
-
-
?
eIF5A-N6-(4-aminobutyl)-L-lysine + AH2 + O2
eIF5A-N6-(4-amino-2-hydroxybutyl)-L-lysine + A + H2O
-
different eIF5A isozymes exist, no activity with eIF5A mutant K51R, that lacks hypusine. The unique posttranslational modification occurs in only one cellular protein, the eukaryotic translation initiation factor 5A, eIF5A
-
-
?
eIF5A-N6-(4-aminobutyl)-L-lysine + AH2 + O2
eIF5A-N6-(4-amino-2-hydroxybutyl)-L-lysine + A + H2O
-
-
-
-
?
eIF5A-N6-(4-aminobutyl)-L-lysine + AH2 + O2
eIF5A-N6-(4-amino-2-hydroxybutyl)-L-lysine + A + H2O
-
the unique posttranslational modification occurs in only one cellular protein, the eukaryotic translation initiation factor 5A, eIF5A
-
-
?
eIF5A-Nepsilon-(4-aminobutyl)lysine + AH2 + O2
eIF5A-Nepsilon-(4-amino-2-hydroxybutyl)lysine + A + H2O
the enzyme catalyzes the maturation of eukaryotic initiation factor 5A, synthesis of hypusine is essential for the function of eIF5A in eukaryotic cell proliferation and survival
-
-
?
eIF5A-Nepsilon-(4-aminobutyl)lysine + AH2 + O2
eIF5A-Nepsilon-(4-amino-2-hydroxybutyl)lysine + A + H2O
eIF5A is the eukaryotic translation initiation factor 5A
-
-
?
eIF5A-Nepsilon-(4-aminobutyl)lysine + AH2 + O2
eIF5A-Nepsilon-(4-amino-2-hydroxybutyl)lysine + A + H2O
-
the enzyme catalyzes the final step of the post-translational synthesis of hypusine, i.e. Nepsilon-(4-amino-2-hydroxybutyl)lysine, in the eukaryotic translation initiation factor 5A, eIF5A
-
-
?
eIF5A-Nepsilon-(4-aminobutyl)lysine + AH2 + O2
eIF5A-Nepsilon-(4-amino-2-hydroxybutyl)lysine + A + H2O
-
eIF5A is the eukaryotic translation initiation factor 5A, specificity of the interaction between eIF5A and DOHH using the isoform eIF5A-1, DOHH displays a strong preference for binding the deoxyhypusine-containing form of eIF5A, over the eIF5A precursor or the hypusine-containing eIF5A, the deoxyhypusine side chain of the substrate is primarily anchored by gamma-carboxyl groups of Glu57 and Glu208 at the DOHH active site, substrate binding modelling, overview
-
-
?
eukaryotic translation initiation factor eIF-5A deoxyhypusine + O2 + AH2
eukaryotic translation initiation factor eIF-5A hypusine + H2O + A
-
-
-
-
?
eukaryotic translation initiation factor eIF-5A deoxyhypusine + O2 + AH2
eukaryotic translation initiation factor eIF-5A hypusine + H2O + A
-
-
-
-
?
N'-(4-aminobutyl)lysine + electron donor + O2
N'-(4-amino-2-hydroxybutyl)lysine + oxidized electron donor + H2O
-
i.e. deoxyhypusine
i.e. hypusine
?
N'-(4-aminobutyl)lysine + electron donor + O2
N'-(4-amino-2-hydroxybutyl)lysine + oxidized electron donor + H2O
-
i.e. deoxyhypusine
i.e. hypusine
?
N'-(4-aminobutyl)lysine + electron donor + O2
N'-(4-amino-2-hydroxybutyl)lysine + oxidized electron donor + H2O
-
i.e. deoxyhypusine
i.e. hypusine
?
N'-(4-aminobutyl)lysine + electron donor + O2
N'-(4-amino-2-hydroxybutyl)lysine + oxidized electron donor + H2O
-
i.e. deoxyhypusine
i.e. hypusine
?
N'-(4-aminobutyl)lysine + electron donor + O2
N'-(4-amino-2-hydroxybutyl)lysine + oxidized electron donor + H2O
-
i.e. deoxyhypusine
i.e. hypusine
?
N'-(4-aminobutyl)lysine + electron donor + O2
N'-(4-amino-2-hydroxybutyl)lysine + oxidized electron donor + H2O
-
i.e. deoxyhypusine
i.e. hypusine
?
N'-(4-aminobutyl)lysine + electron donor + O2
N'-(4-amino-2-hydroxybutyl)lysine + oxidized electron donor + H2O
-
i.e. deoxyhypusine
i.e. hypusine
?
N'-(4-aminobutyl)lysine + electron donor + O2
N'-(4-amino-2-hydroxybutyl)lysine + oxidized electron donor + H2O
-
i.e. deoxyhypusine
i.e. hypusine
?
N'-(4-aminobutyl)lysine + electron donor + O2
N'-(4-amino-2-hydroxybutyl)lysine + oxidized electron donor + H2O
-
i.e. deoxyhypusine
i.e. hypusine
?
N'-(4-aminobutyl)lysine + electron donor + O2
N'-(4-amino-2-hydroxybutyl)lysine + oxidized electron donor + H2O
-
i.e. deoxyhypusine
i.e. hypusine
?
N'-(4-aminobutyl)lysine + electron donor + O2
N'-(4-amino-2-hydroxybutyl)lysine + oxidized electron donor + H2O
-
i.e. deoxyhypusine
i.e. hypusine
?
N'-(4-aminobutyl)lysine + electron donor + O2
N'-(4-amino-2-hydroxybutyl)lysine + oxidized electron donor + H2O
-
i.e. deoxyhypusine
i.e. hypusine
?
[eIF5A]-deoxyhypusine + AH2 + O2
[eIF5A]-hypusine + A + H2O
-
-
-
?
[eIF5A]-deoxyhypusine + AH2 + O2
[eIF5A]-hypusine + A + H2O
-
-
-
?
[eIF5A]-deoxyhypusine + AH2 + O2
[eIF5A]-hypusine + A + H2O
-
-
-
?
[eIF5A]-deoxyhypusine + AH2 + O2
[eIF5A]-hypusine + A + H2O
-
-
-
-
?
[eIF5A]-deoxyhypusine + AH2 + O2
[eIF5A]-hypusine + A + H2O
-
-
-
?
[eIF5A]-deoxyhypusine + AH2 + O2
[eIF5A]-hypusine + A + H2O
-
-
-
-
?
[eIF5A]-deoxyhypusine + AH2 + O2
[eIF5A]-hypusine + A + H2O
-
-
-
ir
[eIF5A]-deoxyhypusine + AH2 + O2
[eIF5A]-hypusine + A + H2O
-
-
-
-
?
