EC Number | Application | Comment | Organism |
---|---|---|---|
1.14.99.29 | drug development | eIF5A and the hypusine biosynthetic enzymes are potential targets for intervention in aberrant cell proliferation | Drosophila melanogaster |
1.14.99.29 | drug development | eIF5A and the hypusine biosynthetic enzymes are potential targets for intervention in aberrant cell proliferation | Homo sapiens |
1.14.99.29 | drug development | eIF5A and the hypusine biosynthetic enzymes are potential targets for intervention in aberrant cell proliferation | Saccharomyces cerevisiae |
1.14.99.29 | drug development | eIF5A and the hypusine biosynthetic enzymes are potential targets for intervention in aberrant cell proliferation | Bos taurus |
1.14.99.29 | drug development | eIF5A and the hypusine biosynthetic enzymes are potential targets for intervention in aberrant cell proliferation | Schizosaccharomyces pombe |
1.14.99.29 | drug development | eIF5A and the hypusine biosynthetic enzymes are potential targets for intervention in aberrant cell proliferation | Caenorhabditis elegans |
EC Number | Cloned (Comment) | Organism |
---|---|---|
1.14.99.29 | single copy gene dohh | Saccharomyces cerevisiae |
EC Number | Protein Variants | Comment | Organism |
---|---|---|---|
1.14.99.29 | E66K | mutation E66K in the DOHH homologue gene, Mmd1, causes a temperature-sensitive growth phenotype and altered mitochondrial morphology and distribution | Schizosaccharomyces pombe |
1.14.99.29 | additional information | single copy gene dohh inactivation of deoxyhypusine hydroxylase | Saccharomyces cerevisiae |
EC Number | Inhibitors | Comment | Organism | Structure |
---|---|---|---|---|
1.14.99.29 | additional information | a number of metal-chelating inhibitors of DOHH causes growth inhibition and G1 cell cycle arrest in mammalian cells | Bos taurus | |
1.14.99.29 | additional information | a number of metal-chelating inhibitors of DOHH causes growth inhibition and G1 cell cycle arrest in mammalian cells | Homo sapiens |
EC Number | Metals/Ions | Comment | Organism | Structure |
---|---|---|---|---|
1.14.99.29 | Fe2+ | the enzyme contains a nonheme diiron active center that activates O2 | Drosophila melanogaster | |
1.14.99.29 | Fe2+ | the enzyme contains a nonheme diiron active center that activates O2 | Homo sapiens | |
1.14.99.29 | Fe2+ | the enzyme contains a nonheme diiron active center that activates O2 | Saccharomyces cerevisiae | |
1.14.99.29 | Fe2+ | the enzyme contains a nonheme diiron active center that activates O2 | Bos taurus | |
1.14.99.29 | Fe2+ | the enzyme contains a nonheme diiron active center that activates O2 | Schizosaccharomyces pombe | |
1.14.99.29 | Fe2+ | the enzyme contains a nonheme diiron active center that activates O2 | Caenorhabditis elegans |
EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
1.14.99.29 | eIF5A-N6-(4-aminobutyl)-L-lysine + AH2 + O2 | Saccharomyces cerevisiae | 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-amino-2-hydroxybutyl)-L-lysine + A + H2O | - |
? | |
1.14.99.29 | eIF5A-N6-(4-aminobutyl)-L-lysine + AH2 + O2 | Homo sapiens | different eIF5A isozymes exist. The unique posttranslational modification occurs in only one cellular protein, the eukaryotic translation initiation factor 5A, eIF5A | eIF5A-N6-(4-amino-2-hydroxybutyl)-L-lysine + A + H2O | - |
? | |
1.14.99.29 | eIF5A-N6-(4-aminobutyl)-L-lysine + AH2 + O2 | Caenorhabditis elegans | different eIF5A isozymes exist. The unique posttranslational modification occurs in only one cellular protein, the eukaryotic translation initiation factor 5A, eIF5A | eIF5A-N6-(4-amino-2-hydroxybutyl)-L-lysine + A + H2O | - |
? | |
1.14.99.29 | eIF5A-N6-(4-aminobutyl)-L-lysine + AH2 + O2 | Drosophila melanogaster | the unique posttranslational modification occurs in only one cellular protein, the eukaryotic translation initiation factor 5A, eIF5A | eIF5A-N6-(4-amino-2-hydroxybutyl)-L-lysine + A + H2O | - |
