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Information on EC 2.5.1.46 - deoxyhypusine synthase
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2.5.1.46 deoxyhypusine synthaseIUBMB Comments
The eukaryotic initiation factor eIF5A contains a hypusine residue that is essential for activity. This enzyme catalyses the first reaction of hypusine formation from one specific lysine residue of the eIF5A precursor. The reaction occurs in four steps: NAD+-dependent dehydrogenation of spermidine (1a), formation of an enzyme-imine intermediate by transfer of the 4-aminobutylidene group from dehydrospermidine to the active site lysine residue (Lys329 for the human enzyme; 1b), transfer of the same 4-aminobutylidene group from the enzyme intermediate to the e1F5A precursor (1c), reduction of the e1F5A-imine intermediate to form a deoxyhypusine residue (1d). Hence the overall reaction is transfer of a 4-aminobutyl group. For the plant enzyme, homospermidine can substitute for spermidine and putrescine can substitute for the lysine residue of the eIF5A precursor. Hypusine is formed from deoxyhypusine by the action of EC 1.14.99.29, deoxyhypusine monooxygenase.
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Word Map
- 2.5.1.46
- polyamine
- gc7
- homospermidine
-
pyrrolizidine
- n1-guanyl-1,7-diaminoheptane
-
nepsilon-4-amino-2-hydroxybutyllysine
-
aminobutylation
-
hypusine-containing
- 1,7-diaminoheptane
-
deoxyhypusine-containing
- butylamine
-
polyamine-derived
-
eif-4d
- medicine
- 1,3-diaminopropane
- triamine
-
wolff
- drug development
- analysis
The expected taxonomic range for this enzyme is: Archaea, Bacteria, Eukaryota
Reaction Schemes
Synonyms
deoxyhypusine synthase, dhs34, cpdhs, pf3d7_1412600, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
deoxyhypusine synthase
deoxyhypusine synthase (Caulobacter crescentus gene CC0359)
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deoxyhypusine synthase (Halobacterium strain NRC-1 gene dhs)
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-
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-
deoxyhypusine synthase (human clone 30649 gene DHPS subunit reduced)
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-
deoxyhypusine synthase (Nicotiana tabacum gene DHS1)
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-
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deoxyhypusine synthase (Senecio vernalis gene DHS1)
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-
deoxyhypusinesynthase
DHPS
DHS
DHS34
DHSc
DHSp
Dys1p
EC 1.1.1.249
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-
formerly
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HVO 2297
synthase, deoxyhypusine
-
-
-
-
TbDHSc
TbDHSp
DHS
-
-
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
dehydrospermidine + [enzyme]-lysine = N-(4-aminobutylidene)-[enzyme]-lysine + propane-1,3-diamine
(1b)
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-
-
N-(4-aminobutylidene)-[eIF5A-precursor]-lysine + NADH + H+ = [eIF5A-precursor]-deoxyhypusine + NAD+
(1d)
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-
-
N-(4-aminobutylidene)-[enzyme]-lysine + [eIF5A-precursor]-lysine = N-(4-aminobutylidene)-[eIF5A-precursor]-lysine + [enzyme]-lysine
(1c)
-
-
-
spermidine + NAD+ = dehydrospermidine + NADH
(1a)
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-
-
[eIF5A-precursor]-lysine + spermidine = [eIF5A-precursor]-deoxyhypusine + propane-1,3-diamine
[eIF5A-precursor]-lysine + spermidine = [eIF5A-precursor]-deoxyhypusine + propane-1,3-diamine
first reaction
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[eIF5A-precursor]-lysine + spermidine = [eIF5A-precursor]-deoxyhypusine + propane-1,3-diamine
the eukaryotic initiation factor eIF5A contains a hypusine residue that is essential for activity. This enzyme catalyses the first reaction of hypusine formation from one specific lysine residue of the eIF5A precursor, the second reaction being catalysed by EC 1.14.99.29, deoxyhypusine monooxygenase. The reaction of this enzyme occurs in four steps: i. NAD-dependent dehydrogenation of spermidine, ii. formation of an enzyme-imine intermediate by transfer of the 4-aminobutylidene group from dehydrospermidine to the active site lysine residue, Lys329 for the human enzyme, iii. transfer of the same 4-aminobutylidene group from the enzyme intermediate to the eIF5A precursor, iv. reduction of the eIF5A-imine intermediate to form a deoxyhypusine residue. Hence the overall reaction is transfer of a 4-aminobutyl group. For the plant enzyme, homospermidine can substitute for spermidine and putrescine can substitute for the lysine residue of the eIF5A precursor
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
aminobutyl group transfer
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-
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-
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SYSTEMATIC NAME
IUBMB Comments
[eIF5A-precursor]-lysine:spermidine 4-aminobutyltransferase (propane-1,3-diamine-forming)
The eukaryotic initiation factor eIF5A contains a hypusine residue that is essential for activity. This enzyme catalyses the first reaction of hypusine formation from one specific lysine residue of the eIF5A precursor. The reaction occurs in four steps: NAD+-dependent dehydrogenation of spermidine (1a), formation of an enzyme-imine intermediate by transfer of the 4-aminobutylidene group from dehydrospermidine to the active site lysine residue (Lys329 for the human enzyme; 1b), transfer of the same 4-aminobutylidene group from the enzyme intermediate to the e1F5A precursor (1c), reduction of the e1F5A-imine intermediate to form a deoxyhypusine residue (1d). Hence the overall reaction is transfer of a 4-aminobutyl group. For the plant enzyme, homospermidine can substitute for spermidine and putrescine can substitute for the lysine residue of the eIF5A precursor. Hypusine is formed from deoxyhypusine by the action of EC 1.14.99.29, deoxyhypusine monooxygenase.
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CAS REGISTRY NUMBER
COMMENTARY
127069-31-2
deoxyhypusine synthase
171041-87-5
human clone 30649 gene DHPS subunit reduced
253180-41-5
Nicotiana tabacum gene DHS1
259168-76-8
Senecio vernalis gene DHS1
302492-11-1
Halobacterium strain NRC-1 gene dhs
332963-67-4
Caulobacter crescentus gene CC0359
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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
1-ethylspermidine + [eIF5A-precursor]-lysine
[eIF5A-precursor]-deoxyhypusine + ?
-
-
-
?
1-methylspermidine + [eIF5A-precursor]-lysine
[eIF5A-precursor]-deoxyhypusine + ?
-
-
-
?
8-ethylspermidine + [eIF5A-precursor]-lysine
[eIF5A-precursor]-ethyldeoxyhypusine + ?
-
-
-
?
8-methylspermidine + [eIF5A-precursor]-lysine
[eIF5A-precursor]-methyldeoxyhypusine + ?
-
-
-
?
aminopropylcadaverine + [eIF5A-precursor]-lysine
[eIF5A-precursor]-homodeoxyhypusine + ?
-
-
-
?
homospermidine + [eIF5A-precursor]-lysine
[eIF5A-precursor]-deoxyhypusine + ?
-
-
-
?
N-(3-aminopropyl)-1,4-diamino-cis-but-2-ene + putrescine
(1Z)-N4-(4-aminobutyl)but-1-ene-1,4-diamine + 1,3-diaminopropane
-
-
-
?
N-(3-aminopropyl)-1,4-diamino-cis-but-2-ene + [eIF5A-precursor]-lysine
?
-
-
-
?
N-(3-aminopropyl)-1,4-diamino-trans-but-2-ene + putrescine
(1E)-N4-(4-aminobutyl)but-1-ene-1,4-diamine + 1,3-diaminopropane
-
-
-
?
N-(3-aminopropyl)-1,4-diamino-trans-but-2-ene + [eIF5A-precursor]-lysine
?
-
-
-
?
[eIF5A-1-precursor]-lysine + spermidine
[eIF5A-1-precursor]-deoxyhypusine + propane-1,3-diamine
[eIF5A-2-precursor]-lysine + spermidine
[eIF5A-2-precursor]-deoxyhypusine + propane-1,3-diamine
-
-
-
-
?
[eIF5A-precursor]-L-lysine + spermidine
[eIF5A-precursor]-deoxyhypusine + propane-1,3-diamine
[eIF5A-precursor]-lysine + homospermidine
[eIF5A-precursor]-deoxyhypusine + putrescine
-
-
?
[eIF5A-precursor]-lysine + spermidine
[eIF5A-precursor]-deoxyhypusine + propane-1,3-diamine
[eIF5A-precursor]-lysine42 + spermidine
[eIF5A-precursor]-lysine42-deoxyhypusine + propane-1,3-diamine
[TveIF-5A-precursor]-lysine + spermidine
[TveIF-5A-precursor]-deoxyhypusine + propane-1,3-diamine
spermidine
1,3-diaminopropane + DELTA1-pyrroline
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reaction in absence of eIF5A-precursor
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?
spermidine
1,3-diaminopropane + DELTA1-pyrroline
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reaction in absence of eIF5A-precursor
-
?
spermidine
1,3-diaminopropane + DELTA1-pyrroline
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reaction in absence of eIF5A-precursor
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?
spermidine
1,3-diaminopropane + DELTA1-pyrroline
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reaction in absence of eIF5A-precursor
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?
spermidine + NAD+
dehydrospermidine + NADH
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-
-
?
[eIF5A-1-precursor]-lysine + spermidine
[eIF5A-1-precursor]-deoxyhypusine + propane-1,3-diamine
-
-
-
-
?
[eIF5A-1-precursor]-lysine + spermidine
[eIF5A-1-precursor]-deoxyhypusine + propane-1,3-diamine
-
-
-
-
?
[eIF5A-precursor] + spermidine
[eIF5A-precursor]-deoxyhypusine + propane-1,3-diamine
-
-
-
?
[eIF5A-precursor] + spermidine
[eIF5A-precursor]-deoxyhypusine + propane-1,3-diamine
-
-
-
?
[eIF5A-precursor] + spermidine
[eIF5A-precursor]-deoxyhypusine + propane-1,3-diamine
-
-
-
?
[eIF5A-precursor] + spermidine
[eIF5A-precursor]-deoxyhypusine + propane-1,3-diamine
-
-
-
?
[eIF5A-precursor]-L-lysine + spermidine
[eIF5A-precursor]-deoxyhypusine + propane-1,3-diamine
-
-
-
?
[eIF5A-precursor]-L-lysine + spermidine
[eIF5A-precursor]-deoxyhypusine + propane-1,3-diamine
-
-
-
?
[eIF5A-precursor]-L-lysine + spermidine
[eIF5A-precursor]-deoxyhypusine + propane-1,3-diamine
-
-
-
?
[eIF5A-precursor]-L-lysine + spermidine
[eIF5A-precursor]-deoxyhypusine + propane-1,3-diamine
-
-
-
-
?
[eIF5A-precursor]-L-lysine + spermidine
[eIF5A-precursor]-deoxyhypusine + propane-1,3-diamine
-
-
-
?
[eIF5A-precursor]-lysine + (R)-3-methylspermidine
?
enzyme DHS prefers the (R)- over the (S)-enantiomer as a substrate
-
-
?
[eIF5A-precursor]-lysine + (R)-3-methylspermidine
?
no activity with the (S)-enantiomer
-
-
?
[eIF5A-precursor]-lysine + 2-methylspermidine
?
-
the S-enantiomer of 2-MeSpd, which supports long-term growth, is a good substrate for DHS in vitro, whereas the R isomer is not
-
-
?
[eIF5A-precursor]-lysine + spermidine
[eIF5A-precursor]-deoxyhypusine + propane-1,3-diamine
-
-
-
-
?
[eIF5A-precursor]-lysine + spermidine
[eIF5A-precursor]-deoxyhypusine + propane-1,3-diamine
-
-
-
?
[eIF5A-precursor]-lysine + spermidine
[eIF5A-precursor]-deoxyhypusine + propane-1,3-diamine
transfer of a 4-aminobutyl moiety group
-
-
?
[eIF5A-precursor]-lysine + spermidine
[eIF5A-precursor]-deoxyhypusine + propane-1,3-diamine
-
-
-
?
[eIF5A-precursor]-lysine + spermidine
[eIF5A-precursor]-deoxyhypusine + propane-1,3-diamine
transfer of a 4-aminobutyl moiety group
-
-
?
[eIF5A-precursor]-lysine + spermidine
[eIF5A-precursor]-deoxyhypusine + propane-1,3-diamine
deoxyhypusine synthase is the first of the two enzymes that catalyze the maturation of eukaryotic initiation factor 5A. Synthesis of hypusine is essential for the function of eIF5A in eukaryotic cell proliferation and survival
-
-
?
[eIF5A-precursor]-lysine + spermidine
[eIF5A-precursor]-deoxyhypusine + propane-1,3-diamine
bovine enzyme is approximately 26times as effective as the human enzyme in catalyzing the reaction
-
-
?