[eIF5A]-deoxyhypusine + AH2 + O2
[eIF5A]-hypusine + A + H2O
-
product analysis by GC/MS and gel filtration
-
?
[eIF5A]-deoxyhypusine + AH2 + O2
[eIF5A]-hypusine + A + H2O
-
product analysis by GC/MS and gel filtration
-
?
additional information
?
-
eIF5A occurs in tumor cells, and it also acts as a cofactor of the Rev transactivator protein in HIV-1-infected cells
-
-
?
additional information
?
-
-
eIF5A occurs in tumor cells, and it also acts as a cofactor of the Rev transactivator protein in HIV-1-infected cells
-
-
?
additional information
?
-
-
DOHH hydroxylates deoxyhypusine and irreversibly completes the hypusination process, the eukaryotic translation initiation factor eIF-5A is the sole known target of hypusination
-
-
?
additional information
?
-
-
substrate specifc bindign of recombinant wild-type and mutant enzymes, overview
-
-
?
additional information
?
-
-
DOHH hydroxylates the deoxyhypusyl-eukaryotic translation initiation factor eIF5A intermediate to hyposine-containing mature eIF5A using molecular oxygen
-
-
?
additional information
?
-
DOHH activity completes hypusine biosynthesis via hydroxylation and thereby completes eukaryotic translation initiation factor eIF-5A formation
-
-
?
additional information
?
-
-
DOHH activity completes hypusine biosynthesis via hydroxylation and thereby completes eukaryotic translation initiation factor eIF-5A formation
-
-
?
additional information
?
-
-
purified DOHH protein displays no phycocyanin lyase activity
-
-
?
additional information
?
-
-
following mutants of human eIF-5A are substrates for DOHH - K47A, K47R, G49A, G52A, K55A, P74A, L91A and L101A
-
-
?
additional information
?
-
-
Lia1 contains HEAT-like repeats with a role for mediating protein-protein interactions
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
eIF5A-N6-(4-aminobutyl)-L-lysine + AH2 + O2
eIF5A-N6-(4-amino-2-hydroxybutyl)-L-lysine + A + H2O
eIF5A-Nepsilon-(4-aminobutyl)lysine + AH2 + O2
eIF5A-Nepsilon-(4-amino-2-hydroxybutyl)lysine + A + H2O
eukaryotic translation initiation factor eIF-5A deoxyhypusine + O2 + AH2
eukaryotic translation initiation factor eIF-5A hypusine + H2O + A
[eIF5A]-deoxyhypusine + AH2 + O2
[eIF5A]-hypusine + A + H2O
[eIF5A]-deoxyhypusine + NADH + H+ + O2
[eIF5A]-hypusine + NAD+ + H2O
-
-
-
-
?
additional information
?
-
eIF5A-N6-(4-aminobutyl)-L-lysine + AH2 + O2
eIF5A-N6-(4-amino-2-hydroxybutyl)-L-lysine + A + H2O
-
-
-
-
?
eIF5A-N6-(4-aminobutyl)-L-lysine + AH2 + O2
eIF5A-N6-(4-amino-2-hydroxybutyl)-L-lysine + A + H2O
-
the unique posttranslational modification occurs in only one cellular protein, the eukaryotic translation initiation factor 5A, eIF5A
-
-
?
eIF5A-N6-(4-aminobutyl)-L-lysine + AH2 + O2
eIF5A-N6-(4-amino-2-hydroxybutyl)-L-lysine + A + H2O
-
different eIF5A isozymes exist. The unique posttranslational modification occurs in only one cellular protein, the eukaryotic translation initiation factor 5A, eIF5A
-
-
?
eIF5A-N6-(4-aminobutyl)-L-lysine + AH2 + O2
eIF5A-N6-(4-amino-2-hydroxybutyl)-L-lysine + A + H2O
-
-
-
-
?
eIF5A-N6-(4-aminobutyl)-L-lysine + AH2 + O2
eIF5A-N6-(4-amino-2-hydroxybutyl)-L-lysine + A + H2O
-
the unique posttranslational modification occurs in only one cellular protein, the eukaryotic translation initiation factor 5A, eIF5A
-
-
?
eIF5A-N6-(4-aminobutyl)-L-lysine + AH2 + O2
eIF5A-N6-(4-amino-2-hydroxybutyl)-L-lysine + A + H2O
-
-
-
-
?
eIF5A-N6-(4-aminobutyl)-L-lysine + AH2 + O2
eIF5A-N6-(4-amino-2-hydroxybutyl)-L-lysine + A + H2O
-
different eIF5A isozymes exist. The unique posttranslational modification occurs in only one cellular protein, the eukaryotic translation initiation factor 5A, eIF5A
-
-
?
eIF5A-N6-(4-aminobutyl)-L-lysine + AH2 + O2
eIF5A-N6-(4-amino-2-hydroxybutyl)-L-lysine + A + H2O
-
the DOHH reaction is irreversible
-
-
ir
eIF5A-N6-(4-aminobutyl)-L-lysine + AH2 + O2
eIF5A-N6-(4-amino-2-hydroxybutyl)-L-lysine + A + H2O
-
-
-
-
?
eIF5A-N6-(4-aminobutyl)-L-lysine + AH2 + O2
eIF5A-N6-(4-amino-2-hydroxybutyl)-L-lysine + A + H2O
-
-
-
-
?
eIF5A-N6-(4-aminobutyl)-L-lysine + AH2 + O2
eIF5A-N6-(4-amino-2-hydroxybutyl)-L-lysine + A + H2O
-
-
-
-
?
eIF5A-N6-(4-aminobutyl)-L-lysine + AH2 + O2
eIF5A-N6-(4-amino-2-hydroxybutyl)-L-lysine + A + H2O
-
activation of eIF5A
-
-
?
eIF5A-N6-(4-aminobutyl)-L-lysine + AH2 + O2
eIF5A-N6-(4-amino-2-hydroxybutyl)-L-lysine + A + H2O
-
different eIF5A isozymes exist, no activity with eIF5A mutant K51R, that lacks hypusine. The unique posttranslational modification occurs in only one cellular protein, the eukaryotic translation initiation factor 5A, eIF5A
-
-
?
eIF5A-N6-(4-aminobutyl)-L-lysine + AH2 + O2
eIF5A-N6-(4-amino-2-hydroxybutyl)-L-lysine + A + H2O
-
-
-
-
?
eIF5A-N6-(4-aminobutyl)-L-lysine + AH2 + O2
eIF5A-N6-(4-amino-2-hydroxybutyl)-L-lysine + A + H2O
-
the unique posttranslational modification occurs in only one cellular protein, the eukaryotic translation initiation factor 5A, eIF5A
-
-
?
