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Information on EC 1.14.99.29 - deoxyhypusine monooxygenase and Organism(s) Homo sapiens and UniProt Accession Q9BU89
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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
-
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
The taxonomic range for the selected organisms is: Homo sapiens
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
-
-
-
-
DOHH
oxygenase, deoxyhypusine di-
-
-
-
-
additional information
deoxyhypusine hydroxylase
-
-
-
-
deoxyhypusine hydroxylase
-
-
DOHH
-
-
-
-
additional information
-
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
additional information
-
the enzyme belongs to the family of 2-oxoacid- and Fe(II)-dependent dioxygenases
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
[eIF5A]-deoxyhypusine + reduced acceptor + O2 = [eIF5A]-hypusine + acceptor + H2O
binuclear iron mediated reaction mechanism
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
redox reaction
-
-
-
-
oxidation
reduction
oxidation
-
-
-
-
reduction
-
-
-
-
PATHWAY SOURCE
PATHWAYS
-
-
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
-
102576-87-4
-
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
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
-
strong preference of enzyme for binding the 6-N-(4-amino-2-hydroxybutyl)-L-lysine-containing form of translation initiation factor 5A
-
-
?
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 + AH2 + O2
[eIF5A]-hypusine + A + 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
-
-
-
-
?
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
-
-
?
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-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
-
-
?
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
?
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
-
-
?
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-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 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
-
-
-
-
?
additional information
?
-
-
DOHH hydroxylates the deoxyhypusyl-eukaryotic translation initiation factor eIF5A intermediate to hyposine-containing mature eIF5A using molecular oxygen
-
-
?
[eIF5A]-deoxyhypusine + AH2 + O2
[eIF5A]-hypusine + A + H2O
-
-
-
?
[eIF5A]-deoxyhypusine + AH2 + O2
[eIF5A]-hypusine + 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
-
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
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Iron
Fe2+
additional information
-
iron cannot be replaced by Cd2+, Co2+, Cr2+, Cu2+, Mg2+, Mn2+, Ni2+, Zn2+
Fe2+
-
a non-heme iron enzyme, DOHH probably contains one binuclear, diiron, active center, iron-binding active site structure of DOHH and mode of iron binding, the strictly conserved His-Glu motifs His56-Glu57, His89-Glu90, His207-Glu208 and His240-Glu241, are involved in iron binding, overview
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
mimosine
synergistic growth inhibition with the combination of miR-331-3p and miR-642-5p and mimosine
2-(2-hydroxy-5-methylphenyl)-4,5-dihydro-1,3-thiazole-4-carboxylic acid
-
inhibition in vitro and in cells
deferoxamine
-
targets the active metalloenzyme and inhibits DOHH in human vascular endothelial cells
2,2'-dipyridyl
-
targets the active metalloenzyme and inhibits DOHH in human vascular endothelial cells
ciclopirox
-
targets the active metalloenzyme and inhibits DOHH in human vascular endothelial cells
deferiprone
-
targets the active metalloenzyme and inhibits DOHH in human vascular endothelial 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
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
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.000065
6-N-[(R)-4-amino-2-hydroxybutyl]-L-lysine of human translation initiation factor 5A
-
pH 7.5, 37°C
-
0.000376
6-N-[(R)-4-amino-2-hydroxybutyl]-L-lysine of yeast translation initiation factor 5A
-
pH 7.5, 37°C
-
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.5
8.5
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
37
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
physiological function
evolution
metabolism
physiological function
additional information
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
the cellular concentration of the enzyme and its enzymatic activity play a role in HIV-1, HTLV-1 and MMTV IRES-mediated translation initiation
evolution
-
hypusine occurs only in eukaryotes and certain archaea, but not in eubacteria
evolution
-
the deoxyhypusine/hypusine synthetic pathway has evolved in archaea and eukaryotes, evolution of eIF5A and the hypusine pathway, 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
-
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
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
-
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
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
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_HUMAN
302
0
32904
Swiss-Prot
other Location (Reliability: 1)
PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
-
DOHHs from different species differ in their HEAT-like repeats
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
in complex with glycerol, hanging drop vapor diffusion method, using 30% polyethylene glycol 6000 (w/v), 400 mM guanidinium hydrochloride, 100 mM Bis-Tris propane (pH 7.2-7.4).
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
E208A
E208D
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
E241A
E57A
E57D
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
E90A
E93A
-
site-directed mutagenesis, the mutant shows reduced eIF5A(deoxyhypusine) binding
G214A
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
G63A
H207A
H240A
H56A
H89A
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
additional information
-
construction of a polycistronic vector encoding eIF5A, DHS and DOHH, overview
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
-
site-directed mutagenesis, the mutant shows severely impairment in eIF5A(deoxyhypusine) binding
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
-
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
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
GSH-Sepharose resin column chromatography and Superdex 200 gel filtration
recombinant GST-tagged DOHH by glutathione affinity chromatography. Recombinant His-tagged hypusine pathway enzymes from Escherichia coli by anion exchange and nickel affinity chromatography
-
recombinant GST-tagged wild-type and mutant enzymes from Escherichia coli strain BL21(DE3) by glutathione affinity chromatography, the tag is cleaved off by thrombin
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
construction of a polycistronic vector encoding eIF5A, DHS and DOHH, expression in Escherichia coli strain BL21(DE3), overview. Effects of time and temperature on the expression of recombinant proteins and hypusine modification, DOHH effectively hydroxylates all the eIF5A(Dhp), a deoxyhypusine-containing intermediate, formed
-
expression of GST-tagged wild-type and mutant enzymes in Escherichia coli strain BL21(DE3)
-
single copy gene dohh, expression as GST-tagged protein, expression of the hypusine pathway genes in Escherichia coli as His-tagged proteins
-
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
transient overexpression of micro-RNA miR-331-3p and/or miR-642-5p in DU-145 prostate cancer cells reduces DOHH mRNA and protein expression and inhibits cell proliferation
RENATURED/Commentary
ORGANISM
UNIPROT
LITERATURE
activity of metal-free apoenzyme can be restored by addition of Fe2+, but not by Cd2+, Co2+, Cr2+, Cu2+, Mg2+, Mn2+, Ni2+, Zn2+
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
drug development
-
eIF5A and the hypusine biosynthetic enzymes are potential targets for intervention in aberrant cell proliferation
medicine
medicine
-
inhibition of DOHH leads to a decrease of hypusine-containing eIF5A and inhibition of eukaryotic cell growth, consequently, these results suggest that eIF5A and DOHH could be promising targets for antitumor and anti-HIV-1 therapies
medicine
-
the results support the concept that drugs targeting DOHH should be tested clinically for HIV-1 inhibition and could be developed as antiretrovirals
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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
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
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
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
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
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
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
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
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
Homo sapiens, Saccharomyces cerevisiae
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
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
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
Kerscher, B.; Nzukou, E.; Kaiser, A.
Assessment of deoxyhypusine hydroxylase as a putative, novel drug target
Amino Acids
38
471-477
2010
Bos taurus, Drosophila melanogaster, Homo sapiens, Plasmodium falciparum, Rattus norvegicus, Saccharomyces cerevisiae, Schizosaccharomyces pombe
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
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
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
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)
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
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)
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