[eIF5A-precursor]-lysine + spermidine
[eIF5A-precursor]-deoxyhypusine + propane-1,3-diamine
-
-
-
-
?
[eIF5A-precursor]-lysine + spermidine
[eIF5A-precursor]-deoxyhypusine + propane-1,3-diamine
-
-
-
-
?
[eIF5A-precursor]-lysine + spermidine
[eIF5A-precursor]-deoxyhypusine + propane-1,3-diamine
-
-
-
-
?
[eIF5A-precursor]-lysine + spermidine
[eIF5A-precursor]-deoxyhypusine + propane-1,3-diamine
-
the enzyme catalyzes the first reaction in a two-step conversion of inactive eIF-5A to its active form
-
-
?
[eIF5A-precursor]-lysine + spermidine
[eIF5A-precursor]-deoxyhypusine + propane-1,3-diamine
-
-
-
?
[eIF5A-precursor]-lysine + spermidine
[eIF5A-precursor]-deoxyhypusine + propane-1,3-diamine
-
-
-
-
?
[eIF5A-precursor]-lysine + spermidine
[eIF5A-precursor]-deoxyhypusine + propane-1,3-diamine
-
-
-
-
?
[eIF5A-precursor]-lysine + spermidine
[eIF5A-precursor]-deoxyhypusine + propane-1,3-diamine
hypusination of Lys56
-
-
?
[eIF5A-precursor]-lysine + spermidine
[eIF5A-precursor]-deoxyhypusine + propane-1,3-diamine
-
-
-
-
?
[eIF5A-precursor]-lysine + spermidine
[eIF5A-precursor]-deoxyhypusine + propane-1,3-diamine
-
-
-
-
?
[eIF5A-precursor]-lysine + spermidine
[eIF5A-precursor]-deoxyhypusine + propane-1,3-diamine
-
the enzyme catalyzes the first reaction in a two-step conversion of inactive eIF-5A to its active form
-
-
?
[eIF5A-precursor]-lysine + spermidine
[eIF5A-precursor]-deoxyhypusine + propane-1,3-diamine
-
-
-
-
?
[eIF5A-precursor]-lysine + spermidine
[eIF5A-precursor]-deoxyhypusine + propane-1,3-diamine
-
-
-
-
ir
[eIF5A-precursor]-lysine + spermidine
[eIF5A-precursor]-deoxyhypusine + propane-1,3-diamine
-
-
-
?
[eIF5A-precursor]-lysine + spermidine
[eIF5A-precursor]-deoxyhypusine + propane-1,3-diamine
-
-
-
-
?
[eIF5A-precursor]-lysine + spermidine
[eIF5A-precursor]-deoxyhypusine + propane-1,3-diamine
-
-
-
?
[eIF5A-precursor]-lysine + spermidine
[eIF5A-precursor]-deoxyhypusine + propane-1,3-diamine
-
-
i.e. [eIF5A-precursor]-N6-(4-aminobutyl)lysine
?
[eIF5A-precursor]-lysine + spermidine
[eIF5A-precursor]-deoxyhypusine + propane-1,3-diamine
-
-
i.e. [eIF5A-precursor]-N6-(4-aminobutyl)lysine
?
[eIF5A-precursor]-lysine + spermidine
[eIF5A-precursor]-deoxyhypusine + propane-1,3-diamine
-
-
i.e. [eIF5A-precursor]-N6-(4-aminobutyl)lysine
?
[eIF5A-precursor]-lysine + spermidine
[eIF5A-precursor]-deoxyhypusine + propane-1,3-diamine
-
-
i.e. [eIF5A-precursor]-N6-(4-aminobutyl)lysine
?
[eIF5A-precursor]-lysine + spermidine
[eIF5A-precursor]-deoxyhypusine + propane-1,3-diamine
-
-
i.e. [eIF5A-precursor]-N6-(4-aminobutyl)lysine
?
[eIF5A-precursor]-lysine + spermidine
[eIF5A-precursor]-deoxyhypusine + propane-1,3-diamine
-
-
i.e. [eIF5A-precursor]-N6-(4-aminobutyl)lysine
?
[eIF5A-precursor]-lysine + spermidine
[eIF5A-precursor]-deoxyhypusine + propane-1,3-diamine
-
-
i.e. [eIF5A-precursor]-N6-(4-aminobutyl)lysine
?
[eIF5A-precursor]-lysine + spermidine
[eIF5A-precursor]-deoxyhypusine + propane-1,3-diamine
-
-
i.e. [eIF5A-precursor]-N6-(4-aminobutyl)lysine
?
[eIF5A-precursor]-lysine + spermidine
[eIF5A-precursor]-deoxyhypusine + propane-1,3-diamine
-
-
i.e. [eIF5A-precursor]-N6-(4-aminobutyl)lysine
?
[eIF5A-precursor]-lysine + spermidine
[eIF5A-precursor]-deoxyhypusine + propane-1,3-diamine
-
-
i.e. [eIF5A-precursor]-N6-(4-aminobutyl)lysine
?
[eIF5A-precursor]-lysine + spermidine
[eIF5A-precursor]-deoxyhypusine + propane-1,3-diamine
-
i.e. [eIF5A-precursor]-N6-(4-aminobutyl)lysine
?
[eIF5A-precursor]-lysine + spermidine
[eIF5A-precursor]-deoxyhypusine + propane-1,3-diamine
-
reversal of reaction in presence of NAD+
i.e. [eIF5A-precursor]-N6-(4-aminobutyl)lysine
r
[eIF5A-precursor]-lysine + spermidine
[eIF5A-precursor]-deoxyhypusine + propane-1,3-diamine
-
first step in the biosynthesis of hypusine
-
-
?
[eIF5A-precursor]-lysine + spermidine
[eIF5A-precursor]-deoxyhypusine + propane-1,3-diamine
first step in the biosynthesis of hypusine
-
-
?
[eIF5A-precursor]-lysine + spermidine
[eIF5A-precursor]-deoxyhypusine + propane-1,3-diamine
-
posttranslational activation of eIF-5A which has a specialized role in proliferation and in serum starvation-induced apoptosis in endothelial cells
-
-
?
[eIF5A-precursor]-lysine + spermidine
[eIF5A-precursor]-deoxyhypusine + propane-1,3-diamine
overall reaction
-
-
?
[eIF5A-precursor]-lysine + spermidine
[eIF5A-precursor]-deoxyhypusine + propane-1,3-diamine
-
bovine enzyme is approximately 26times as effective as the human enzyme in catalyzing the reaction
-
-
?
[eIF5A-precursor]-lysine + spermidine
[eIF5A-precursor]-deoxyhypusine + propane-1,3-diamine
-
DHS catalyzes a NAD-dependent cleavage between N4 and C5 of spermidine and the transfer of the butylamine moiety to the ?-amino group of a specific lysine residue of the eIF5A precursor, eIF5A(Lys), to form the deoxyhypusine residue. The enzyme is modification is strictly specific for one single lysine residue of the cellular protein eukaryotic initiation factor 5A (eIF5A) and does not work on short peptides
1,3-diaminopropane is released as a byproduct from spermidine cleavage
-
?
[eIF5A-precursor]-lysine + spermidine
[eIF5A-precursor]-deoxyhypusine + propane-1,3-diamine
formation of [N(epsilon)-(4-amino-2-hydroxybutyl)lysine]
-
-
?
[eIF5A-precursor]-lysine + spermidine
[eIF5A-precursor]-deoxyhypusine + propane-1,3-diamine
-
-
-
-
?
[eIF5A-precursor]-lysine + spermidine
[eIF5A-precursor]-deoxyhypusine + propane-1,3-diamine
-
-
-
-
?
[eIF5A-precursor]-lysine + spermidine
[eIF5A-precursor]-deoxyhypusine + propane-1,3-diamine
-
-
-
-
?
[eIF5A-precursor]-lysine + spermidine
[eIF5A-precursor]-deoxyhypusine + propane-1,3-diamine
-
-
-
-
?
[eIF5A-precursor]-lysine + spermidine
[eIF5A-precursor]-deoxyhypusine + propane-1,3-diamine
-
-
-
?
[eIF5A-precursor]-lysine + spermidine
[eIF5A-precursor]-deoxyhypusine + propane-1,3-diamine
-
-
-
?
[eIF5A-precursor]-lysine + spermidine
[eIF5A-precursor]-deoxyhypusine + propane-1,3-diamine
-
-
-
-
?
[eIF5A-precursor]-lysine + spermidine
[eIF5A-precursor]-deoxyhypusine + propane-1,3-diamine
-
-
-
-
?
[eIF5A-precursor]-lysine + spermidine
[eIF5A-precursor]-deoxyhypusine + propane-1,3-diamine
-
-
-
?
[eIF5A-precursor]-lysine + spermidine
[eIF5A-precursor]-deoxyhypusine + propane-1,3-diamine
-
i.e. [eIF5A-precursor]-N6-(4-aminobutyl)lysine
?
[eIF5A-precursor]-lysine + spermidine
[eIF5A-precursor]-deoxyhypusine + propane-1,3-diamine
-
-
-
?
[eIF5A-precursor]-lysine + spermidine
[eIF5A-precursor]-deoxyhypusine + propane-1,3-diamine
-
i.e. [eIF5A-precursor]-N6-(4-aminobutyl)lysine
?
[eIF5A-precursor]-lysine + spermidine
[eIF5A-precursor]-deoxyhypusine + propane-1,3-diamine
overall reaction
-
-
?
[eIF5A-precursor]-lysine + spermidine
[eIF5A-precursor]-deoxyhypusine + propane-1,3-diamine
the enzyme is involved in synthesis of synthesis of homospermidine
-
-
?
[eIF5A-precursor]-lysine + spermidine
[eIF5A-precursor]-deoxyhypusine + propane-1,3-diamine
-
-
-
-
?
[eIF5A-precursor]-lysine + spermidine
[eIF5A-precursor]-deoxyhypusine + propane-1,3-diamine
-
-
i.e. [eIF5A-precursor]-N6-(4-aminobutyl)lysine
?
[eIF5A-precursor]-lysine + spermidine
[eIF5A-precursor]-deoxyhypusine + propane-1,3-diamine
-
-
i.e. [eIF5A-precursor]-N6-(4-aminobutyl)lysine
?
[eIF5A-precursor]-lysine + spermidine
[eIF5A-precursor]-deoxyhypusine + propane-1,3-diamine
-
-
i.e. [eIF5A-precursor]-N6-(4-aminobutyl)lysine
?
[eIF5A-precursor]-lysine + spermidine
[eIF5A-precursor]-deoxyhypusine + propane-1,3-diamine
-
-
-
-
?
[eIF5A-precursor]-lysine + spermidine
[eIF5A-precursor]-deoxyhypusine + propane-1,3-diamine
-
-
i.e. [eIF5A-precursor]-N6-(4-aminobutyl)lysine
?
[eIF5A-precursor]-lysine + spermidine
[eIF5A-precursor]-deoxyhypusine + propane-1,3-diamine
-
-
i.e. [eIF5A-precursor]-N6-(4-aminobutyl)lysine
?
[eIF5A-precursor]-lysine + spermidine
[eIF5A-precursor]-deoxyhypusine + propane-1,3-diamine
-
-
i.e. [eIF5A-precursor]-N6-(4-aminobutyl)lysine
?
[eIF5A-precursor]-lysine + spermidine
[eIF5A-precursor]-deoxyhypusine + propane-1,3-diamine
-
-
i.e. [eIF5A-precursor]-N6-(4-aminobutyl)lysine
?
[eIF5A-precursor]-lysine + spermidine
[eIF5A-precursor]-deoxyhypusine + propane-1,3-diamine
-
-
i.e. [eIF5A-precursor]-N6-(4-aminobutyl)lysine
?
[eIF5A-precursor]-lysine + spermidine
[eIF5A-precursor]-deoxyhypusine + propane-1,3-diamine
-
-
i.e. [eIF5A-precursor]-N6-(4-aminobutyl)lysine
?
[eIF5A-precursor]-lysine + spermidine
[eIF5A-precursor]-deoxyhypusine + propane-1,3-diamine
-
the enzyme catalyzes the first reaction in a two-step conversion of inactive eIF-5A to its active form
-
-
?
[eIF5A-precursor]-lysine + spermidine
[eIF5A-precursor]-deoxyhypusine + propane-1,3-diamine
-
-
-
-
?
[eIF5A-precursor]-lysine + spermidine
[eIF5A-precursor]-deoxyhypusine + propane-1,3-diamine
-
-
-
?