eIF5A-Nepsilon-(4-aminobutyl)lysine + AH2 + O2
eIF5A-Nepsilon-(4-amino-2-hydroxybutyl)lysine + A + H2O
the enzyme catalyzes the maturation of eukaryotic initiation factor 5A, synthesis of hypusine is essential for the function of eIF5A in eukaryotic cell proliferation and survival
-
-
?
eIF5A-Nepsilon-(4-aminobutyl)lysine + AH2 + O2
eIF5A-Nepsilon-(4-amino-2-hydroxybutyl)lysine + A + H2O
-
the enzyme catalyzes the final step of the post-translational synthesis of hypusine, i.e. Nepsilon-(4-amino-2-hydroxybutyl)lysine, in the eukaryotic translation initiation factor 5A, eIF5A
-
-
?
eukaryotic translation initiation factor eIF-5A deoxyhypusine + O2 + AH2
eukaryotic translation initiation factor eIF-5A hypusine + H2O + A
-
-
-
-
?
eukaryotic translation initiation factor eIF-5A deoxyhypusine + O2 + AH2
eukaryotic translation initiation factor eIF-5A hypusine + H2O + A
-
-
-
-
?
[eIF5A]-deoxyhypusine + AH2 + O2
[eIF5A]-hypusine + A + H2O
-
-
-
?
[eIF5A]-deoxyhypusine + AH2 + O2
[eIF5A]-hypusine + A + H2O
-
-
-
?
[eIF5A]-deoxyhypusine + AH2 + O2
[eIF5A]-hypusine + A + H2O
-
-
-
?
[eIF5A]-deoxyhypusine + AH2 + O2
[eIF5A]-hypusine + A + H2O
-
-
-
-
?
[eIF5A]-deoxyhypusine + AH2 + O2
[eIF5A]-hypusine + A + H2O
-
-
-
?
[eIF5A]-deoxyhypusine + AH2 + O2
[eIF5A]-hypusine + A + H2O
-
-
-
-
?
[eIF5A]-deoxyhypusine + AH2 + O2
[eIF5A]-hypusine + A + H2O
-
-
-
ir
[eIF5A]-deoxyhypusine + AH2 + O2
[eIF5A]-hypusine + A + H2O
-
-
-
-
?
[eIF5A]-deoxyhypusine + AH2 + O2
[eIF5A]-hypusine + A + H2O
-
-
-
?
[eIF5A]-deoxyhypusine + AH2 + O2
[eIF5A]-hypusine + A + H2O
-
-
-
?
additional information
?
-
eIF5A occurs in tumor cells, and it also acts as a cofactor of the Rev transactivator protein in HIV-1-infected cells
-
-
?
additional information
?
-
-
eIF5A occurs in tumor cells, and it also acts as a cofactor of the Rev transactivator protein in HIV-1-infected cells
-
-
?
additional information
?
-
-
DOHH hydroxylates deoxyhypusine and irreversibly completes the hypusination process, the eukaryotic translation initiation factor eIF-5A is the sole known target of hypusination
-
-
?
additional information
?
-
-
DOHH hydroxylates the deoxyhypusyl-eukaryotic translation initiation factor eIF5A intermediate to hyposine-containing mature eIF5A using molecular oxygen
-
-
?
additional information
?
-
DOHH activity completes hypusine biosynthesis via hydroxylation and thereby completes eukaryotic translation initiation factor eIF-5A formation
-
-
?
additional information
?
-
-
DOHH activity completes hypusine biosynthesis via hydroxylation and thereby completes eukaryotic translation initiation factor eIF-5A formation
-
-
?
additional information
?
-
-
following mutants of human eIF-5A are substrates for DOHH - K47A, K47R, G49A, G52A, K55A, P74A, L91A and L101A
-
-
?
additional information
?
-
-
Lia1 contains HEAT-like repeats with a role for mediating protein-protein interactions
-
-
?
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.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
1,10-Diaminodecane
-
94% of initial activity at 2 mM
1,10-phenanthroline
-
complete inhibition at 0.01 mM
1,3-diaminopropane
-
86% of initial activity at 0.5 mM
1,6-diaminohexane
-
97% of initial activity at 2 mM
1,7-Diaminoheptane
-
91% of initial activity at 2 mM
1,8-diaminooctane
-
93% of initial activity at 2 mM
2,3-Dihydroxybenzoic acid
-
slight inhibition at 2 mM
2-(2-hydroxy-5-methylphenyl)-1,3-thiazole-4-carboxylic acid
-
inhibition in vitro and in cells
2-(2-hydroxy-5-methylphenyl)-4,5-dihydro-1,3-thiazole-4-carboxylic acid
2-(4-methoxyphenyl)-6-[[2-(4-methoxyphenyl)-3H-benzimidazol-5-yl]methyl]-1H-benzimidazole
-
94.1% inhibition at 0.002 mM
3,4-dihydroxybenzoic acid
-
above 50% inhibition at 2 mM
4,6-diphenyl-1-hydroxy-pyridine-2-one
-
IC50 0.0007 mM
alkyl 4-oxo-piperidine 3 carboxylates
-
structurally related to dihydropyrimidines, most potent, putative DOHH inhibitors in vitro
CaCl2
-
98% of initial activity at 0.005 mM
cadaverine
-
87% of initial activity at 0.5 mM
caldine
-
47% of initial activity at 0.5 mM
deferoxamine
-
targets the active metalloenzyme and inhibits DOHH in human vascular endothelial cells
desferrioxamine B
-
IC50 0.016 mM
desferrioxamine mesylate
-
-
ethyl 3,4-dihydroxybenzoate
-
IC50 0.5 mM
FeCl3
-
65% of initial activity at 0.005 mM
FeSO4
-
13% of initial activity at 0.005 mM
Lys-Thr-Gly-deoxyhypusine-His-Gly-His-Ala-Lys
-
competitive inhibition
methyl 2,3-dihydroxybenzoate
-
IC50 1.6 mM
metipirox
-
IC50 0.0028 mM
Mn(C2H3O2)2
-
above 0.001 mM
MnCl2
-
64% of initial activity at 0.005 mM
N''-guanyl-1,7-diaminoheptane
-
competitive inhibition
N-(2-cyanoethyl)butane-1,4-diamine
-
80% of initial activity at 2 mM
N-(3-cyanopropyl)propane-1,3-diamine
-
79% of initial activity at 2 mM
N-phenyl-1-[1-(phenylmethyl)benzimidazol-2-yl]diazenylnaphthalen-2-amine
-
87.6% inhibition at 0.002 mM
N-[4-(3,4-diethoxyphenyl)-1,2,5-oxadiazole-3-yl]-3-methylbenzamide
-
92.6% inhibition at 0.002 mM
N1-acetyl-L-Orn-L-Pro-Gly
-
above 2 mM
N1-acetyl-N4-(2,3-dihydroxybenzoyl)-L-Orn-L-Pro-Gly
-
IC50 0.2 mM
N1-acetyl-N4-(3,4-dihydroxybenzoyl)-L-Orn-L-Pro-Gly
-
IC50 0.03 mM
Ni(C2H3O2)2
-
above 0.001 mM
NiSO4
-
72% of initial activity at 0.005 mM
putrescine
-
85% of initial activity at 0.5 mM
pyridine 2,3-dicarboxylate
Pyridine 2,4-dicarboxylate
Pyridine 2,5-dicarboxylate
Pyridine 3,4-dicarboxylate
Pyridine 3,5-dicarboxylate
spermidine
-
58% of initial activity at 0.5 mM
spermine
-
41% of initial activity at 0.5 mM
thermine
-
35% of initial activity at 0.5 mM
Zn(C2H3O2)2
-
above 0.01 mM
ZnCl2
-
93% of initial activity at 0.005 mM
2,2'-dipyridyl
-
-
2,2'-dipyridyl
-
IC50 0.026 mM
2,2'-dipyridyl
-
IC50 0.029 mM
2,2'-dipyridyl
-
targets the active metalloenzyme and inhibits DOHH in human vascular endothelial cells
2-(2-hydroxy-5-methylphenyl)-4,5-dihydro-1,3-thiazole-4-carboxylic acid
-
inhibition in vitro and in cells
2-(2-hydroxy-5-methylphenyl)-4,5-dihydro-1,3-thiazole-4-carboxylic acid
-
inhibition in vitro and in cells
ciclopirox
-
IC50 0.005 mM, complete inhibition above 0.01 mM
ciclopirox
-
IC50 0.0006 mM
ciclopirox
-
CPX, topical fungicide
ciclopirox
-
targets the active metalloenzyme and inhibits DOHH in human vascular endothelial cells
Co(C2H3O2)2
-
above 0.01 mM
Co(C2H3O2)2
-
94% of initial activity at 0.005 mM
deferiprone
