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Literature summary for 1.14.99.29 extracted from

  • Park, M.H.; Nishimura, K.; Zanelli, C.F.; Valentini, S.R.
    Functional significance of eIF5A and its hypusine modification in eukaryotes (2010), Amino Acids, 38, 491-500.
    View publication on PubMedView publication on EuropePMC

Application

Application Comment Organism
drug development eIF5A and the hypusine biosynthetic enzymes are potential targets for intervention in aberrant cell proliferation Drosophila melanogaster
drug development eIF5A and the hypusine biosynthetic enzymes are potential targets for intervention in aberrant cell proliferation Homo sapiens
drug development eIF5A and the hypusine biosynthetic enzymes are potential targets for intervention in aberrant cell proliferation Saccharomyces cerevisiae
drug development eIF5A and the hypusine biosynthetic enzymes are potential targets for intervention in aberrant cell proliferation Bos taurus
drug development eIF5A and the hypusine biosynthetic enzymes are potential targets for intervention in aberrant cell proliferation Schizosaccharomyces pombe
drug development eIF5A and the hypusine biosynthetic enzymes are potential targets for intervention in aberrant cell proliferation Caenorhabditis elegans

Cloned(Commentary)

Cloned (Comment) Organism
single copy gene dohh Saccharomyces cerevisiae

Protein Variants

Protein Variants Comment Organism
E66K mutation E66K in the DOHH homologue gene, Mmd1, causes a temperature-sensitive growth phenotype and altered mitochondrial morphology and distribution Schizosaccharomyces pombe
additional information single copy gene dohh inactivation of deoxyhypusine hydroxylase Saccharomyces cerevisiae

Inhibitors

Inhibitors Comment Organism Structure
additional information a number of metal-chelating inhibitors of DOHH causes growth inhibition and G1 cell cycle arrest in mammalian cells Bos taurus
additional information a number of metal-chelating inhibitors of DOHH causes growth inhibition and G1 cell cycle arrest in mammalian cells Homo sapiens

Metals/Ions

Metals/Ions Comment Organism Structure
Fe2+ the enzyme contains a nonheme diiron active center that activates O2 Drosophila melanogaster
Fe2+ the enzyme contains a nonheme diiron active center that activates O2 Homo sapiens
Fe2+ the enzyme contains a nonheme diiron active center that activates O2 Saccharomyces cerevisiae
Fe2+ the enzyme contains a nonheme diiron active center that activates O2 Bos taurus
Fe2+ the enzyme contains a nonheme diiron active center that activates O2 Schizosaccharomyces pombe
Fe2+ the enzyme contains a nonheme diiron active center that activates O2 Caenorhabditis elegans

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
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
-
?
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
-
?
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
-
?
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
-
?
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
-
?
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
-
?

Organism

Organism UniProt Comment Textmining
Bos taurus
-
-
-
Caenorhabditis elegans
-
-
-
Drosophila melanogaster
-
-
-
Homo sapiens
-
-
-
Saccharomyces cerevisiae
-
-
-
Schizosaccharomyces pombe
-
gene Mmd1
-

Source Tissue

Source Tissue Comment Organism Textmining
germ cell
-
Caenorhabditis elegans
-
gonad
-
Caenorhabditis elegans
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
eIF5A-N6-(4-aminobutyl)-L-lysine + AH2 + O2
-
Drosophila melanogaster eIF5A-N6-(4-amino-2-hydroxybutyl)-L-lysine + A + H2O
-
?
eIF5A-N6-(4-aminobutyl)-L-lysine + AH2 + O2
-
Homo sapiens eIF5A-N6-(4-amino-2-hydroxybutyl)-L-lysine + A + H2O
-
?
eIF5A-N6-(4-aminobutyl)-L-lysine + AH2 + O2
-
Saccharomyces cerevisiae eIF5A-N6-(4-amino-2-hydroxybutyl)-L-lysine + A + H2O
-
?
eIF5A-N6-(4-aminobutyl)-L-lysine + AH2 + O2
-
Bos taurus eIF5A-N6-(4-amino-2-hydroxybutyl)-L-lysine + A + H2O
-
?
eIF5A-N6-(4-aminobutyl)-L-lysine + AH2 + O2
-
Schizosaccharomyces pombe eIF5A-N6-(4-amino-2-hydroxybutyl)-L-lysine + A + H2O
-
?
eIF5A-N6-(4-aminobutyl)-L-lysine + AH2 + O2
-
Caenorhabditis elegans eIF5A-N6-(4-amino-2-hydroxybutyl)-L-lysine + A + H2O
-
?
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
-
?
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
-
?
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
-
?
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
-
?
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
-
?
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
-
?

Synonyms

Synonyms Comment Organism
deoxyhypusine hydroxylase
-
Drosophila melanogaster
deoxyhypusine hydroxylase
-
Homo sapiens
deoxyhypusine hydroxylase
-
Saccharomyces cerevisiae
deoxyhypusine hydroxylase
-
Bos taurus
deoxyhypusine hydroxylase
-
Schizosaccharomyces pombe
deoxyhypusine hydroxylase
-
Caenorhabditis elegans
DOHH
-
Drosophila melanogaster
DOHH
-
Homo sapiens
DOHH
-
Saccharomyces cerevisiae
DOHH
-
Bos taurus
DOHH
-
Schizosaccharomyces pombe
DOHH
-
Caenorhabditis elegans

General Information

General Information Comment Organism
evolution the deoxyhypusine/hypusine synthetic pathway has evolved in archaea and eukaryotes, evolution of eIF5A and the hypusine pathway, overview Drosophila melanogaster
evolution the deoxyhypusine/hypusine synthetic pathway has evolved in archaea and eukaryotes, evolution of eIF5A and the hypusine pathway, overview Homo sapiens
evolution the deoxyhypusine/hypusine synthetic pathway has evolved in archaea and eukaryotes, evolution of eIF5A and the hypusine pathway, overview Saccharomyces cerevisiae
evolution the deoxyhypusine/hypusine synthetic pathway has evolved in archaea and eukaryotes, evolution of eIF5A and the hypusine pathway, overview Bos taurus
evolution the deoxyhypusine/hypusine synthetic pathway has evolved in archaea and eukaryotes, evolution of eIF5A and the hypusine pathway, overview Schizosaccharomyces pombe
evolution the deoxyhypusine/hypusine synthetic pathway has evolved in archaea and eukaryotes, evolution of eIF5A and the hypusine pathway, overview Caenorhabditis elegans
malfunction inactivation of DOHH is recessively lethal Caenorhabditis elegans
malfunction inactivation of DOHH is recessively lethal, phenotypes resulting from depletion of DOHH and hypusine-modified eIF5A, overview Drosophila melanogaster
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
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
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
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
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
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
physiological function requirement for eIF5A and for the hypusine modification enzymes in cell viability and growth Homo sapiens
physiological function requirement for eIF5A and for the hypusine modification enzymes in cell viability and growth Bos taurus
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
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
physiological function requirement for eIF5A and for the hypusine modification enzymes in cell viability and growth. The DOHH gene is essential Drosophila melanogaster
physiological function requirement for eIF5A and for the hypusine modification enzymes in cell viability and growth. The DOHH gene is essential Caenorhabditis elegans