[eIF5A-precursor]-lysine + spermidine
[eIF5A-precursor]-deoxyhypusine + propane-1,3-diamine
-
i.e. [eIF5A-precursor]-N6-(4-aminobutyl)lysine
?
[eIF5A-precursor]-lysine + spermidine
[eIF5A-precursor]-deoxyhypusine + propane-1,3-diamine
-
i.e. [eIF5A-precursor]-N6-(4-aminobutyl)lysine
?
[eIF5A-precursor]-lysine + spermidine
[eIF5A-precursor]-deoxyhypusine + propane-1,3-diamine
posttranslational activation of the initiation factor 5A
-
-
?
[eIF5A-precursor]-lysine + spermidine
[eIF5A-precursor]-deoxyhypusine + propane-1,3-diamine
-
i.e. [eIF5A-precursor]-N6-(4-aminobutyl)lysine
?
[eIF5A-precursor]-lysine + spermidine
[eIF5A-precursor]-deoxyhypusine + propane-1,3-diamine
-
-
-
?
[eIF5A-precursor]-lysine + spermidine
[eIF5A-precursor]-deoxyhypusine + propane-1,3-diamine
-
-
-
?
[eIF5A-precursor]-lysine + spermidine
[eIF5A-precursor]-deoxyhypusine + propane-1,3-diamine
-
-
-
-
?
[eIF5A-precursor]-lysine + spermidine
[eIF5A-precursor]-deoxyhypusine + propane-1,3-diamine
-
-
-
?
[eIF5A-precursor]-lysine + spermidine
[eIF5A-precursor]-deoxyhypusine + propane-1,3-diamine
Trypanosoma brucei brucei 927 / 4 GUTat10.1 / TREU927
-
-
-
?
[eIF5A-precursor]-lysine + spermidine
[eIF5A-precursor]-deoxyhypusine + propane-1,3-diamine
-
-
-
-
?
[eIF5A-precursor]-lysine42 + spermidine
[eIF5A-precursor]-lysine42-deoxyhypusine + propane-1,3-diamine
-
substrate [eIF5A-precursor]-lysine42 of Haloferax volcanii
overall reaction
-
?
[eIF5A-precursor]-lysine42 + spermidine
[eIF5A-precursor]-lysine42-deoxyhypusine + propane-1,3-diamine
-
substrate [eIF5A-precursor]-lysine42 of Haloferax volcanii
overall reaction
-
?
[TveIF-5A-precursor]-lysine + spermidine
[TveIF-5A-precursor]-deoxyhypusine + propane-1,3-diamine
-
-
-
?
[TveIF-5A-precursor]-lysine + spermidine
[TveIF-5A-precursor]-deoxyhypusine + propane-1,3-diamine
transfer of 4-amino-2-hydroxybutyl side chain, MS/MS analysis for determination of the hypusine residue
-
-
?
[TveIF-5A-precursor]-lysine + spermidine
[TveIF-5A-precursor]-deoxyhypusine + propane-1,3-diamine
-
-
-
?
[TveIF-5A-precursor]-lysine + spermidine
[TveIF-5A-precursor]-deoxyhypusine + propane-1,3-diamine
transfer of 4-amino-2-hydroxybutyl side chain, MS/MS analysis for determination of the hypusine residue
-
-
?
additional information
?
-
-
deoxyhypusine synthase-suppressed Brassica napus plants have larger leaves as well as enhanced seed yield, this appears to reflect increased tolerance to chronic sublethal stress
-
-
?
additional information
?
-
-
recombinant deoxyhypusine synthase from Haloferax volcanii does not show any activity under varying aIF5A concentration and substrate concentration unsing spermidine, agmatine, cadaverine, and putrescine. In vivo, the eIF5A-precursor in Haloferax volcanii is shown to be deoxyhypusinylated
-
-
?
additional information
?
-
-
recombinant deoxyhypusine synthase from Haloferax volcanii does not show any activity under varying aIF5A concentration and substrate concentration unsing spermidine, agmatine, cadaverine, and putrescine. In vivo, the eIF5A-precursor in Haloferax volcanii is shown to be deoxyhypusinylated
-
-
?
additional information
?
-
-
as racemic mixtures, only 2-MeSpd and 3-MeSpd support long-term growth (9-18 days) of spermidine-depleted DU-145 cells, whereas gamma-MeSpd and omega-MeSpd do not
-
-
?
additional information
?
-
-
development of a radioactive assay method for detection of spermidine incorporation into eIF5A, overview
-
-
?
additional information
?
-
(R)-3-methylspermidine competes with spermidine for cellular uptake less efficiently than the (S)-3-methylspermidine
-
-
?
additional information
?
-
(R)-3-methylspermidine competes with spermidine for cellular uptake less efficiently than the (S)-3-methylspermidine
-
-
?
additional information
?
-
-
the DHSL20 protein lacks a critical lysine residue, and the recombinant protein shows no DHS activity in vitro, while DHS34 contains the critical lysine residue, and the recombinant DHS34 effectively catalyzes deoxyhypusine synthesis
-
-
?
additional information
?
-
the DHSL20 protein lacks a critical lysine residue, and the recombinant protein shows no DHS activity in vitro, while DHS34 contains the critical lysine residue, and the recombinant DHS34 effectively catalyzes deoxyhypusine synthesis
-
-
?
additional information
?
-
the DHSL20 protein lacks a critical lysine residue, and the recombinant protein shows no DHS activity in vitro, while DHS34 contains the critical lysine residue, and the recombinant DHS34 effectively catalyzes deoxyhypusine synthesis
-
-
?
additional information
?
-
no synthesis of [eIF5A-precursor]-hypusine
-
-
?
additional information
?
-
-
no synthesis of [eIF5A-precursor]-hypusine
-
-
?
additional information
?
-
no synthesis of [eIF5A-precursor]-hypusine
-
-
?
additional information
?
-
-
mutants of substrate [eIF5A-1-precursor]-lysine with changes in residue K50, and mutants G52A and K55A are no substrates. The hypusine site loop has critical importance in eIF5A function and hypusine modification
-
-
?
additional information
?
-
the rTvDHS enzyme is bifunctional and is also involved in the hydroxylation of deoxyhypusine-containing rTveIF-5A, cf. EC 1.14.99.29
-
-
?
additional information
?
-
-
the rTvDHS enzyme is bifunctional and is also involved in the hydroxylation of deoxyhypusine-containing rTveIF-5A, cf. EC 1.14.99.29
-
-
?
additional information
?
-
formation of a TvDHS-TveIF-5A complex
-
-
?
additional information
?
-
-
formation of a TvDHS-TveIF-5A complex
-
-
?
additional information
?
-
the rTvDHS enzyme is bifunctional and is also involved in the hydroxylation of deoxyhypusine-containing rTveIF-5A, cf. EC 1.14.99.29
-
-
?
additional information
?
-
formation of a TvDHS-TveIF-5A complex
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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-precursor]-lysine + spermidine
[eIF5A-precursor]-deoxyhypusine + propane-1,3-diamine
[TveIF-5A-precursor]-lysine + spermidine
[TveIF-5A-precursor]-deoxyhypusine + propane-1,3-diamine
[eIF5A-precursor]-lysine + spermidine
[eIF5A-precursor]-deoxyhypusine + propane-1,3-diamine
-
-
-
?
[eIF5A-precursor]-lysine + spermidine
[eIF5A-precursor]-deoxyhypusine + propane-1,3-diamine
-
-
-
?
[eIF5A-precursor]-lysine + spermidine
[eIF5A-precursor]-deoxyhypusine + propane-1,3-diamine
deoxyhypusine synthase is the first of the two enzymes that catalyze the maturation of eukaryotic initiation factor 5A. Synthesis of hypusine is essential for the function of eIF5A in eukaryotic cell proliferation and survival
-
-
?
[eIF5A-precursor]-lysine + spermidine
[eIF5A-precursor]-deoxyhypusine + propane-1,3-diamine
-
-
-
-
?
[eIF5A-precursor]-lysine + spermidine
[eIF5A-precursor]-deoxyhypusine + propane-1,3-diamine
-
-
-
-
?
[eIF5A-precursor]-lysine + spermidine
[eIF5A-precursor]-deoxyhypusine + propane-1,3-diamine
-
the enzyme catalyzes the first reaction in a two-step conversion of inactive eIF-5A to its active form
-
-
?
[eIF5A-precursor]-lysine + spermidine
[eIF5A-precursor]-deoxyhypusine + propane-1,3-diamine
-
-
-
?
[eIF5A-precursor]-lysine + spermidine
[eIF5A-precursor]-deoxyhypusine + propane-1,3-diamine
-
-
-
-
?
[eIF5A-precursor]-lysine + spermidine
[eIF5A-precursor]-deoxyhypusine + propane-1,3-diamine
-
-
-
-
?
[eIF5A-precursor]-lysine + spermidine
[eIF5A-precursor]-deoxyhypusine + propane-1,3-diamine
hypusination of Lys56
-
-
?
[eIF5A-precursor]-lysine + spermidine
[eIF5A-precursor]-deoxyhypusine + propane-1,3-diamine
-
-
-
-
?
[eIF5A-precursor]-lysine + spermidine
[eIF5A-precursor]-deoxyhypusine + propane-1,3-diamine
-
the enzyme catalyzes the first reaction in a two-step conversion of inactive eIF-5A to its active form
-
-
?
[eIF5A-precursor]-lysine + spermidine
[eIF5A-precursor]-deoxyhypusine + propane-1,3-diamine
-
-
-
-
?
[eIF5A-precursor]-lysine + spermidine
[eIF5A-precursor]-deoxyhypusine + propane-1,3-diamine
-
-
-
-
ir
[eIF5A-precursor]-lysine + spermidine
[eIF5A-precursor]-deoxyhypusine + propane-1,3-diamine
-
-
-
?
[eIF5A-precursor]-lysine + spermidine
[eIF5A-precursor]-deoxyhypusine + propane-1,3-diamine
-
-
-
-
?
[eIF5A-precursor]-lysine + spermidine
[eIF5A-precursor]-deoxyhypusine + propane-1,3-diamine
-
-
-
?
[eIF5A-precursor]-lysine + spermidine
[eIF5A-precursor]-deoxyhypusine + propane-1,3-diamine
-
first step in the biosynthesis of hypusine
-
-
?
[eIF5A-precursor]-lysine + spermidine
[eIF5A-precursor]-deoxyhypusine + propane-1,3-diamine
first step in the biosynthesis of hypusine
-
-
?
[eIF5A-precursor]-lysine + spermidine
[eIF5A-precursor]-deoxyhypusine + propane-1,3-diamine
-
posttranslational activation of eIF-5A which has a specialized role in proliferation and in serum starvation-induced apoptosis in endothelial cells
-
-
?
[eIF5A-precursor]-lysine + spermidine
[eIF5A-precursor]-deoxyhypusine + propane-1,3-diamine
-
-
-
-
?
[eIF5A-precursor]-lysine + spermidine
[eIF5A-precursor]-deoxyhypusine + propane-1,3-diamine
-
-
-
-
?
[eIF5A-precursor]-lysine + spermidine
[eIF5A-precursor]-deoxyhypusine + propane-1,3-diamine
-
-
-
-
?
[eIF5A-precursor]-lysine + spermidine
[eIF5A-precursor]-deoxyhypusine + propane-1,3-diamine
-
-
-
-
?
[eIF5A-precursor]-lysine + spermidine
[eIF5A-precursor]-deoxyhypusine + propane-1,3-diamine
-
-
-
?
[eIF5A-precursor]-lysine + spermidine
[eIF5A-precursor]-deoxyhypusine + propane-1,3-diamine
-
-
-
?
[eIF5A-precursor]-lysine + spermidine
[eIF5A-precursor]-deoxyhypusine + propane-1,3-diamine
-
-
-
-
?
[eIF5A-precursor]-lysine + spermidine
[eIF5A-precursor]-deoxyhypusine + propane-1,3-diamine
-
-
-
-
?
[eIF5A-precursor]-lysine + spermidine
[eIF5A-precursor]-deoxyhypusine + propane-1,3-diamine
-
-
-
?
[eIF5A-precursor]-lysine + spermidine
[eIF5A-precursor]-deoxyhypusine + propane-1,3-diamine
-
-
-
?
[eIF5A-precursor]-lysine + spermidine
[eIF5A-precursor]-deoxyhypusine + propane-1,3-diamine
the enzyme is involved in synthesis of synthesis of homospermidine
-
-
?
[eIF5A-precursor]-lysine + spermidine
[eIF5A-precursor]-deoxyhypusine + propane-1,3-diamine
-
-
-
-
?
[eIF5A-precursor]-lysine + spermidine
[eIF5A-precursor]-deoxyhypusine + propane-1,3-diamine
-
-
-
-
?