-
IC50 0.117 mM
deferiprone
-
0.2 mM in cells
deferiprone
-
DEF, systemic medicinal iron chelator
deferiprone
-
targets the active metalloenzyme and inhibits DOHH in human vascular endothelial cells
EDTA
-
IC50 0.0003 mM
EDTA
-
high ionic strength EDTA, Tris concentrations above 30 mM
mimosine
-
reversible inhibition
mimosine
-
S-isomer, complete inhibition at 0.2 mM in LAZ463 cells
mimosine
-
IC50 0.0033 mM
mimosine
-
0.2 mM in cells
mimosine
-
inhibition of enzyme resulting in reduction of steady-state level of transcription initiation factor eIF5A. Effect does not appear to be involved in the modulation of differentiation-related gene 1 expression by mimosine
mimosine
-
targets the active metalloenzyme and inhibits DOHH in human vascular endothelial cells
mimosine
synergistic growth inhibition with the combination of miR-331-3p and miR-642-5p and mimosine
mimosine
-
inhibits progression of cells from the G1 to S-phase by DOHH inhibition. DOHH reactivation occurs rapidly after inhibitor withdrawal and correlates with synchronized entry into the S-phase. Toxic in vivo
Picolinic acid
-
-
pyridine 2,3-dicarboxylate
-
-
pyridine 2,3-dicarboxylate
-
inhibitory effect of pyridine depends on the carboxyl group position
Pyridine 2,4-dicarboxylate
-
-
Pyridine 2,4-dicarboxylate
-
inhibitory effect of pyridine depends on the carboxyl group position
Pyridine 2,5-dicarboxylate
-
-
Pyridine 2,5-dicarboxylate
-
inhibitory effect of pyridine depends on the carboxyl group position
Pyridine 3,4-dicarboxylate
-
-
Pyridine 3,4-dicarboxylate
-
inhibitory effect of pyridine depends on the carboxyl group position
Pyridine 3,5-dicarboxylate
-
-
Pyridine 3,5-dicarboxylate
-
inhibitory effect of pyridine depends on the carboxyl group position
zileuton
-
i.e. N-[1-(1-benzothien-2-yl)ethyl]-N-hydroxyurea
additional information
-
a number of metal-chelating inhibitors of DOHH causes growth inhibition and G1 cell cycle arrest in mammalian cells
-
additional information
-
no inhibition by S-isomers of kojic acid, 3-pyridylalanine, 4-pyridylalanine at 0.3 mM in vitro and at 0.2 mM in cells, no inhibition by 2-(2-aminophenyl)-1,3-thiazole-4-carboxylic acid at 0.4 mM in cells
-
additional information
-
partial reconstitution of chelator inhibited activity with CuCl2 or Zn(C2H3O2)2
-
additional information
-
a number of metal-chelating inhibitors of DOHH causes growth inhibition and G1 cell cycle arrest in mammalian cells
-
additional information
-
design of inhibitors against the human parasite enzyme from Plasmodium falciparum might profit from structural differences and the five HEAT-like repeats present in the parasite DOHH that differ in number and amino acid identity from its human orthologue, which contains four repeats
-
additional information
-
design of inhibitors against the parasite enzyme might profit from structural differences and the five HEAT-like repeats present in the parasite DOHH that differ in number and amino acid identity from its human orthologue, which contains four repeats. Compounds related structurally to dihydropyrimidines, like the plant amino acid mimosine and the antifungal drug ciclopiroxolamine, are toxic and/or not effective in vivo as anti-malarial drugs in rodents
-
additional information
-
no inhibition by CuSO4, HgCl2, MgCl2, CdSO4 at 0.005 mM; partial reconstitution of 0.01 mM 1,10-phenanthroline inhibited activity with Co(C2H3O2)2 at 0.03 mM or FeSO4 at 0.005 mM
-
additional information
-
no inhibition by 2-oxoglutarate, 2-oxoadipinate, 2-oxosuccinate, 3-oxoglutarate, glutarate, malonate, pyruvate
-
additional information
-
no inhibition at 2 mM N-(2-cyanopropyl)-3-cyanopropylamine
-
additional information
-
partial reconstitution of 0.01 mM 1,10-phenanthroline inhibited activity with Co(C2H3O2)2 at 0.03 mM or FeSO4 at 0.005 mM
-
additional information
-
the active site is blocked by two catecholpeptides containing alpha 3,4-dihydroxybenzoyl- and alpha 2,3-dihydroxybenzoyl moiety. The 3,4-dihydroxybenzoyl-containing compound is more potent with a Ki of 32 mM
-
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evolution
-
hypusine occurs only in eukaryotes and certain archaea, but not in eubacteria
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
evolution
-
the deoxyhypusine/hypusine synthetic pathway has evolved in archaea and eukaryotes, evolution of eIF5A and the hypusine pathway, overview
evolution
-
the deoxyhypusine/hypusine synthetic pathway has evolved in archaea and eukaryotes, evolution of eIF5A and the hypusine pathway, overview
evolution
-
the deoxyhypusine/hypusine synthetic pathway has evolved in archaea and eukaryotes, evolution of eIF5A and the hypusine pathway, overview
evolution
-
the deoxyhypusine/hypusine synthetic pathway has evolved in archaea and eukaryotes, evolution of eIF5A and the hypusine pathway, overview
evolution
-
the deoxyhypusine/hypusine synthetic pathway has evolved in archaea and eukaryotes, evolution of eIF5A and the hypusine pathway, overview
evolution
-
the deoxyhypusine/hypusine synthetic pathway has evolved in archaea and eukaryotes, evolution of eIF5A and the hypusine pathway, overview
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
malfunction
-
a mutation in the dohh gene causes defects in mitochondrial morphology, distribution and displayed synthetic defects in growth
malfunction
-
inactivation of DOHH is recessively lethal
malfunction
-
inactivation of DOHH is recessively lethal, phenotypes resulting from depletion of DOHH and hypusine-modified eIF5A, overview
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
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
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
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
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
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
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
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
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
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
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
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
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
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
metabolism