? | |
1.14.99.29 | eIF5A-N6-(4-aminobutyl)-L-lysine + AH2 + O2 | Bos taurus | the unique posttranslational modification occurs in only one cellular protein, the eukaryotic translation initiation factor 5A, eIF5A | eIF5A-N6-(4-amino-2-hydroxybutyl)-L-lysine + A + H2O | - |
? | |
1.14.99.29 | eIF5A-N6-(4-aminobutyl)-L-lysine + AH2 + O2 | Schizosaccharomyces pombe | the unique posttranslational modification occurs in only one cellular protein, the eukaryotic translation initiation factor 5A, eIF5A | eIF5A-N6-(4-amino-2-hydroxybutyl)-L-lysine + A + H2O | - |
? |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
1.14.99.29 | Bos taurus | - |
- |
- |
1.14.99.29 | Caenorhabditis elegans | - |
- |
- |
1.14.99.29 | Drosophila melanogaster | - |
- |
- |
1.14.99.29 | Homo sapiens | - |
- |
- |
1.14.99.29 | Saccharomyces cerevisiae | - |
- |
- |
1.14.99.29 | Schizosaccharomyces pombe | - |
gene Mmd1 | - |
2.5.1.46 | Mus musculus | - |
single gene | - |
2.5.1.46 | Saccharomyces cerevisiae | - |
single gene | - |
EC Number | Source Tissue | Comment | Organism | Textmining |
---|---|---|---|---|
1.14.99.29 | germ cell | - |
Caenorhabditis elegans | - |
1.14.99.29 | gonad | - |
Caenorhabditis elegans | - |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
1.14.99.29 | eIF5A-N6-(4-aminobutyl)-L-lysine + AH2 + O2 | - |
Drosophila melanogaster | eIF5A-N6-(4-amino-2-hydroxybutyl)-L-lysine + A + H2O | - |
? | |
1.14.99.29 | eIF5A-N6-(4-aminobutyl)-L-lysine + AH2 + O2 | - |
Homo sapiens | eIF5A-N6-(4-amino-2-hydroxybutyl)-L-lysine + A + H2O | - |
? | |
1.14.99.29 | eIF5A-N6-(4-aminobutyl)-L-lysine + AH2 + O2 | - |
Saccharomyces cerevisiae | eIF5A-N6-(4-amino-2-hydroxybutyl)-L-lysine + A + H2O | - |
? | |
1.14.99.29 | eIF5A-N6-(4-aminobutyl)-L-lysine + AH2 + O2 | - |
Bos taurus | eIF5A-N6-(4-amino-2-hydroxybutyl)-L-lysine + A + H2O | - |
? | |
1.14.99.29 | eIF5A-N6-(4-aminobutyl)-L-lysine + AH2 + O2 | - |
Schizosaccharomyces pombe | eIF5A-N6-(4-amino-2-hydroxybutyl)-L-lysine + A + H2O | - |
? | |
1.14.99.29 | eIF5A-N6-(4-aminobutyl)-L-lysine + AH2 + O2 | - |
Caenorhabditis elegans | eIF5A-N6-(4-amino-2-hydroxybutyl)-L-lysine + A + H2O | - |
? | |
1.14.99.29 | eIF5A-N6-(4-aminobutyl)-L-lysine + AH2 + O2 | 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 | Saccharomyces cerevisiae | eIF5A-N6-(4-amino-2-hydroxybutyl)-L-lysine + A + H2O | - |
? | |
1.14.99.29 | eIF5A-N6-(4-aminobutyl)-L-lysine + AH2 + O2 | different eIF5A isozymes exist. The unique posttranslational modification occurs in only one cellular protein, the eukaryotic translation initiation factor 5A, eIF5A | Homo sapiens | eIF5A-N6-(4-amino-2-hydroxybutyl)-L-lysine + A + H2O | - |
? | |
1.14.99.29 | eIF5A-N6-(4-aminobutyl)-L-lysine + AH2 + O2 | different eIF5A isozymes exist. The unique posttranslational modification occurs in only one cellular protein, the eukaryotic translation initiation factor 5A, eIF5A | Caenorhabditis elegans | eIF5A-N6-(4-amino-2-hydroxybutyl)-L-lysine + A + H2O | - |
? | |
1.14.99.29 | eIF5A-N6-(4-aminobutyl)-L-lysine + AH2 + O2 | the unique posttranslational modification occurs in only one cellular protein, the eukaryotic translation initiation factor 5A, eIF5A | Drosophila melanogaster | eIF5A-N6-(4-amino-2-hydroxybutyl)-L-lysine + A + H2O | - |
? | |
1.14.99.29 | eIF5A-N6-(4-aminobutyl)-L-lysine + AH2 + O2 | the unique posttranslational modification occurs in only one cellular protein, the eukaryotic translation initiation factor 5A, eIF5A | Bos taurus | eIF5A-N6-(4-amino-2-hydroxybutyl)-L-lysine + A + H2O | - |
? | |
1.14.99.29 | eIF5A-N6-(4-aminobutyl)-L-lysine + AH2 + O2 | the unique posttranslational modification occurs in only one cellular protein, the eukaryotic translation initiation factor 5A, eIF5A | Schizosaccharomyces pombe | eIF5A-N6-(4-amino-2-hydroxybutyl)-L-lysine + A + H2O | - |
? |