[eIF5A-precursor]-lysine + spermidine
[eIF5A-precursor]-deoxyhypusine + propane-1,3-diamine
-
the enzyme catalyzes the first reaction in a two-step conversion of inactive eIF-5A to its active form
-
-
?
[eIF5A-precursor]-lysine + spermidine
[eIF5A-precursor]-deoxyhypusine + propane-1,3-diamine
-
-
-
?
[eIF5A-precursor]-lysine + spermidine
[eIF5A-precursor]-deoxyhypusine + propane-1,3-diamine
posttranslational activation of the initiation factor 5A
-
-
?
[eIF5A-precursor]-lysine + spermidine
[eIF5A-precursor]-deoxyhypusine + propane-1,3-diamine
-
-
-
?
[eIF5A-precursor]-lysine + spermidine
[eIF5A-precursor]-deoxyhypusine + propane-1,3-diamine
-
-
-
?
[eIF5A-precursor]-lysine + spermidine
[eIF5A-precursor]-deoxyhypusine + propane-1,3-diamine
-
-
-
-
?
[eIF5A-precursor]-lysine + spermidine
[eIF5A-precursor]-deoxyhypusine + propane-1,3-diamine
-
-
-
?
[eIF5A-precursor]-lysine + spermidine
[eIF5A-precursor]-deoxyhypusine + propane-1,3-diamine
Trypanosoma brucei brucei 927 / 4 GUTat10.1 / TREU927
-
-
-
?
[eIF5A-precursor]-lysine + spermidine
[eIF5A-precursor]-deoxyhypusine + propane-1,3-diamine
-
-
-
-
?
[TveIF-5A-precursor]-lysine + spermidine
[TveIF-5A-precursor]-deoxyhypusine + propane-1,3-diamine
-
-
-
?
[TveIF-5A-precursor]-lysine + spermidine
[TveIF-5A-precursor]-deoxyhypusine + propane-1,3-diamine
-
-
-
?
additional information
?
-
-
deoxyhypusine synthase-suppressed Brassica napus plants have larger leaves as well as enhanced seed yield, this appears to reflect increased tolerance to chronic sublethal stress
-
-
?
additional information
?
-
-
as racemic mixtures, only 2-MeSpd and 3-MeSpd support long-term growth (9-18 days) of spermidine-depleted DU-145 cells, whereas gamma-MeSpd and omega-MeSpd do not
-
-
?
additional information
?
-
the rTvDHS enzyme is bifunctional and is also involved in the hydroxylation of deoxyhypusine-containing rTveIF-5A, cf. EC 1.14.99.29
-
-
?
additional information
?
-
-
the rTvDHS enzyme is bifunctional and is also involved in the hydroxylation of deoxyhypusine-containing rTveIF-5A, cf. EC 1.14.99.29
-
-
?
additional information
?
-
the rTvDHS enzyme is bifunctional and is also involved in the hydroxylation of deoxyhypusine-containing rTveIF-5A, cf. EC 1.14.99.29
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
NAD+
-
one enzyme tetramer can bind up to four each of NAD+ and spermidine, the binding of spermidine being dependent on NAD+
NAD+
-
the NADH generated in the first step of the reaction remains enzyme-associated during the reaction and the hydride ion generated by the oxidation of spermidine is preserved for the reduction of the eIF5A-imine intermediate
NAD+
required, Km value is 0.082 mM, kcat is 0.018/s for the heterotetrameric DHS
NAD+
each enzyme heterodimer contains two NAD+ binding sites, one housed in the functional catalytic site and the second bound in a remnant dead site that lacks key catalytic residues
NADH
there is a measurable release of enzyme-bound NADH in the absence of eIF5A precursor. The NADH:DHS ratio is around 6
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
(4-[[2-(1H-benzimidazol-2-yl)hydrazinylidene]methyl]phenyl)(hydroxy)oxoammonium
55% inhibition
1-amino-7-guanidinoheptane
-
competitive, inhibits binding of spermidine to the enzyme
6-bromo-N-(1H-indol-4-yl)-1-benzothiophene-2-carboxamide
the 6'-bromo substituent is necessary for binding to DHPS
8-fluoro-N-[3-(morpholin-4-yl)propyl]-5H-pyrimido[5,4-b]indol-4-amine
23.6% inhibition
GC7
-
a specific DHS-inhibitor, inhibits DHS by competitive replacement of its native spermidine substrate. Inhibition of DHS by GC7 induces antiproliferative effects in vitro. The compound shows a strong antiproliferative effect in glioblastoma cell lines in vitro, while normal human astrocytes are not affected, and it causes p53 dependent premature senescence, a permanent cell cycle arrestin U-MG 87 cells
N,N'-bis[3,5-bis[1(aminoiminomethyl)-hydrazoethyl]phenyl]dodecanediamide-tetrahydrochloride
N-(3-aminopropyl)-cis-1,4-diaminocyclohexane
-
1 mM, less than 50% inhibition
N-(3-aminopropyl)-trans-1,4-diaminocyclohexane
-
1 mM, less than 50% inhibition
N-(7-chloroquinolin-4-yl)-N'-methylpropane-1,3-diamine
12.45% inhibition
N-guanyl-1,7-diaminoheptane
shows only little inhibitory effect on the leishmanial recombinant DHS34
N1-methylspermidine
-
inhibits generation of spermidine from [eIF5A-precursor]-deoxyhypusine
N4-(3-aminopropyl)-4-methylpentane-1,4-diamine
-
1 mM, less than 50% inhibition
1,7-Diaminoheptane
-
inhibits generation of spermidine from [eIF5A-precursor]-deoxyhypusine
CNI-1493
-
inhibition in vitro and in vivo, inhibits germination conidia. Although DHS of wheat, fungus, and human can be equally inhibited by the inhibitor CNI-1493 in vitro, application during infection of wheat and maize flowers results in strong inhibition of the pathogen without interference with kernel development, providing the possibiity to selectively inhibit fungal growth without affecting plant growth
CNI-1493
a compound that inhibits fungal DHS activity without affecting grain development
CNI-1493
-
inhibition in vitro. Although DHS of wheat, fungus, and human can be equally inhibited by the inhibitor CNI-1493 in vitro, application during infection of wheat and maize flowers results in strong inhibition of the pathogen without interference with kernel development, providing the possibiity to selectively inhibit fungal growth without affecting plant growth
CNI-1493
-
inhibition in vitro. Although DHS of wheat, fungus, and human can be equally inhibited by the inhibitor CNI-1493 in vitro, application during infection of wheat and maize flowers results in strong inhibition of the pathogen without interference with kernel development, providing the possibiity to selectively inhibit fungal growth without affecting plant growth
N''-guanyl-1,7-diaminoheptane
i.e. GC7, almost complete inhibition at 20 microM in both one-step and two-step assays
N''-guanyl-1,7-diaminoheptane
i.e. GC7. Downregulation of eIF5A through inhibition of deoxyhypusine synthase favors the reversal of the Th1 mediated cellular processes but minimally affects CD8 T-cells. Inhibition of elF5A increases the Treg/Th17 ratio, reduces anti-GAD65 antibody production and islet/beta-cell ER stress that leads to improvement in the endocrine pancreas functionality in a humanized model of T1D. Diabetes onset is delayed
N,N'-bis[3,5-bis[1(aminoiminomethyl)-hydrazoethyl]phenyl]decanediamide-tetrahydrochloride
-
i.e. CNI-1493
N,N'-bis[3,5-bis[1(aminoiminomethyl)-hydrazoethyl]phenyl]decanediamide-tetrahydrochloride
-
i.e. CNI-1493
N,N'-bis[3,5-bis[1(aminoiminomethyl)-hydrazoethyl]phenyl]dodecanediamide-tetrahydrochloride
-
i.e. DHSI-15
N,N'-bis[3,5-bis[1(aminoiminomethyl)-hydrazoethyl]phenyl]dodecanediamide-tetrahydrochloride
-
i.e. DHSI-15
N1-ethylspermidine
-
inhibits generation of spermidine from [eIF5A-precursor]-deoxyhypusine
N1-guanyl-1,7-diaminoheptane
GC7, a potent competitive inhibitor of DHS, causes an effective inhibition of infection and growth of Cryptosporidium parvum in human HCT-8 adenocarcinoma cells. Complete inhibition at 0.01 mM
N1-guanyl-1,7-diaminoheptane
-
inhibits generation of spermidine from [eIF5A-precursor]-deoxyhypusine
N1-guanyl-1,7-diaminoheptane
GC7, inhibits the activity of TbDHSc-TbDBHSp heterotetrameric complex; GC7, inhibits the activity of TbDHSc-TbDBHSp heterotetrameric complex
spermidine
-
inhibits generation of spermidine from [eIF5A-precursor]-deoxyhypusine
additional information
no growth inhibition by alpha-difluoromethylornithine, an inhibitor of polyamine biosynthesis, and (R)-3-methylspermidine, while the the combination of alpha-difluoromethylornithine with a racemate or (S)-3-methylspermidine causes cessation of cell growth. Cells treated with racemic 3-MeSpd accumulat intracellularly mainly (S)-3-methylspermidine, but not DHS substrate (R)-3-methylspermidine, explaining the inability of the racemate to support long-term growth
-
additional information
inhibitor screning in an anti-malaria compound collection, a guanyl residue seems to be an important lead structure for inhibition of Theileria parva DHS enzyme
-
additional information
-
inhibitor screning in an anti-malaria compound collection, a guanyl residue seems to be an important lead structure for inhibition of Theileria parva DHS enzyme
-
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DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
Adenocarcinoma
A hypusine-eIF5A-PEAK1 switch regulates the pathogenesis of pancreatic cancer.
Carcinogenesis
Hypusine biosynthesis in ? cells links polyamine metabolism to facultative cellular proliferation to maintain glucose homeostasis.
Carcinoma
The hypusine cascade promotes cancer progression and metastasis through the regulation of RhoA in squamous cell carcinoma.
Diabetes Mellitus, Type 1
Deoxyhypusine synthase promotes differentiation and proliferation of T helper type 1 (Th1) cells in autoimmune diabetes.
Diabetes Mellitus, Type 1
Protective effects of polyamine depletion in mouse models of type 1 diabetes: implications for therapy.
Diabetes Mellitus, Type 2
Inhibition of deoxyhypusine synthase enhances islet {beta} cell function and survival in the setting of endoplasmic reticulum stress and type 2 diabetes.
Glioblastoma
Expression of Eukaryotic Initiation Factor 5A and Hypusine Forming Enzymes in Glioblastoma Patient Samples: Implications for New Targeted Therapies.
Hyperglycemia
Protective effects of polyamine depletion in mouse models of type 1 diabetes: implications for therapy.
Leishmaniasis
Targeting polyamine metabolism for finding new drugs against leishmaniasis: a review.
Leukemia
Evaluation of deoxyhypusine synthase inhibitors targeting BCR-ABL positive leukemias.
Leukemia, Erythroblastic, Acute
Effects of inhibitors of deoxyhypusine synthase on the differentiation of mouse neuroblastoma and erythroleukemia cells.
Malaria
A suggested vital function for eIF-5A and dhs genes during murine malaria blood-stage infection.
Malaria
Cloning, expression and functional activity of deoxyhypusine synthase from Plasmodium vivax.
Melanoma
Novel Allosteric Inhibitors of Deoxyhypusine Synthase against Malignant Melanoma: Design, Synthesis, and Biological Evaluation.
Neoplasm Metastasis
The hypusine cascade promotes cancer progression and metastasis through the regulation of RhoA in squamous cell carcinoma.
Neoplasms
Aminohexanoic hydroxamate is a potent inducer of the differentiation of mouse neuroblastoma cells.
Neoplasms
Deoxyhypusine synthase (DHPS) inhibitor GC7 induces p21/Rb-mediated inhibition of tumor cell growth and DHPS expression correlates with poor prognosis in neuroblastoma patients.
Neoplasms
Effects of inhibitors of deoxyhypusine synthase on the differentiation of mouse neuroblastoma and erythroleukemia cells.
Neoplasms
Evaluation of deoxyhypusine synthase inhibitors targeting BCR-ABL positive leukemias.
Neoplasms
N1-guanyl-1,7-diaminoheptane enhances the chemosensitivity of acute lymphoblastic leukemia cells to vincristine through inhibition of eif5a-2 activation.
Neoplasms
The polyamine-derived amino acid hypusine: its post-translational formation in eIF-5A and its role in cell proliferation.
Neuroblastoma
Aminohexanoic hydroxamate is a potent inducer of the differentiation of mouse neuroblastoma cells.
Neuroblastoma
Deoxyhypusine synthase (DHPS) inhibitor GC7 induces p21/Rb-mediated inhibition of tumor cell growth and DHPS expression correlates with poor prognosis in neuroblastoma patients.