-
the unique amino acid hypusine is formed exclusively in eIF5A by the successive action of deoxyhypusine synthase and deoxyhypusine hydroxylase
physiological function
-
deoxyhypusine hydroxylase catalyze post-translational hypusination of eIF5A protein, that plays an important role in human hepatocellular carcinoma tumorigenesis and metastasis
physiological function
-
deoxyhypusine hydroxylase completes the modification of eukaryotic initiation factor 5A, eIF5A, through hydroxylation. Hypusination in eIF5A is a unique posttranslational modification. Hypusine-containing eIF5A promotes translation elongation
physiological function
-
deoxyhypusine hydroxylase completes the modification of eukaryotic initiation factor 5A, eIF5A, through hydroxylation. Hypusination in eIF5A is a unique posttranslational modification. Hypusine-containing eIF5A promotes translation elongation
physiological function
-
deoxyhypusine hydroxylase completes the modification of eukaryotic initiation factor 5A, eIF5A, through hydroxylation. Hypusination in eIF5A is a unique posttranslational modification. Hypusine-containing eIF5A promotes translation elongation
physiological function
-
deoxyhypusine hydroxylase completes the modification of eukaryotic initiation factor 5A, eIF5A, through hydroxylation. Hypusination in eIF5A is a unique posttranslational modification. Hypusine-containing eIF5A promotes translation elongation
physiological function
-
deoxyhypusine hydroxylase completes the modification of eukaryotic initiation factor 5A, eIF5A, through hydroxylation. Hypusination in eIF5A is a unique posttranslational modification. Hypusine-containing eIF5A promotes translation elongation. Deoxyhypusinated eIF5A intermediate can fulfill the function of the hypusinated eIF5A in yeast
physiological function
-
deoxyhypusine hydroxylase completes the modification of eukaryotic initiation factor 5A, eIF5A, through hydroxylation. Hypusination in eIF5A is a unique posttranslational modification. Hypusine-containing eIF5A promotes translation elongation. The homologous dohh gene and its target eIF5A are required for cell growth and the regulation of autophagy. The Nero protein regulates eIF5A activity, eIF5A is upregulated in nero mutants
physiological function
-
DOHH is required for the alignment of mitochondria along microtubules. Deoxyhypusine hydroxylase completes the modification of eukaryotic initiation factor 5A, eIF5A, through hydroxylation. Hypusination in eIF5A is a unique posttranslational modification. Hypusine-containing eIF5A promotes translation elongation
physiological function
-
Hypusine modification is essential for the activity of eIF5A and for eukaryotic cell proliferation. eIF5A binds to the ribosome and stimulates translation in a hypusine-dependent manner
physiological function
-
requirement for eIF5A and for the hypusine modification enzymes in cell viability and growth
physiological function
-
requirement for eIF5A and for the hypusine modification enzymes in cell viability and growth
physiological function
-
requirement for eIF5A and for the hypusine modification enzymes in cell viability and growth, but DOHH is not an essential gene in yeast, as a DOHH null strain is viable and grows at a rate slightly slower than the wild-type strain. Even though endogenous yeast eIF5A mostly exists as the fully modified hypusine form. EIF5A binds only to translating ribosomes and in a hypusine-dependent manner playing a a direct role in translation elongation, overview
physiological function
-
requirement for eIF5A and for the hypusine modification enzymes in cell viability and growth. Role for DOHH, or eIF5A, in micro-tubule assembly and mitochondrial function
physiological function
-
requirement for eIF5A and for the hypusine modification enzymes in cell viability and growth. The DOHH gene is essential
physiological function
-
requirement for eIF5A and for the hypusine modification enzymes in cell viability and growth. The DOHH gene is essential
physiological function
-
the enzyme activates eIF5A, that plays a role in the elongation step of translation
physiological function
deoxyhypusine hydroxylase completes hypusine biosynthesis in eukaryotic initiation factor (eIF-5A) which is the only cellular protein known to contain the unusual amino acid hypusine. Modified EIF-5A is important for proliferation of the malaria parasite
physiological function
the enzyme catalyzes the activation of eukaryotic translation initiation factor, eIF5A, a protein essential for cell growth. Expression of DOHH is regulated by micro-RNAs miR-331-3p and miR-642-5p in prostate cancer cells, overview. Transient overexpression of miR-331-3p and/or miR-642-5p in DU-145 prostate cancer cells reduces DOHH mRNA and protein expression and inhibits cell proliferation
physiological function
an enzyme-overexpressing mutant has low virulence towards maize
physiological function
the cellular concentration of the enzyme and its enzymatic activity play a role in HIV-1, HTLV-1 and MMTV IRES-mediated translation initiation
physiological function
-
deoxyhypusine hydroxylase completes hypusine biosynthesis in eukaryotic initiation factor (eIF-5A) which is the only cellular protein known to contain the unusual amino acid hypusine. Modified EIF-5A is important for proliferation of the malaria parasite
-
additional information
-
antiretroviral effects of alpha-hydroxypyridones (i.e. mimosine and deferiprone) on HIV-1 multiplication in T-lymphocytic and promonocytic cell lines through deoxyhypusine hydroxylase inhibition
additional information
-
eIF5A is a prognostic factor for human hepatocellular carcinoma patients
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E57G
site-directed mutagenesis, the substitution located at one of the four conserved His-Glu pairs, the potential metal coordination sites, results in severe reduction of deoxyhypusine hydroxylase activity compared to the wild-type enzyme
E208N
-
site-directed mutagenesis, the mutant shows severely impairment in eIF5A(deoxyhypusine) binding
E208Q
-
site-directed mutagenesis, the mutant shows severely impairment in eIF5A(deoxyhypusine) binding
E57N
-
site-directed mutagenesis, the mutant shows severely impairment in eIF5A(deoxyhypusine) binding
E57Q
-
