1.14.99.29: deoxyhypusine monooxygenase
This is an abbreviated version!
For detailed information about deoxyhypusine monooxygenase, go to the full flat file.
Word Map on EC 1.14.99.29
-
1.14.99.29
-
eif-5a
-
spermidine
-
hypusine-containing
-
gc7
-
mimosine
-
ciclopirox
-
nepsilon-4-amino-2-hydroxybutyllysine
-
drug development
-
deferiprone
-
eif5a-1
-
polyamine-derived
-
4-aminobutyl
-
diiron
-
n1-guanyl-1,7-diaminoheptane
-
heat-repeats
-
heat-like
-
peroxo
-
deoxyhypusine-containing
-
medicine
- 1.14.99.29
-
eif-5a
- spermidine
-
hypusine-containing
- gc7
- mimosine
- ciclopirox
-
nepsilon-4-amino-2-hydroxybutyllysine
- drug development
- deferiprone
-
eif5a-1
-
polyamine-derived
-
4-aminobutyl
-
diiron
- n1-guanyl-1,7-diaminoheptane
-
heat-repeats
-
heat-like
-
peroxo
-
deoxyhypusine-containing
- medicine
Reaction
Synonyms
deoxyhypusine hydroxylase, deoxyhypusine hydroxylase homologue nero, deoxyhypusine synthase/hydroxylase, deoxyhypusyl hydroxylase, DOHH, DOOH, hDOHH, Lia1, More, nero, oxygenase, deoxyhypusine di-
ECTree
Advanced search results
General Information
General Information on EC 1.14.99.29 - deoxyhypusine monooxygenase
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
evolution
malfunction
metabolism
physiological function
additional information
-
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
-
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, phenotypes resulting from depletion of DOHH and hypusine-modified eIF5A, overview
-
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
-
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
-
-
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