Neuroblastoma
Effects of inhibitors of deoxyhypusine synthase on the differentiation of mouse neuroblastoma and erythroleukemia cells.
Pancreatitis
[Methylated analogues of spermine and spermidine as tools to investigate cellular functions of polyamines and the enzymes of their metabolism]
Squamous Cell Carcinoma of Head and Neck
The hypusine cascade promotes cancer progression and metastasis through the regulation of RhoA in squamous cell carcinoma.
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0012
NAD+
mutant E166A, pH not specified in the publication, temperature not specified in the publication
0.0013
NAD+
wild-type, pH not specified in the publication, temperature not specified in the publication
0.098
NAD+
mutant H266A, pH not specified in the publication, temperature not specified in the publication
0.0098
spermidine
wild-type, pH not specified in the publication, temperature not specified in the publication
0.011
spermidine
mutant E166A, pH not specified in the publication, temperature not specified in the publication
0.012
spermidine
mutant H266A, pH not specified in the publication, temperature not specified in the publication
0.0007
[eIF5A-precursor]-lysine
pH 7.5, 37°C, heterotetrameric DHS
0.00091
[eIF5A-precursor]-lysine
pH 7.5, 37°C, heterotetrameric DHS
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.018
[eIF5A-precursor]-lysine
pH 7.5, 37°C, heterotetrameric DHS
0.15
NAD+
wild-type, pH not specified in the publication, temperature not specified in the publication
0.16
NAD+
mutant E166A, pH not specified in the publication, temperature not specified in the publication
0.16
NAD+
mutant H266A, pH not specified in the publication, temperature not specified in the publication
0.081
spermidine
mutant H266A, pH not specified in the publication, temperature not specified in the publication
0.12
spermidine
mutant E166A, pH not specified in the publication, temperature not specified in the publication
0.18
spermidine
wild-type, pH not specified in the publication, temperature not specified in the publication
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.141
(R)-3-methylspermidine
pH and temperature not specified in the publication
0.019
(S)-3-methylspermidine
pH and temperature not specified in the publication
0.01
N1-guanyl-1,7-diaminoheptane
-
pH and temperature not specified in the publication
additional information
additional information
inhibition profile in a series of kinetic experiments
-
additional information
additional information
-
inhibition profile in a series of kinetic experiments
-
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IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.000062
6-bromo-N-(1H-indol-4-yl)-1-benzothiophene-2-carboxamide
Homo sapiens
pH 8.0, 23°C
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.0000096
low specific activity of DHS34 could be due to the fact that one of the NAD+ binding regions in the DHS34 is present in the big long insertion when compared with human deoxyhypusine synthase
additional information
additional information
-
the recombinant DHSL20 protein does not show any activity
additional information
the recombinant DHSL20 protein does not show any activity
additional information
-
the recombinant protein shows significant deoxyhypusine synthase activity
additional information
the recombinant protein shows significant deoxyhypusine synthase activity
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
9.2
9.5
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
8.5 - 11
-
pH 8.5: about 45% of maximal activity, pH 11.0: about 50% of maximal activity
8.8 - 9.9
pH 8.8: about 35% of maximal activity, pH 9.9: about 60% of maximal activity
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
37
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
20 - 37
-
20°C: about 75% of maximal activity, 37°C: about 25% of maximal activity
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pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
DHS34; DHSL20 is a DHS-like gene from chromosome 20 and DHS34, a DHS gene from chromosome 34
SwissProt
brenda
Trypanosoma brucei brucei 927 / 4 GUTat10.1 / TREU927
Q38BX0 i.e. catalytic subunit DHSc, Q4GZD1 i.e. regulatory subunit DHSp
UniProt
brenda
-
638068, 638069, 638070, 638071, 638073, 638079, 638081, 638082, 638083, 658627, 716821, 721265, 722424, 723106, 723584
-
-
brenda
DHS34; DHSL20 is a DHS-like gene from chromosome 20 and DHS34, a DHS gene from chromosome 34
SwissProt
brenda
two putative deoxyhypusine synthase sequences are identified in the Leishmania donovani genome
-
-
brenda
two putative deoxyhypusine synthase sequences are identified in the Leishmania donovani genome
SwissProt
brenda
-
-
-
brenda
Q38BX0 i.e. catalytic subunit DHSc, Q4GZD1 i.e. regulatory subunit DHSp
UniProt
brenda
Trypanosoma brucei brucei 927 / 4 GUTat10.1 / TREU927
gene Tb10.70.4900
UniProt
brenda
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
DHS is ubiquitously expressed in primary mouse cells and murine cell lines
brenda
SpeY accumulates in vegetative cells but also at significant levels in heterocysts
brenda
SpeY accumulates in vegetative cells but also at significant levels in heterocysts
brenda
additional information
additional information
-
DHS is ubiquitously expressed in CD34+ cellss from patients with chronic myeloid leukemia and acute myeloid leukemia
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
of clonal transgenic parasites with integration of glmS riboswitch downstream of the DHS gene
brenda
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
malfunction
metabolism
physiological function
additional information
evolution
CpDHS is more closely related to apicomplexan and human DHS than to kinetoplast DHS
evolution
-
homospermidine synthase, HSS, EC 2.5.1.44/45, evolved from the gene encoding deoxyhypusine synthase, DHS, by gene duplication. HSS and deoxyhypusine synthase have also diverged with respect to their regulation
evolution
-
homospermidine synthase, HSS, EC 2.5.1.44/45, evolved from the gene encoding deoxyhypusine synthase, DHS, by gene duplication. HSS and deoxyhypusine synthase have also diverged with respect to their regulation
evolution
-
homospermidine synthase, HSS, EC 2.5.1.44/45, evolved from the gene encoding deoxyhypusine synthase, DHS, by gene duplication. HSS and deoxyhypusine synthase have also diverged with respect to their regulation
evolution
-
homospermidine synthase, HSS, EC 2.5.1.44/45, evolved from the gene encoding deoxyhypusine synthase, DHS, by gene duplication. HSS and deoxyhypusine synthase have also diverged with respect to their regulation
evolution
-
homospermidine synthase, HSS, EC 2.5.1.44/45, evolved from the gene encoding deoxyhypusine synthase, DHS, by gene duplication. HSS and deoxyhypusine synthase have also diverged with respect to their regulation
evolution
-
homospermidine synthase, HSS, EC 2.5.1.44/45, evolved from the gene encoding deoxyhypusine synthase, DHS, by gene duplication. HSS and deoxyhypusine synthase have also diverged with respect to their regulation
evolution
-
homospermidine synthase, HSS, EC 2.5.1.44/45, evolved from the gene encoding deoxyhypusine synthase, DHS, by gene duplication. HSS and deoxyhypusine synthase have also diverged with respect to their regulation
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
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
malfunction
DHSL20 lacks the catalytic lysine residue at residue 344, which is indispensable for the enzymatic reaction and is present in the active center for catalysis, and contains leucine instead
malfunction
gene deletion mutations are attempted via targeted gene replacement. Chromosomal null mutants of DHS34 could only be obtained in the presence of a DHS34-containing episome, indicating that DHS34 is an essential gene
malfunction
-
deoxyhypusine synthase haploinsufficiency attenuates acute cytokine signaling, overview. DHS dysfunction in the setting of diabetes mellitus, overview
malfunction
-
inhibition of DHS by GC7 induces antiproliferative effects in vitro. GC7 treatment induces premature senescence in U87-MG cells, co-treatment of glioblastoma cells with TMZ/BCNU and GC7 has an additive antiproliferative effect
malfunction
-
inhibition of proliferation of BA/F3 p210 cells including the imatinib resistant mutants M351T, E255K, and T315I by deoxyhypusine synthase inhibitors
malfunction
-
severe effects of knockout of Eif5a gene or Dhps gene in mice in cell lines RRE174 with Eif5a disruption and RRM039 with Dhps disruption, Eif5a heterozygous knockout mice and Dhps heterozygous knockout mice are viable and fertile, but, homozygous Eif5a1gt/gt embryos and Dhpsgt/gt embryos die early in embryonic development. Upon transfer to in vitro culture, homozygous Eif5agt/gt or Dhpsgt/gt blastocysts at E3.5 show growth defects when compared to heterozygous or wild-type blastocysts
malfunction
DHS enzyme inhibition by N1-guanyl-1,7-diaminoheptane results in a significant decrease in tumor formation in vivo. In patients with esophageal squamous cell carcinoma, overexpression of gene DHPS in ESCC tumors is significantly associated with worse recurrence-free survival, and correlated with distant metastasis. Although the mRNA levels of RhoA in DHPS-knockdown cells do not change, RhoA protein levels significantly decrease compared with control
malfunction
early flowering phenotype of dexamethasone-treated siDHS knockout transgenic plants, hypersensitivityof siDHS transgenic plants to osmotic stressors and abscisic acid. The sensitivity of transgenic siDHS plantsto abscisic acid in the absence of the silencing drug dexamethasone probably reflects that the genetic inactivation system is slightly leaky and that minor inactivation of the eIF5A pathway is very sensitive to alterations in abscisic acid homeostasis. Non-silenced siDHS plants display partial growth inhibition under salt treatment. Alterations in root cell expansion and root hair phenotypes caused by DHS silencing, overview
malfunction
importance of imbalances in eIF5A hypusination in Fusarium graminearum: overexpression of gene DHS leads to increased virulence in Triticum aestivum, elevated production of the mycotoxin deoxynivalenol, more infection structures, faster Triticum aestivum tissue invasion in plants and increases vegetatively produced conidia. Overexpression of the enzyme DOHH completely prevents infection structure formation, pathogenicity in Triticum aestivum and Zea mays, leads to overproduction of reactive oxygen species, reduced DON mycotoxin production and increased sexual reproduction. Simultaneous overexpression of both genes restores wild type-like phenotypes, strongly increased hypusinated eIF5A in DOHH overexpression mutant in comparison to wild-type, and the DHS overexpression mutants
malfunction
-
the dys1-1 mutant shows a strong depletion of mutated Dys1 protein, resulting in more than 2fold decrease in hypusine levels relative to the wild type. he growth phenotype of dys1-1 mutant is severe, growing only in the presence of 1 M sorbitol, an osmotic stabilizer, the sorbitol requirement from dys1-1 is not associated with cell lysis. The dys1-1 mutant genetically interacts with the sole yeast protein kinase C (Pkc1) and Asc1, a component of the 40S ribosomal subunit. The dys1-1 mutant is synthetically lethal in combination with asc1DELTA and overexpression of TIF51A (eIF5A) or DYS1 is toxic for an asc1DELTA strain. Inactive Pkc1 (K853R) form does not affect the dys1-1 mutant. Dys1-1 mutant phenotype, overview
malfunction
-
gene deletion mutations are attempted via targeted gene replacement. Chromosomal null mutants of DHS34 could only be obtained in the presence of a DHS34-containing episome, indicating that DHS34 is an essential gene
-
malfunction
-
deoxyhypusine synthase haploinsufficiency attenuates acute cytokine signaling, overview. DHS dysfunction in the setting of diabetes mellitus, overview
-
malfunction
-
severe effects of knockout of Eif5a gene or Dhps gene in mice in cell lines RRE174 with Eif5a disruption and RRM039 with Dhps disruption, Eif5a heterozygous knockout mice and Dhps heterozygous knockout mice are viable and fertile, but, homozygous Eif5a1gt/gt embryos and Dhpsgt/gt embryos die early in embryonic development. Upon transfer to in vitro culture, homozygous Eif5agt/gt or Dhpsgt/gt blastocysts at E3.5 show growth defects when compared to heterozygous or wild-type blastocysts
-
malfunction
-
early flowering phenotype of dexamethasone-treated siDHS knockout transgenic plants, hypersensitivityof siDHS transgenic plants to osmotic stressors and abscisic acid. The sensitivity of transgenic siDHS plantsto abscisic acid in the absence of the silencing drug dexamethasone probably reflects that the genetic inactivation system is slightly leaky and that minor inactivation of the eIF5A pathway is very sensitive to alterations in abscisic acid homeostasis. Non-silenced siDHS plants display partial growth inhibition under salt treatment. Alterations in root cell expansion and root hair phenotypes caused by DHS silencing, overview
-
metabolism
-
deoxyhypusine synthase catalyzes a step in hypusine sythesis, a unique mmoified lysine derivative of eukaryotic translation initiation factor 5A, eIF5A
metabolism
-
the functions of Asc1 associated with protein synthesis are necessary in the absence of wild type levels of hypusine-containing eIF5A in the cell