site-directed mutagenesis, the mutant shows severely impairment in eIF5A(deoxyhypusine) binding
E93A
-
site-directed mutagenesis, the mutant shows reduced eIF5A(deoxyhypusine) binding
G247A
-
site-directed mutagenesis, the mutant shows 50-80% reduced activity compared to the wild-type enzyme, but is capable of binding both iron and substrate
M237A
-
site-directed mutagenesis, the mutant shows reduced, but existing eIF5A(deoxyhypusine) and iron binding, but is catalytically inactive
Q215
-
site-directed mutagenesis, the mutant shows 50-80% reduced activity compared to the wild-type enzyme, but is capable of binding both iron and substrate
R183a
-
site-directed mutagenesis, the mutant shows 50-80% reduced activity compared to the wild-type enzyme, but is capable of binding both iron and substrate
R26A
-
site-directed mutagenesis, the mutant shows 50-80% reduced activity compared to the wild-type enzyme, but is capable of binding both iron and substrate
R88A
-
site-directed mutagenesis, the mutant shows 50-80% reduced activity compared to the wild-type enzyme, but is capable of binding both iron and substrate
S202A
-
site-directed mutagenesis, the mutant shows 50-80% reduced activity compared to the wild-type enzyme, but is capable of binding both iron and substrate
E113A
-
site-directed mutagenesis, the mutant is completely inactive in deoxyhypusine hydroxylation, structure comparison to the wild-type enzyme
E116A
-
site-directed mutagenesis, the mutant is completely inactive in deoxyhypusine hydroxylation, structure comparison to the wild-type enzyme
E116D
-
site-directed mutagenesis, the mutant is completely inactive in deoxyhypusine hydroxylation, structure comparison to the wild-type enzyme
E238A
-
site-directed mutagenesis, the mutant is completely inactive in deoxyhypusine hydroxylation, structure comparison to the wild-type enzyme
E271A
-
site-directed mutagenesis, the mutant is completely inactive in deoxyhypusine hydroxylation, structure comparison to the wild-type enzyme
E80A
-
site-directed mutagenesis, the mutant is completely inactive in deoxyhypusine hydroxylation, structure comparison to the wild-type enzyme
H112A
-
site-directed mutagenesis, the mutant is completely inactive in deoxyhypusine hydroxylation, structure comparison to the wild-type enzyme
H237A
-
site-directed mutagenesis, the mutant is completely inactive in deoxyhypusine hydroxylation, structure comparison to the wild-type enzyme
H270A
-
site-directed mutagenesis, the mutant is completely inactive in deoxyhypusine hydroxylation, structure comparison to the wild-type enzyme
H79A
-
site-directed mutagenesis, the mutant is completely inactive in deoxyhypusine hydroxylation, structure comparison to the wild-type enzyme
E66K
-
mutation E66K in the DOHH homologue gene, Mmd1, causes a temperature-sensitive growth phenotype and altered mitochondrial morphology and distribution
E208A
-
little reduction in iron content of enzyme, complete loss of activity
E208A
-
severe impairment in binding of substrate translation initiation factor 5A, complete loss of activity
E208A
-
site-directed mutagenesis, the mutant shows severely impairment in eIF5A(deoxyhypusine) binding
E208D
-
impairment in binding of substrate translation initiation factor 5A, retains some activity
E208D
-
site-directed mutagenesis, the mutant shows reduced but not fully abolished eIF5A(deoxyhypusine) binding
E241A
-
severe impairment in binding of substrate translation initiation factor 5A
E241A
-
severe reduction in iron content of enzyme, complete loss of activity
E241A
-
site-directed mutagenesis, the mutant shows severely impairment in eIF5A(deoxyhypusine) binding
E57A
-
little reduction in iron content of enzyme, complete loss of activity
E57A
-
severe impairment in binding of substrate translation initiation factor 5A, complete loss of activity
E57A
-
site-directed mutagenesis, the mutant shows severely impairment in eIF5A(deoxyhypusine) binding
E57D
-
impairment in binding of substrate translation initiation factor 5A, retains some activity
E57D
-
site-directed mutagenesis, the mutant shows reduced but not fully abolished eIF5A(deoxyhypusine) binding
E90A
-
severe impairment in binding of substrate translation initiation factor 5A
E90A
-
severe reduction in iron content of enzyme, complete loss of activity
E90A
-
site-directed mutagenesis, the mutant shows severely impairment in eIF5A(deoxyhypusine) and iron binding
G214A
-
severe impairment in binding of substrate translation initiation factor 5A
G214A
-
site-directed mutagenesis, the mutant shows reduced eIF5A(deoxyhypusine) but unaltered iron binding
G63A
-
severe impairment in binding of substrate translation initiation factor 5A
G63A
-
site-directed mutagenesis, the mutant shows reduced eIF5A(deoxyhypusine), but unaltered iron binding
H207A
-
severe reduction in iron content of enzyme, complete loss of activity
H207A
-
site-directed mutagenesis, the mutant is defective in iron binding
H240A
-
severe reduction in iron content of enzyme, complete loss of activity
H240A
-
site-directed mutagenesis, the mutant is defective in iron binding
H56A
-
severe reduction in iron content of enzyme, complete loss of activity
H56A
-
site-directed mutagenesis, the mutant is defective in iron binding
H89A
-
severe reduction in iron content of enzyme, complete loss of activity
H89A
-
site-directed mutagenesis, the mutant is defective in iron binding
additional information
a deletion at the HEAT-repeats 1-3, potential metal coordination sites, results in complete losses of deoxyhypusine hydroxylase activity, the different clones encoding the enzyme show differing activity, overview
additional information
-
a deletion at the HEAT-repeats 1-3, potential metal coordination sites, results in complete losses of deoxyhypusine hydroxylase activity, the different clones encoding the enzyme show differing activity, overview
additional information
-
construction of a polycistronic vector encoding eIF5A, DHS and DOHH, overview
additional information
-
enzyme deletion mutant grows similar to wild-type in rich and minimal medium despite lack of 6-N-[(R)-4-amino-2-hydroxybutyl]-L-lysine
additional information
-
single copy gene dohh inactivation of deoxyhypusine hydroxylase
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Abbruzzese, A.; Park, M.H.; Folk J.E.
