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Information on EC 1.14.99.29 - deoxyhypusine monooxygenase and Organism(s) Bos taurus and UniProt Accession Q0VC53
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1.14.99.29 deoxyhypusine monooxygenaseIUBMB Comments
The enzyme catalyses the final step in the formation of the amino acid hypusine in the eukaryotic initiation factor 5A.
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Word Map
- 1.14.99.29
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eif-5a
- spermidine
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hypusine-containing
- gc7
- mimosine
- ciclopirox
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nepsilon-4-amino-2-hydroxybutyllysine
- drug development
- deferiprone
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eif5a-1
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polyamine-derived
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4-aminobutyl
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diiron
- n1-guanyl-1,7-diaminoheptane
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heat-repeats
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heat-like
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peroxo
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deoxyhypusine-containing
- medicine
The taxonomic range for the selected organisms is: Bos taurus
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea
Synonyms
deoxyhypusine hydroxylase, hdohh, deoxyhypusyl hydroxylase, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
deoxyhypusine hydroxylase
deoxyhypusyl hydroxylase
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DOHH
oxygenase, deoxyhypusine di-
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additional information
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DOHH belongs to a family of HEAT-like repeat proteins which comprise the Huntingtin protein, elongation factor 3, the protein phosphatase subunit 2A, and the target of rapamycin
deoxyhypusine hydroxylase
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DOHH
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
redox reaction
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oxidation
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reduction
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PATHWAY SOURCE
PATHWAYS
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SYSTEMATIC NAME
IUBMB Comments
deoxyhypusine,hydrogen-donor:oxygen oxidoreductase (2-hydroxylating)
The enzyme catalyses the final step in the formation of the amino acid hypusine in the eukaryotic initiation factor 5A.
CAS REGISTRY NUMBER
COMMENTARY
101920-83-6
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102576-87-4
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
eIF5A-Nepsilon-(4-aminobutyl)lysine + AH2 + O2
eIF5A-Nepsilon-(4-amino-2-hydroxybutyl)lysine + A + 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
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
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-
?
eIF5A-Nepsilon-(4-aminobutyl)lysine + AH2 + O2
eIF5A-Nepsilon-(4-amino-2-hydroxybutyl)lysine + A + H2O
eIF5A is the eukaryotic translation initiation factor 5A
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-
?
eIF5A-N6-(4-aminobutyl)-L-lysine + AH2 + O2
eIF5A-N6-(4-amino-2-hydroxybutyl)-L-lysine + A + H2O
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-
-
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?
eIF5A-N6-(4-aminobutyl)-L-lysine + AH2 + O2
eIF5A-N6-(4-amino-2-hydroxybutyl)-L-lysine + A + H2O
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the unique posttranslational modification occurs in only one cellular protein, the eukaryotic translation initiation factor 5A, eIF5A
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?
additional information
?
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eIF5A occurs in tumor cells, and it also acts as a cofactor of the Rev transactivator protein in HIV-1-infected cells
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?
additional information
?
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eIF5A occurs in tumor cells, and it also acts as a cofactor of the Rev transactivator protein in HIV-1-infected cells
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?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
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-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
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?
eIF5A-N6-(4-aminobutyl)-L-lysine + AH2 + O2
eIF5A-N6-(4-amino-2-hydroxybutyl)-L-lysine + A + H2O
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the unique posttranslational modification occurs in only one cellular protein, the eukaryotic translation initiation factor 5A, eIF5A
-
-
?
additional information
?
-
eIF5A occurs in tumor cells, and it also acts as a cofactor of the Rev transactivator protein in HIV-1-infected cells
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?
additional information
?
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eIF5A occurs in tumor cells, and it also acts as a cofactor of the Rev transactivator protein in HIV-1-infected cells
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?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Fe2+
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
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a number of metal-chelating inhibitors of DOHH causes growth inhibition and G1 cell cycle arrest in mammalian cells
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pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
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the deoxyhypusine/hypusine synthetic pathway has evolved in archaea and eukaryotes, evolution of eIF5A and the hypusine pathway, overview
metabolism
physiological function
metabolism
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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
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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
physiological function
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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
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requirement for eIF5A and for the hypusine modification enzymes in cell viability and growth
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). DOHH_BOVIN
303
0
33261
Swiss-Prot
other Location (Reliability: 2)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
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DOHHs from different species differ in their HEAT-like repeats
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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
additional information
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
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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
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant GST-tagged wild-type and mutant enzymes from Escherichia coli strain JM109 by glutathione affinity chromatography, the GST-tag is cleaved off
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
DNA and amino acid sequence determination and analysis, different clones, sequence comparisons, expression of GST-tagged wild-type and mutant enzymes in Escherichia coli strain JM109
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
drug development
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eIF5A and the hypusine biosynthetic enzymes are potential targets for intervention in aberrant cell proliferation
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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
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, Caenorhabditis elegans, Drosophila melanogaster, Homo sapiens, Saccharomyces cerevisiae, Schizosaccharomyces pombe
EXTERNAL LINKS (specific for EC-Number 1.14.99.29)
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Release 2023.1 (January 2023)
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