metabolism
the enzyme is involved in synthesis of synthesis homospermidine
physiological function
-
deoxyhypusine synthase catalyzes the synthesis of deoxyhypusine [N?-(4-aminobutyl)-lysine], the first step in the post-translational synthesis of an unusual amino acid hypusine [N?-(4-amino-2-hydroxybutyl)-lysine]
physiological function
deoxyhypusine synthase, an NAD+-dependent enzyme, catalyzes the first step in the post-translational synthesis of an unusual amino acid, hypusine (N-(4-amino-2-hydroxybutyl)lysine), in the eukaryotic initiation factor 5A precursor protein, DHS34 is essential for Leishmania donovani
physiological function
-
deoxyhypusine synthase, DHS, catalyzes the post-translational formation of the amino acid hypusine. Hypusine is unique to the eukaryotic translational initiation factor 5A (eIF5A), and is required for its functions in mRNA shuttling, translational elongation and stress granule formation. DHS promotes cytokine and ER stress signaling in the islet beta cell and thereby contributes to its dysfunction in the setting of diabetes mellitus
physiological function
-
eukaryotic translation initiation factor 5A, eIF5A, is a small acidic protein and the only cellular protein that contains the unique modified lysine, hypusine [N1-(4-amino-2-hydroxybutyl)lysine]. Hypusine is formed by the post-translational modification of one specific lysine residue of the eIF5A precursor, eIF5A(Lys), in two consecutive enzymatic steps. The first enzyme, deoxyhypusine synthase, DHS, catalyzes the transfer of the aminobutyl moiety from the polyamine spermidine to form an intermediate, deoxyhypusine [N1-(4-aminobutyl)lysine] residue, which is subsequently hydroxylated by deoxyhypusine hydroxylase
physiological function
-
hypusine is formed posttranslationally by the addition of the 4-aminobutyl moiety from the polyamine spermidine to a specific lysine residue, catalyzed by deoxyhypusine synthase, DHPS, and subsequent hydroxylation by deoxyhypusine hydroxylase, DOHH. Essential role of eIF5A-1 and deoxyhypusine synthase in mouse embryonic development, overview
physiological function
-
hypusine modification is an irreversible protein modification and naturally occurring eIF5A exists predominantly as the hypusinated form. Deoxyhypusine synthase catalyzes the transfer of the aminobutyl moiety from spermidine to a specific lysine of the eIF5A precursor to form the deoxyhypusine [N?-(4-aminobutyl)lysine] intermediate. Hypusine is formed from deoxyhypusine by the action of EC 1.14.99.29, deoxyhypusine monooxygenase
physiological function
activation of eukaryotic translation initiation factor eIF5A requires a posttranslational modification, forming the unique amino acid hypusine. This activation is mediated by two enzymes, deoxyhypusine synthase, DHS, and deoxyhypusine hydroxylase, DOHH. Enzyme DHS catalyzes eIF5A Lys56 hypusination and is essential in Fusarium graminearum
physiological function
hypusination of eIF5A is an important post-translational modification essential for cell proliferation. This modification occurs in a two step processcatalyzed by deoxyhypusine synthase followed by deoxyhypusine hydroxylase
physiological function
hypusine is formed from spermidine, a metabolite of polyamine metabolism, by the sequential action of two catalytic enzymes, deoxyhypusine synthase (DHPS) and deoxyhypusine hydroxylase (DOHH). These enzymes have an important role in post-translational modification of eukaryotic translation factor 5A (eIF5A), which functions in protein synthesis. The hypusine cascade contributes to cell proliferation and embryogenesis by the regulation of translation elongation in healthy cells. DHPS-mediated hypusine-modification of eukaryotic translation factor 5A facilitates the translation of RhoA, resulting in the activation of the RhoA signaling pathway and leading to not only increased cell motility, invasion and metastasis of cancer cells in vitro, but also increased tumor growth in vivo. DHPS regulates the expression and activation of RhoA, DHPS may regulate the organization of F-actin through the increase in RhoA protein level. Hypusinated eIF5A may regulate tumor growth and metastasis via the RhoA signaling pathway
physiological function
the enzyme deoxyhypusine synthase is required for spermidine-dependent hypusine modification of a lysine residue in the essential translation factor eIF5A. Enzyme DHS is essential for infectivity of Trypanosoma brucei in mice
physiological function
the enzyme is required for spermidine-mediated activation of eIF5A by hypusination. Activated elF5A is involved in several aspects of plant biology such as the control of flowering time, the aerial and root architecture, and root hair growth. In addition, the pathway is required for adaptation to challenging growth conditions such as high salt and high glucose medium and to elevated concentrations of the plant hormone abscisic acid
physiological function
the eukaryotic translation initiation factor 5A (eIF5A) is essential for cell proliferation, becoming functionally active only after post-translational conversion of a specific Lys to hypusine catalyzed by deoxyhypusine synthase, the rate-limiting enzyme of this two-step process
physiological function
the plant stress hormone abscisic acid causes a reduction in the hypusination of eIF5A1 probably through the post-transcriptional alteration of DHS activity
physiological function
-
translation factor eIF5A undergoes an essential and conserved posttranslational modification at a specific lysine, K51, to generate the residue hypusine. The enzymes deoxyhypusine synthase (Dys1) and deoxyhypusine hydroxylase (Lia1) catalyze this two-step modification process. Correlated role for eIF5A and Asc1 in coordinating the translational control of a subset of mRNAs associated with cell integrity
physiological function
translation elongation factor aIF5A is hypusinated and also forms a stable complex with deoxyhypusine synthase
physiological function
clonal transgenic parasites with integration of glmS riboswitch downstream of the DHS gene show DHS protein in the cytoplasm of in asexual stages. The DHS protein can be attenuated fivefold in transgenic parasites with an active riboswitch. Attenuation of DHS expression for 72 h leads to a significant reduction of hypusinated protein, while global protein synthesis is unaffected. Parasites with attenuated DHS expression show a significant growth defect. DHS-attenuated parasites show increased sensitivity to inhibitor N1-guanyl-1,7-diaminoheptane
physiological function
in a mouse model that enables the inducible, postnatal deletion of Dhps specifically in postnatal islet beta cells, removal of Dhps does not have an effect under normal physiologic conditions. Upon development of insulin resistance, which induces beta-cell proliferation, Dhps deletion causes alterations in proteins required for mRNA translation and protein secretion, reduced production of the cell cycle molecule cyclin D2, impaired beta-cell proliferation, and induces overt diabetes. Hypusine biosynthesis is downstream of protein kinase C-zeta and is required for c-Myc-induced proliferation
physiological function
-
virus-mediated PhDHS silencing causes a sectored chlorotic leaf phenotype. Chlorophyll levels and photosystem II activity are reduced, and chloroplast development is abnormal in DHS-silenced leaves. Silencing results in extended leaf longevity and thick leaves. 308 proteins are upregulated and 266 proteins are downregulated in DHS-silenced plants compared with control. The mRNA level of eIF5A-1 significantly decreases in DHS-silenced plants, while those of another three eIF5As are not significantly affected
physiological function
-
deoxyhypusine synthase, an NAD+-dependent enzyme, catalyzes the first step in the post-translational synthesis of an unusual amino acid, hypusine (N-(4-amino-2-hydroxybutyl)lysine), in the eukaryotic initiation factor 5A precursor protein, DHS34 is essential for Leishmania donovani
-
physiological function
-
deoxyhypusine synthase, DHS, catalyzes the post-translational formation of the amino acid hypusine. Hypusine is unique to the eukaryotic translational initiation factor 5A (eIF5A), and is required for its functions in mRNA shuttling, translational elongation and stress granule formation. DHS promotes cytokine and ER stress signaling in the islet beta cell and thereby contributes to its dysfunction in the setting of diabetes mellitus
-
physiological function
-
hypusine is formed posttranslationally by the addition of the 4-aminobutyl moiety from the polyamine spermidine to a specific lysine residue, catalyzed by deoxyhypusine synthase, DHPS, and subsequent hydroxylation by deoxyhypusine hydroxylase, DOHH. Essential role of eIF5A-1 and deoxyhypusine synthase in mouse embryonic development, overview
-
physiological function
-
the plant stress hormone abscisic acid causes a reduction in the hypusination of eIF5A1 probably through the post-transcriptional alteration of DHS activity
-
physiological function
-
the enzyme is required for spermidine-mediated activation of eIF5A by hypusination. Activated elF5A is involved in several aspects of plant biology such as the control of flowering time, the aerial and root architecture, and root hair growth. In addition, the pathway is required for adaptation to challenging growth conditions such as high salt and high glucose medium and to elevated concentrations of the plant hormone abscisic acid
-
physiological function
-
translation elongation factor aIF5A is hypusinated and also forms a stable complex with deoxyhypusine synthase
-
physiological function
Trypanosoma brucei brucei 927 / 4 GUTat10.1 / TREU927
-
the enzyme deoxyhypusine synthase is required for spermidine-dependent hypusine modification of a lysine residue in the essential translation factor eIF5A. Enzyme DHS is essential for infectivity of Trypanosoma brucei in mice
-
additional information
-
Dhps heterozygosity does not lead to significant inhibition of proliferation or cell cycle progression, Dhps heterozygosity does not alter growth or metabolic homeostasis, overview
additional information
-
inhibition of eIF5A by siRNA or DHS-inhibitors in combination with Imatinib exerts synergistic cytotoxic effects on BCR-ABL positive cell lines
additional information
enzyme structure modelling, model evaluation and comparative structural analysis, overview
additional information
-
enzyme structure modelling, model evaluation and comparative structural analysis, overview
additional information
structural comparison of the three-dimensional structure of Theileria parva DHS with Homo sapiens DHS
additional information
-
structural comparison of the three-dimensional structure of Theileria parva DHS with Homo sapiens DHS
additional information
-
the Convulvulaceae species Ipomoea hederifolia contains ipanguline- and triangularine-type polyamines
additional information
-
the Convulvulaceae species Ipomoea meyeri contains triangularine-type polyamines
additional information
-
the Convulvulaceae species Ipomoea neei contains ipanguline-type polyamines
additional information
-
the Convulvulaceae species Merremia quinquefolia contains lycopsamine-type polyamines
additional information
the inability of racemic 3-methylspermidine and (S)-3-methylspermidine to support DU-145 cells growth due to the fact that only the (R)-isomer is a substrate of DHS, but this isomer, (R)-3-methylspermidine, competes with spermidine for cellular uptake and is less efficient than the (S)-3-methylspermidine, which results in accumulation of inactive (S)-3-methylspermidine in the cell. Synthesis of (S)-3-methylspermidine and (R)-3-methylspermidine, overview
additional information
Trypanosoma brucei encodes two deoxyhypusine synthase isozymes TbDHSc and TbDHSp that form a functional complex
additional information
Trypanosoma brucei encodes two deoxyhypusine synthase isozymes TbDHSc and TbDHSp that form a functional complex
additional information
Trypanosoma brucei encodes two deoxyhypusine synthase isozymes TbDHSc and TbDHSp that form a functional heterotetrameric complex
additional information
Trypanosoma brucei encodes two deoxyhypusine synthase isozymes TbDHSc and TbDHSp that form a functional heterotetrameric complex
additional information
-
structural modeling of DHS34, overview
-
additional information
-
Dhps heterozygosity does not lead to significant inhibition of proliferation or cell cycle progression, Dhps heterozygosity does not alter growth or metabolic homeostasis, overview
-
additional information
-
structural comparison of the three-dimensional structure of Theileria parva DHS with Homo sapiens DHS
-
additional information
Trypanosoma brucei brucei 927 / 4 GUTat10.1 / TREU927
-
Trypanosoma brucei encodes two deoxyhypusine synthase isozymes TbDHSc and TbDHSp that form a functional heterotetrameric complex
-
additional information
Trypanosoma brucei brucei 927 / 4 GUTat10.1 / TREU927
-
Trypanosoma brucei encodes two deoxyhypusine synthase isozymes TbDHSc and TbDHSp that form a functional complex
-
Show AA Sequence and Transmembrane Helices (3209 entries)
Please use the AA Sequence and Transmembrane Helices Search for a specific query.
Please use the AA Sequence and Transmembrane Helices Search for a specific query.