Deoxyhypusine hydroxylase from rat testis. Partial purification and characterization
J. Biol. Chem.
261
3085-3089
1986
Rattus norvegicus
brenda
Park, M.H.; Cooper, H.L.; Folk, J.E.
The biosynthesis of protein-bound hypusine (N epsilon-(4-amino-2-hydroxybutyl)lysine). Lysine as the amino acid precursor and the intermediate role of deoxyhypusine (N epsilon-(4-aminobutyl)lysine)
J. Biol. Chem.
257
7217-7222
1982
Cricetulus griseus
brenda
Clement, P.M.J.; Hanauske-Abel, H.M.; Wolff, E.C.; Kleinman, H.K.; Park, M.H.
The antifungal drug ciclopirox inhibits deoxyhypusine and proline hydroxylation, endothelial cell growth and angiogenesis in vitro
Int. J. Cancer
100
491-498
2002
Homo sapiens
brenda
Beninati, S.; Ferraro, G.; Abbruzzese, A.
Catalytic properties of deoxyhypusine hydroxylase
Ital. J. Biochem.
39
183A-185A
1990
Rattus norvegicus
brenda
Hanauske-Abel, H.M.; Park, M.H.; Hanauske, A.R.; Popowicz, A.M.; Lalande, M.; Folk, J.E.
Inhibition of the G1-S transition of the cell cycle by inhibitors of deoxyhypusine hydroxylation
Biochim. Biophys. Acta
1221
115-124
1994
Cricetulus griseus, Homo sapiens
brenda
Csonga, R.; Ettmayer, P.; Auer, M.; Eckerskorn, C.; Eder, J.; Klier, H.
Evaluation of the metal ion requirement of the human deoxyhypusine hydroxylase from HeLa cells using a novel enzyme assay
FEBS Lett.
380
209-214
1996
Homo sapiens
brenda
Abbruzzese, A.; Hanauske-Abel, H.M.; Park, M.H.; Henke, S.; Folk, J.E.
The active site of deoxyhypusyl hydroxylase: use of catecholpeptides and their component chelator and peptide moieties as molecular probes
Biochim. Biophys. Acta
1077
159-166
1991
Rattus norvegicus
brenda
Andrus, L.; Szabo, P.; Grady, R.W.; Hanauske, A.R.; Huima-Byron, T.; Slowinska, B.; Zagulska, S.; Hanauske-Abel, H.M.
Antiretroviral effects of deoxyhypusyl hydroxylase inhibitors. A hypusine-dependent host cell mechanism for replication of human immunodeficiency virus type 1 (HIV-1)
Biochem. Pharmacol.
55
1807-1818
1998
Homo sapiens
brenda
Abbruzzese, A.; Park, M.H.; Beninati, S.; Folk, J.E.
Inhibition of deoxyhypusine hydroxylase by polyamines and by a deoxyhypusine peptide
Biochim. Biophys. Acta
997
248-255
1989
Cricetulus griseus, Rattus norvegicus
brenda
Abbruzzese, A.; Liguori, V.; Park, M.H.
Deoxyhypusine hydroxylase
Adv. Exp. Med. Biol.
250
459-466
1988
Rattus norvegicus
brenda
Kim, Y.S.; Kang, K.R.; Wolff, E.C.; Bell, J.K.; McPhie, P.; Park, M.H.
Deoxyhypusine hydroxylase is an Fe(II)-dependent, HEAT-repeat enzyme. Identification of amino acid residues critical for Fe(II) binding and catalysis
J. Biol. Chem.
281
13217-13225
2006
Homo sapiens
brenda
Kang, K.R.; Kim, Y.S.; Wolff, E.C.; Park, M.H.
Specificity of the deoxyhypusine hydroxylase-eukaryotic translation initiation factor (eIF5A) interaction: identification of amino acid residues of the enzyme required for binding of its substrate, deoxyhypusine-containing eIF5A
J. Biol. Chem.
282
8300-8308
2007
Homo sapiens
brenda
Dong, Z.; Arnold, R.J.; Yang, Y.; Park, M.H.; Hrncirova, P.; Mechref, Y.; Novotny, M.V.; Zhang, J.T.
Modulation of differentiation-related gene 1 expression by cell cycle blocker mimosine, revealed by proteomic analysis
Mol. Cell. Proteomics
4
993-1001
2005
Homo sapiens
brenda
Park, J.H.; Aravind, L.; Wolff, E.C.; Kaevel, J.; Kim, Y.S.; Park, M.H.
Molecular cloning, expression, and structural prediction of deoxyhypusine hydroxylase: a HEAT-repeat-containing metalloenzyme
Proc. Natl. Acad. Sci. USA
103
51-56
2006
Homo sapiens, Saccharomyces cerevisiae
brenda
Cano, V.S.; Jeon, G.A.; Johansson, H.E.; Henderson, C.A.; Park, J.H.; Valentini, S.R.; Hershey, J.W.; Park, M.H.
Mutational analyses of human eIF5A-1--identification of amino acid residues critical for eIF5A activity and hypusine modification
FEBS J.
275
44-58
2008
Saccharomyces cerevisiae, Homo sapiens
brenda
Huang, J.K.; Cui, Y.; Chen, C.H.; Clampitt, D.; Lin, C.T.; Wen, L.
Molecular cloning and functional expression of bovine deoxyhypusine hydroxylase cDNA and homologs
Protein Expr. Purif.
54
126-133
2007
Bos taurus (Q0VC53), Bos taurus
brenda
Frommholz, D.; Kusch, P.; Blavid, R.; Scheer, H.; Tu, J.M.; Marcus, K.; Zhao, K.H.; Atemnkeng, V.; Marciniak, J.; Kaiser, A.E.
Completing the hypusine pathway in Plasmodium
FEBS J.
276
5881-5891
2009
Plasmodium falciparum (C9QNK6), Plasmodium falciparum
brenda
Patel, P.H.; Costa-Mattioli, M.; Schulze, K.L.; Bellen, H.J.
The Drosophila deoxyhypusine hydroxylase homologue nero and its target eIF5A are required for cell growth and the regulation of autophagy
J. Cell Biol.
185
1181-1194
2009
Drosophila melanogaster
brenda
Vu, V.V.; Emerson, J.P.; Martinho, M.; Kim, Y.S.; Muenck, E.; Park, M.H.; Que, L.
Human deoxyhypusine hydroxylase, an enzyme involved in regulating cell growth, activates O2 with a nonheme diiron center
Proc. Natl. Acad. Sci. USA
106
14814-14819
2009
Homo sapiens
brenda
Hoque, M.; Hanauske-Abel, H.M.; Palumbo, P.; Saxena, D.; DAlliessi Gandolfi, D.; Park, M.H.; Peery, T.; Mathews, M.B.