EC Number | Synonyms | Comment | Organism |
---|---|---|---|
1.14.99.29 | deoxyhypusine hydroxylase | - |
Drosophila melanogaster |
1.14.99.29 | deoxyhypusine hydroxylase | - |
Homo sapiens |
1.14.99.29 | deoxyhypusine hydroxylase | - |
Saccharomyces cerevisiae |
1.14.99.29 | deoxyhypusine hydroxylase | - |
Bos taurus |
1.14.99.29 | deoxyhypusine hydroxylase | - |
Schizosaccharomyces pombe |
1.14.99.29 | deoxyhypusine hydroxylase | - |
Caenorhabditis elegans |
1.14.99.29 | DOHH | - |
Drosophila melanogaster |
1.14.99.29 | DOHH | - |
Homo sapiens |
1.14.99.29 | DOHH | - |
Saccharomyces cerevisiae |
1.14.99.29 | DOHH | - |
Bos taurus |
1.14.99.29 | DOHH | - |
Schizosaccharomyces pombe |
1.14.99.29 | DOHH | - |
Caenorhabditis elegans |
2.5.1.46 | deoxyhypusine synthase | - |
Mus musculus |
2.5.1.46 | deoxyhypusine synthase | - |
Saccharomyces cerevisiae |
2.5.1.46 | DHS | - |
Mus musculus |
2.5.1.46 | DHS | - |
Saccharomyces cerevisiae |
EC Number | General Information | Comment | Organism |
---|---|---|---|
1.14.99.29 | evolution | the deoxyhypusine/hypusine synthetic pathway has evolved in archaea and eukaryotes, evolution of eIF5A and the hypusine pathway, overview | Drosophila melanogaster |
1.14.99.29 | evolution | the deoxyhypusine/hypusine synthetic pathway has evolved in archaea and eukaryotes, evolution of eIF5A and the hypusine pathway, overview | Homo sapiens |
1.14.99.29 | evolution | the deoxyhypusine/hypusine synthetic pathway has evolved in archaea and eukaryotes, evolution of eIF5A and the hypusine pathway, overview | Saccharomyces cerevisiae |
1.14.99.29 | evolution | the deoxyhypusine/hypusine synthetic pathway has evolved in archaea and eukaryotes, evolution of eIF5A and the hypusine pathway, overview | Bos taurus |
1.14.99.29 | evolution | the deoxyhypusine/hypusine synthetic pathway has evolved in archaea and eukaryotes, evolution of eIF5A and the hypusine pathway, overview | Schizosaccharomyces pombe |
1.14.99.29 | evolution | the deoxyhypusine/hypusine synthetic pathway has evolved in archaea and eukaryotes, evolution of eIF5A and the hypusine pathway, overview | Caenorhabditis elegans |
1.14.99.29 | malfunction | inactivation of DOHH is recessively lethal | Caenorhabditis elegans |
1.14.99.29 | malfunction | inactivation of DOHH is recessively lethal, phenotypes resulting from depletion of DOHH and hypusine-modified eIF5A, overview | Drosophila melanogaster |
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 | Drosophila melanogaster |
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 | Homo sapiens |
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 | Saccharomyces cerevisiae |
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 | Bos taurus |
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 | Schizosaccharomyces pombe |
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 | Caenorhabditis elegans |
1.14.99.29 | physiological function | requirement for eIF5A and for the hypusine modification enzymes in cell viability and growth | Homo sapiens |
1.14.99.29 | physiological function | requirement for eIF5A and for the hypusine modification enzymes in cell viability and growth | Bos taurus |
1.14.99.29 | 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 | Saccharomyces cerevisiae |
1.14.99.29 | 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 | Schizosaccharomyces pombe |
1.14.99.29 | physiological function | requirement for eIF5A and for the hypusine modification enzymes in cell viability and growth. The DOHH gene is essential | Drosophila melanogaster |
1.14.99.29 | physiological function | requirement for eIF5A and for the hypusine modification enzymes in cell viability and growth. The DOHH gene is essential | Caenorhabditis elegans |
2.5.1.46 | 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 | Saccharomyces cerevisiae |
2.5.1.46 | 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 | Mus musculus |