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
137000
165000 - 172000
-
gel filtration sedimentation equilibrium centrifugation
180000
40800
41000
42200
42300
43000
48000
73000
2 * 66000, about, DHS34, sequence calculation, 2 * 73000, recombinant His-tagged DHS34, SDS-PAGE
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
homotetramer
tetramer
additional information
dimer
2 * 66000, about, DHS34, sequence calculation, 2 * 73000, recombinant His-tagged DHS34, SDS-PAGE
dimer
-
2 * 66000, about, DHS34, sequence calculation, 2 * 73000, recombinant His-tagged DHS34, SDS-PAGE
-
homotetramer
4 * 41000, recombinant enzyme, SDS-PAGE, 4 * 41260, about, sequence calculation
homotetramer
-
4 * 41000, recombinant enzyme, SDS-PAGE, 4 * 41260, about, sequence calculation
-
tetramer
4 * 35050, calculated from sequence, 4 * 35000, SDS-PAGE
tetramer
-
4 * 35050, calculated from sequence, 4 * 35000, SDS-PAGE
-
additional information
-
structural modeling of DHS34, overview
-
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POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
phosphoprotein
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
at 2.2 A a new form II crystal of the deoxyhypusine synthase:NAD holoenzyme is grown at low ionic strength and pH 8.0, near the optimal pH for enzymatic activity
in complex with inhibitors 6-bromo-N-(1H-indol-4-yl)-1-benzothiophene-2-carboxamide and N''-guanyl-1,7-diaminoheptane. Presence of 6-bromo-N-(1H-indol-4-yl)-1-benzothiophene-2-carboxamide induces a dramatic conformational change in DHPS
structures of the apoprotein, as well as ligand-bound states at 1.41 to 1.69 A resolution. Polyamines namely spermine and putrescine bind DHS in a similar manner as spermidine. Spermine may to some extent serve as an alternative DHS substrate. No conformational changes occur in the DHS structure upon spermidine binding. A conserved ball-and-chain motif is indispensable to assembling a functional DHS tetramer
vapor diffusion in hanging drops, crystal structure of the enzyme-NAD complex at 2.2 A resolution
-
heterotetramer, to 3.5 A resolution. The activity is dependent on heterotetramer formation between paralogs DHSc and DHSp. The X-ray structure of DHS shows a single functional shared active site formed at the DHSc/DHSp heterodimer interface. Deficiencies in one subunit are complemented by the other
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
H288A
N173S
recurrent missense variant identified with likely gene disrupting variant (c.1014+1G>A, c.912_917delTTACAT [p.Tyr305_Ile306del]), or c.1A>G [p.Met1] in unrelated individuals having similar neurodevelopmental features that include global developmental delay and seizures. Two of four affected females have short stature. The c.1014+1G>A variant causes aberrant splicing. Recombinant p.Asn173Ser or p.Tyr305_Ile306del protein show reduced (20%) or absent in vitro activity, respectively. The p.Tyr305_Ile306del and p.Asn173Ser variants result in reduced hypusination of eIF5A compared to wild-type DHPS enzyme
L344K
mutant enzyme is still devoid of any DHS activity, suggesting that other differences in amino acid sequences also contribute to its inactivity
D314A
site-directed mutagenesis, the mutant is active as deoxyhypusine synthase, but inactive as deoxyhypusine hydroxylase
H313A
site-directed mutagenesis, the mutant is active as deoxyhypusine synthase, but inactive as deoxyhypusine hydroxylase
D314A
-
site-directed mutagenesis, the mutant is active as deoxyhypusine synthase, but inactive as deoxyhypusine hydroxylase
-
H313A
-
site-directed mutagenesis, the mutant is active as deoxyhypusine synthase, but inactive as deoxyhypusine hydroxylase
-
D218A
mutation in catalytic site of subunit DHSp, mutant is unable to catalyze the single-turnover formation of NADH
D405A
mutation in catalytic site of subunit DHSc, impaired in activity
E103A
mutation in catalytic site of subunit DHSp, impaired in activity
E104A
mutation in catalytic site of subunit DHSp, impaired in activity
E166A
mutation in dead site of subunit DHSc, activity is similar to wild-type. The heterotetrameric complex shows a decrease in melting temperature by 4.9 degrees
H266A
mutation in dead site of subunit DHSp, activity is similar to wild-type
D218A
-
mutation in catalytic site of subunit DHSp, mutant is unable to catalyze the single-turnover formation of NADH
-
D405A
-
mutation in catalytic site of subunit DHSc, impaired in activity
-
E103A
-
mutation in catalytic site of subunit DHSp, impaired in activity
-
H266A
-
mutation in dead site of subunit DHSp, activity is similar to wild-type
-
additional information
additional information
generation of deoxyhypusine synthase knockout mutants using siRNA via Agrobacterium strainGV3101/pMP90 transfection in Arabidopsis thaliana
additional information
-
generation of deoxyhypusine synthase knockout mutants using siRNA via Agrobacterium strainGV3101/pMP90 transfection in Arabidopsis thaliana
additional information
-
generation of deoxyhypusine synthase knockout mutants using siRNA via Agrobacterium strainGV3101/pMP90 transfection in Arabidopsis thaliana
-
additional information
replacement of the endogenous DHS and DOHH genes by homologous recombination with the PgpdA-DHS or Pgpd1-DOHH alleles, excluding any possibility of mutagenic effects by ectopic integration
additional information
-
replacement of the endogenous DHS and DOHH genes by homologous recombination with the PgpdA-DHS or Pgpd1-DOHH alleles, excluding any possibility of mutagenic effects by ectopic integration
additional information
variant recombinant proteins with i. a truncation of 48 or 97 NH2-terminal amino acids, ii. A truncation of 39 COOH-terminal amino acids, or iii. An internal deletion (ASp262-Ser317) are inactive. A chimeric protein consisting of the complete human sequence and 16 amino acids of the yeast sequence, Gln197-Asn212, not present in the human enzyme, inserted between Glu193 and Gln194 exhibit moderate activity
additional information
-
variant recombinant proteins with i. a truncation of 48 or 97 NH2-terminal amino acids, ii. A truncation of 39 COOH-terminal amino acids, or iii. An internal deletion (ASp262-Ser317) are inactive. A chimeric protein consisting of the complete human sequence and 16 amino acids of the yeast sequence, Gln197-Asn212, not present in the human enzyme, inserted between Glu193 and Gln194 exhibit moderate activity
additional information
-
DHS knock-down by stable lentiviral expression of shRNAs in G55T2 and U87-MG cells
additional information
DHPS gene silencing by transfection of DHPS-specific short hairpin RNA (shRNA) in LM-pGL4.5 cells
additional information
-
DHPS gene silencing by transfection of DHPS-specific short hairpin RNA (shRNA) in LM-pGL4.5 cells
additional information
during purification and crystallization, residue C177 is is covalently modified to a 2-mercaptoethanol adduct
additional information
-
during purification and crystallization, residue C177 is is covalently modified to a 2-mercaptoethanol adduct
additional information
-
DHS34 gene deletion mutations via targeted gene replacement, chromosomal null mutants of DHS34 are only obtained in the presence of a DHS34-containing episome. HYGDELTAdhs34 and PHLEODELLTAdhs34 gene replacement cassettes are individually transfected into wild-type parasites, phenotypes, verview
additional information
DHS34 gene deletion mutations via targeted gene replacement, chromosomal null mutants of DHS34 are only obtained in the presence of a DHS34-containing episome. HYGDELTAdhs34 and PHLEODELLTAdhs34 gene replacement cassettes are individually transfected into wild-type parasites, phenotypes, verview
additional information
-
DHS34 gene deletion mutations via targeted gene replacement, chromosomal null mutants of DHS34 are only obtained in the presence of a DHS34-containing episome. HYGDELTAdhs34 and PHLEODELLTAdhs34 gene replacement cassettes are individually transfected into wild-type parasites, phenotypes, verview
-
additional information
-
construction of heterozygous or homozygous knockout mice via stem cell lines, phenotypes, overview
additional information
-
construction of heterozygous or homozygous knockout mice via stem cell lines, phenotypes, overview
-
additional information
-
generation of the dys1-1 mutant that has a defect in total protein synthesis, a defect in polysome profile indicative of a translation elongation defect and a reduced association of eIF5A with polysomes
additional information
generation of a knockout mutant by gene replacement
additional information
generation of a knockout mutant by gene replacement
additional information
mutation of sets of matched pairs, where the same residue is changed in both the catalytic and dead site, melting temperature of mutants is similar to wild-type
additional information
Trypanosoma brucei brucei 927 / 4 GUTat10.1 / TREU927
-
generation of a knockout mutant by gene replacement
-
additional information
-
mutation of sets of matched pairs, where the same residue is changed in both the catalytic and dead site, melting temperature of mutants is similar to wild-type
-
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
freeze-thawing of the partially purified enzyme inactivates, no stabilization by glycerol
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant enzyme
recombinant His-tagged DHSL20 and DHS34 from Escherichia coli by metal affinity chromatography
recombinant His-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography and desalting gel filtration
recombinant His-tagged enzyme from Escherichia coli strain BL21(DE3) to homogeneity by nickel affinity chromatography
recombinant His-tagged enzyme from Escherichia coli strain BL21-CodonPlus (DE3) by nickel affinity chromatography and ultrafiltration, followed by cleavage of the His-tag through protease 3C and elimination via affinity chromatography
recombinant His6-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography and gel filtration
recombinant His6-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity cromatography and gel filtration
recombinant soluble His-tagged enzyme from Escherichia coli strain Rosetta (DE3)
using Ni-NTA chromatography
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
DHS DNA and amino acid seuence determination and analysis, functional coexpression with human deoxyhypusine hydroxylase and human eukaryotic translation initiation factor 5A in Escherichia coli strain BL21(DE3)pLys that produces eIF5A(Hpu), overview
-
DHS gene, DNA and amino acid sequence determination and analysis
DHSL20 is a DHS-like gene from chromosome 20 and DHS34, a DHS gene from chromosome 34, DNA and amino acid sequence determination and analysis, sequence comparisons and phylogenetic analysis, expression of His-tagged DHSL20 and DHS34 in Escherichia coli
expressed as a C-terminal his-tagged fusion protein
expression in Escherichia coli
expression in Escherichia coli, the deduced amino acid sequence shows a high degree of identity to that of yeast enzyme and to the known sequences of tryptic peptides from the rat and Neurospora enzymes
gene DHPS, DHPS is a metastasis-associated gene within the specific amplification at chromosome 19p13.2p13.13 in HOC313-LM cells, quantitative RT-PCR expressionanalysis
gene DHS, DNA and amino acid sequence determination and analysis, sequence comparisons and phylogenetic analysis, recombinant expression of His-tagged enzyme in Escherichia coli strain BL21(DE3)
gene DHS, located on chromosome 2, DNA and amino acid sequence determination and analysis, sequence comparisons, recombinant expression of soluble His-tagged enzyme in Escherichia coli strain Rosetta (DE3)
gene dhs, recombinant expression of His-tagged enzyme in Escherichia coli strain BL21-CodonPlus (DE3), coexpression with His-tagged DOHH (deoxyhypusine hydroxylase) in Escherichia coli strain BL21-CodonPlus (DE3), quantitative real-time PCR expression analysis
gene dhs, single-copy gene, DNA and amino acid sequence determination and analysis, sequence comparisons and phylogenetic analysis, analysis of gene duplications in Convolvulaceae species
gene DHS, targeted enzyme overexpression in Fusarium graminearum by single crossover event inserting the linearized vector pMW-DHS
gene Tb10.70.4900, DNA and amino acid sequence determination and analysis, sequence comparisons, phylogenetic analysis, recombinant expression of N-terminally His6-tagged enzyme in Escherichia coli strain BL21 (DE3), coexpression with gene TB927.1.870 results in heterotetramer formation with a 3000fold increase in enzyme activity
gene TB927.1.870, DNA and amino acid sequence determination and analysis, sequence comparisons, phylogenetic analysis, recombinant expression of N-terminally His6-tagged enzyme in Escherichia coli strain BL21 (DE3), coexpression with gene Tb10.70.4900 in Escherichia coli strain BL21 (DE3) results in heterotetramer formation with a 3000fold increase in enzyme activity
gene TvDHS, DNA and amino acid sequence determination and analysis, genetic organization, sequence comparisons and phylogenetic tree, recombinant expression of His-tagged enzyme in Escherichia coli strain BL21(DE3), coexpression with recombinant TveIF-5A (rTveIF-5A) precursor protein and formation of a TvDHS-TveIF-5A complex
subcloning of bovine and human DHS gene, overexpression in Escherichia coli
transgenic canola lines with suppressed DHS expression were obtained by introducing a transgene expressing antisense 3'-UTR canola deoxyhypusine synthase cDNA under the regulation of the constitutive cauliflower mosaic virus 35S (CaMV-35S) promoter
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gene dhs, single-copy gene, DNA and amino acid sequence determination and analysis, sequence comparisons and phylogenetic analysis, analysis of gene duplications in Convolvulaceae species
-
gene dhs, single-copy gene, DNA and amino acid sequence determination and analysis, sequence comparisons and phylogenetic analysis, analysis of gene duplications in Convolvulaceae species
-
gene dhs, single-copy gene, DNA and amino acid sequence determination and analysis, sequence comparisons and phylogenetic analysis, analysis of gene duplications in Convolvulaceae species
-
gene dhs, single-copy gene, DNA and amino acid sequence determination and analysis, sequence comparisons and phylogenetic analysis, analysis of gene duplications in Convolvulaceae species
-
gene dhs, single-copy gene, DNA and amino acid sequence determination and analysis, sequence comparisons and phylogenetic analysis, analysis of gene duplications in Convolvulaceae species
-
gene dhs, single-copy gene, DNA and amino acid sequence determination and analysis, sequence comparisons and phylogenetic analysis, analysis of gene duplications in Convolvulaceae species
-
gene dhs, single-copy gene, DNA and amino acid sequence determination and analysis, sequence comparisons and phylogenetic analysis, analysis of gene duplications in Convolvulaceae species
-
subcloning of bovine and human DHS gene, overexpression in Escherichia coli
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
analysis
DHS activity can be determined by coupling the first phase reaction with the NADH-Glo assay in which the generation of luminescence is dependent on NADH derived from the DHS partial reaction. The non-radioactive DHS/NADH-Glo coupled assay is highly specific, sensitive and reproducible and can be configured for high throughput screening of small molecule libraries
drug development
medicine
drug development
-
fungal DHS is a target for the development of inhibitors, for which CNI-1493 may serve as a lead substance
drug development
Cryptosporidium parvum DHS is a traget for drug development, as GC7 effectively inhibits parasite infection and growth in cultured host cells
drug development
-
fungal DHS is a target for the development of inhibitors, for which CNI-1493 may serve as a lead substance
-
medicine
elevated mRNA levels of the target enzymes deoxyhypusine synthase (DHPS) and ornithine decarboxylase (ODC) correlate with poor prognosis in a large cohort of neuroblastoma tumors. The DHPS inhibitor GC7 (N1-guanyl-1,7-diaminoheptane) and the ODC inhibitor alpha-difluoromethylornithine (DFMO) are target-specific and in combination induce synergistic effects in neuroblastomas at concentrations that are not individually cytotoxic. The drug combination induces caspase 3/7/9, but not caspase 8-mediated apoptosis, in neuroblastoma cells. Hypusinated eIF5A levels and intracellular spermidine levels correlate directly with drug treatments
medicine
in a transgenic mouse model of type 1 diabetes, in which human GAD65 is expressed in pancreatic beta-cells, and human MHC-II is expressed on antigen presenting cells, deoxyhypusine synthase inhibitor N''-guanyl-1,7-diaminoheptane, i.e. GC7, alters the pathophysiology by catalyzing the crucial hypusination and the rate-limiting step of elF5A activation. Inhibition of eIF5A resets the proinflammatory bias in the pancreatic microenvironment. There is reduction of Th1/Th17 response, an increase in Treg numbers, debase in IL17 and IL21 cytokines levels in serum, lowering of anti-GAD65 antibodies, and ablation of the ER stress that improves functionality of the beta-cells, but minimal effect on the cytotoxic CD8 T-cell mediated response
medicine
recurrent missense variant p.Asn173Ser is identified with likely gene disrupting variant (c.1014+1G>A, c.912_917delTTACAT [p.Tyr305_Ile306del]), or c.1A>G [p.Met1?] in unrelated individuals having similar neurodevelopmental features that include global developmental delay and seizures. Two of four affected females have short stature. The c.1014+1G>A variant causes aberrant splicing. Recombinant p.Asn173Ser or p.Tyr305_Ile306del protein show reduced (20%) or absent in vitro activity, respectively. The p.Tyr305_Ile306del and p.Asn173Ser variants result in reduced hypusination of eIF5A compared to wild-type DHPS enzyme
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Wolff, E.C.; Park, M.H.; Folk, J.E.