Inhibition of HIV-1 gene expression by Ciclopirox and Deferiprone, drugs that prevent hypusination of eukaryotic initiation factor 5A
Retrovirology
6
90
2009
Homo sapiens
brenda
Park, M.H.; Nishimura, K.; Zanelli, C.F.; Valentini, S.R.
Functional significance of eIF5A and its hypusine modification in eukaryotes
Amino Acids
38
491-500
2010
Bos taurus, Saccharomyces cerevisiae, Caenorhabditis elegans, Drosophila melanogaster, Homo sapiens, Schizosaccharomyces pombe
brenda
Kerscher, B.; Nzukou, E.; Kaiser, A.
Assessment of deoxyhypusine hydroxylase as a putative, novel drug target
Amino Acids
38
471-477
2010
Bos taurus, Saccharomyces cerevisiae, Drosophila melanogaster, Homo sapiens, Plasmodium falciparum, Rattus norvegicus, Schizosaccharomyces pombe
brenda
Cano, V.; Medrano, F.; Park, M.; Valentini, S.
Evidence for conformational changes in the yeast deoxyhypusine hydroxylase Lia1 upon iron displacement from its active site
Amino Acids
38
479-490
2010
Saccharomyces cerevisiae
brenda
Lee, N.; Tsang, F.; Shek, F.; Mao, M.; Dai, H.; Zhang, C.; Dong, S.; Guan, X.; Poon, R.; Luk, J.
Prognostic significance and therapeutic potential of eukaryotic translation initiation factor 5A (eIF5A) in hepatocellular carcinoma
Int. J. Cancer
127
968-976
2010
Homo sapiens
brenda
Park, J.; Dias, C.; Lee, S.; Valentini, S.; Sokabe, M.; Fraser, C.; Park, M.
Production of active recombinant eIF5A: Reconstitution in E. coli of eukaryotic hypusine modification of eIF5A by its coexpression with modifying enzymes
Protein Eng. Des. Sel.
24
301-309
2011
Homo sapiens
brenda
Epis, M.R.; Giles, K.M.; Kalinowski, F.C.; Barker, A.; Cohen, R.J.; Leedman, P.J.
Regulation of expression of deoxyhypusine hydroxylase (DOHH), the enzyme that catalyzes the activation of eIF5A, by miR-331-3p and miR-642-5p in prostate cancer cells
J. Biol. Chem.
287
35251-35259
2012
Homo sapiens (Q9BU89), Homo sapiens
brenda
Atemnkeng, V.A.; Pink, M.; Schmitz-Spanke, S.; Wu, X.J.; Dong, L.L.; Zhao, K.H.; May, C.; Laufer, S.; Langer, B.; Kaiser, A.
Deoxyhypusine hydroxylase from Plasmodium vivax, the neglected human malaria parasite: molecular cloning, expression and specific inhibition by the 5-LOX inhibitor zileuton
PLoS ONE
8
e58318
2013
Plasmodium vivax (A5JZ19), Plasmodium vivax, Plasmodium vivax Salvador I (A5JZ19)
brenda
von Koschitzky, I.; Gerhardt, H.; Laemmerhofer, M.; Kohout, M.; Gehringer, M.; Laufer, S.; Pink, M.; Schmitz-Spanke, S.; Strube, C.; Kaiser, A.
New insights into novel inhibitors against deoxyhypusine hydroxylase from Plasmodium falciparum compounds with an iron chelating potential
Amino Acids
47
1155-1166
2015
Plasmodium falciparum
brenda
Caceres, C.J.; Angulo, J.; Contreras, N.; Pino, K.; Vera-Otarola, J.; Lopez-Lastra, M.
Targeting deoxyhypusine hydroxylase activity impairs cap-independent translation initiation driven by the 5'untranslated region of the HIV-1, HTLV-1, and MMTV mRNAs
Antiviral Res.
134
192-206
2016
Homo sapiens (Q9BU89)
brenda
Quintas-Granados, L.I.; Carvajal Gamez, B.I.; Villalpando, J.L.; Ortega-Lopez, J.; Arroyo, R.; Azuara-Liceaga, E.; Alvarez-Sanchez, M.E.
Bifunctional activity of deoxyhypusine synthase/hydroxylase from Trichomonas vaginalis
Biochimie
123
37-51
2016
Trichomonas vaginalis
brenda
Belda-Palazon, B.; Nohales, M.A.; Rambla, J.L.; Acena, J.L.; Delgado, O.; Fustero, S.; Martinez, M.C.; Granell, A.; Carbonell, J.; Ferrando, A.
Biochemical quantitation of the eIF5A hypusination in Arabidopsis thaliana uncovers ABA-dependent regulation
Front. Plant Sci.
5
202
2014
Arabidopsis thaliana (Q8I701), Arabidopsis thaliana
brenda
Jasniewski, A.J.; Engstrom, L.M.; Vu, V.V.; Park, M.H.; Que, L.
X-ray absorption spectroscopic characterization of the diferric-peroxo intermediate of human deoxyhypusine hydroxylase in the presence of its substrate eIF5a
J. Biol. Inorg. Chem.
21
605-618
2016
Homo sapiens (Q9BU89), Homo sapiens
brenda
Frey, A.G.; Nandal, A.; Park, J.H.; Smith, P.M.; Yabe, T.; Ryu, M.S.; Ghosh, M.C.; Lee, J.; Rouault, T.A.; Park, M.H.; Philpott, C.C.
Iron chaperones PCBP1 and PCBP2 mediate the metallation of the dinuclear iron enzyme deoxyhypusine hydroxylase
Proc. Natl. Acad. Sci. USA
111
8031-8036
2014
Homo sapiens (Q9BU89)
brenda
Martinez-Rocha, A.L.; Woriedh, M.; Chemnitz, J.; Willingmann, P.; Kroeger, C.; Hadeler, B.; Hauber, J.; Schaefer, W.
Posttranslational hypusination of the eukaryotic translation initiation factor-5A regulates Fusarium graminearum virulence
Sci. Rep.
6
24698
2016
Fusarium graminearum (Q8I701), Fusarium graminearum
brenda
Han, Z.; Sakai, N.; Boettger, L.H.; Klinke, S.; Hauber, J.; Trautwein, A.X.; Hilgenfeld, R.
Crystal structure of the peroxo-diiron(III) intermediate of deoxyhypusine hydroxylase, an oxygenase involved in hypusination
Structure
23
882-892
2015
Homo sapiens (Q9BU89), Homo sapiens
brenda