Cleavage of spermidine as the first step in deoxyhypusine synthesis. The role of NAD+
J. Biol. Chem.
265
4793-4799
1990
Rattus norvegicus
brenda
Wolff, E.C.; Folk, J.E.; Park, M.H.
Enzyme-substrate intermediate formation at lysine 329 of human deoxyhypusine synthase
J. Biol. Chem.
272
15865-15871
1997
Homo sapiens
brenda
Chen, K.Y.; Liu, A.Y.C.
Biochemistry and function of hypusine formation on eukaryotic initiation factor 5A
Biol. Signals
6
105-109
1997
Homo sapiens, Neurospora crassa
brenda
Ober, D.; Hartmann, T.
Deoxyhypusine synthase from tobacco. cDNA isolation, characterization, and bacterial expression of an enzyme with extended substrate specificity
J. Biol. Chem.
274
32040-32047
1999
Nicotiana tabacum (Q9SC80), Nicotiana tabacum
brenda
Ober, D.; Hartmann, T.
Homospermidine synthase, the first pathway-specific enzyme of pyrrolizidine alkaloid biosynthesis, evolved form deoxyhypusine synthase
Proc. Natl. Acad. Sci. USA
96
14777-14782
1999
Senecio vernalis (Q9SC14), Senecio vernalis
brenda
Wolff, E.C.; Park, M.H.
Identification of lysine350 of yeast deoxyhypusine synthase as the site of enzyme intermediate formation
Yeast
15
43-50
1999
Saccharomyces cerevisiae
brenda
Wolff, E.C.; Wolff.J.; Park, M.H.
Deoxyhypusine synthase generates and uses bound NADH in a transient hydride transfer mechanism
J. Biol. Chem.
275
9170-9177
2000
Homo sapiens
brenda
Joe, Y.A.; Wolff, E.C.; Park, M.H.
Cloning and expression of human deoxyhypusine synthase cDNA: structure-function studies with the recombinant enzyme and mutant proteins
J. Biol. Chem.
270
22386-22392
1995
Homo sapiens (P49366), Homo sapiens
brenda
Tao, Y.; Chen, K.Y.
Molecular cloning and functional expression of Neurospora deoxyhypusine synthase cDNA and identification of yeast deoxyhypusine synthase cDNA
J. Biol. Chem.
270
23984-23987
1995
Saccharomyces cerevisiae, Neurospora crassa (P49365), Neurospora crassa
brenda
Wang, T.W.; Lu, L.; Wang, D.; Thompson, J.E.
Isolation and characterization of senescence-induced cDNAs encoding deoxyhypusine synthase and eucaryotic translation initiation factor 5A from tomato
J. Biol. Chem.
276
17541-17549
2001
Solanum lycopersicum (Q9AXR0), Solanum lycopersicum
brenda
Lee, C.H.; Um, P.Y.; Park, M.H.
Structure-function studies of human deoxyhypusine synthase: identification of amino acid residues critical for the binding of spermidine and NAD
Biochem. J.
355
841-849
2001
Homo sapiens
brenda
Lee, C.H.; Park, M.H.
Human deoxyhypusine synthase: interrelationship between binding of NAD and substrates
Biochem. J.
352
851-857
2000
Homo sapiens
-
brenda
Lee, Y.B.; Joe, Y.A.; Wolff, E.C.; Dimitriadis, E.K.; Park, M.H.
Complex formation between deoxyhypusine synthase and its protein substrate, the eukaryotic translation initiation factor 5A (eIF5A) precursor
Biochem. J.
340
273-281
1999
Homo sapiens
-
brenda
Liao, D.I.; Wolff, E.C.; Park, M.H.; Davies, D.R.
Crystal structure of the NAD complex of human deoxyhypusine synthase: an enzyme with a ball-and-chain mechanism for blocking the active site
Structure
6(1)
23-32
1998
Homo sapiens
-
brenda
Park, M.H.; Joe, Y.A.; Kang, K.R.
Deoxyhypusine synthase activity is essential for cell viability in the yeast Saccharomyces cerevisiae
J. Biol. Chem.
273
1677-1683
1998
Saccharomyces cerevisiae
brenda
Joe, Y.A.; Wolff, E.C.; Lee, Y.B.; Park, M.H.
Enzyme-substrate intermediate at a specific lysine residue is required for deoxyhypusine synthesis. The role of Lys329 in human deoxyhypusine synthase
J. Biol. Chem.
272
32679-32685
1997
Homo sapiens
brenda
Kang, K.R.; Wolff, E.C.; Park, M.H.; Folk, J.E.; Chung, S.I.
Identification of YHR068w in Saccharomyces cerevisiae chromosome VIII as a gene for deoxyhypusine synthase. Expression and characterization of the enzyme
J. Biol. Chem.
270
18408-18412
1995
Saccharomyces cerevisiae
brenda
Wolff, E.C.; Lee, Y.B.; Chung, S.I.; Folk, J.E.; Park, M.H.
Deoxyhypusine synthase from rat testis: purification and characterization
J. Biol. Chem.
270
8660-8666
1995
Rattus norvegicus
brenda
Jakus, J.; Wolff, E.C.; Park, M.H.; Folk, J.E.
Features of the spermidine-binding site of deoxyhypusine synthase as derived from inhibition studies. Effective inhibition by bis- and mono-guanylated diamines and polyamines
J. Biol. Chem.
268
13151-13159
1993
Rattus norvegicus
brenda
Abid, M.R.; Sasaki, K.; Titani, K.; Miyazaki, M.
Biochemical and immunological characterization of deoxyhypusine synthase purified from the yeast Saccharomyces carlsbergensis
J. Biochem.
121
769-778
1997
Saccharomyces cerevisiae
brenda
Abid, R.; Ueda, K.; Miyazaki, M.
Novel features of the functional site and expression of the yeast deoxyhypusine synthase
Biol. Signals
6
157-165
1997
Saccharomyces cerevisiae
brenda
Klier, H.; Csonga, R.; Steinkasserer, A.; Woehl, T.; Lottspeich, F.; Eder, J.
Purification and characterization of human deoxyhypusine synthase from HeLa cells
FEBS Lett.
364
207-210
1995
Homo sapiens
brenda
Ober, D.; Harms, R.; Witte, L.; Hartmann, T.
Molecular evolution by change of function. Alkaloid-specific homospermidine synthase retains all properties of deoxyhypusine synthase except binding the eIF5A precursor protein
J. Biol. Chem.
278
12805-12812
2003
Senecio vernalis (Q9SC14), Senecio vernalis
brenda
Kang, K.R.; Kim, J.S.; Chang, S.II; Park, M.H.; Kim, Y.W.; Lim, D.; Lee, S.Y.
Deoxyhypusine synthase is phosphorylated by protein kinase C in vivo as well as in vitro
Exp. Mol. Med.
34
489-495
2002
Saccharomyces cerevisiae, Gallus gallus, Cricetulus griseus, Homo sapiens
brenda
Lee, Y.; Kim, H.K.; Park, H.E.
Park, M.H.; Joe, Y.A.: Effect of N1-guanyl-1,7-diaminoheptane, an inhibitor of deoxyhypusine synthase, on endothelial cell growth, differentiation and apoptosis
Mol. Cell. Biochem.
237
69-76
2002
Homo sapiens
brenda
Park, J.H.; Wolff, E.C.; Folk, E.C.; Park, M.H.
Reversal of the deoxyhypusine synthesis reaction. Generation of spermidine or homospermidine from deoxyhypusine by deoxyhypusine synthase
J. Biol. Chem.
278
32683-32691
2003
Homo sapiens
brenda
Moll, S.; Anke, S.; Kahmann, U.; Hnsch, R.; Hartmann, T.; Ober, D.
Cell-specific expression of homospermidine synthase, the entry enzyme of the pyrrolizidine alkaloid pathway in Senecio vernalis, in comparison with its ancestor, deoxyhypusine synthase
Plant Physiol.
130
47-57
2002
Nicotiana tabacum, Senecio vernalis
brenda
Huang, J.K.; Tsai, S.; Huang, G.H.; Sershon, V.C.; Alley, A.M.; Wen, L.
Molecular cloning of bovine eIF5A and deoxyhypusine synthase cDNA
DNA Seq.
15
26-32
2004
Bos taurus (Q6EWQ6), Bos taurus
brenda
Clement, P.M.; Henderson, C.A.; Jenkins, Z.A.; Smit-McBride, Z.; Wolff, E.C.; Hershey, J.W.; Park, M.H.; Johansson, H.E.
Identification and characterization of eukaryotic initiation factor 5A-2
Eur. J. Biochem.
270
4254-4263
2003
Homo sapiens
brenda
Umland, T.C.; Wolff, E.C.; Park, M.H.; Davies, D.R.
A new crystal structure of deoxyhypusine synthase reveals the configuration of the active enzyme and of an enzyme-NAD-inhibitor ternary complex
J. Biol. Chem.
279
28697-28705
2004
Homo sapiens (P49366), Homo sapiens
brenda
Wang, T.W.; Wu, W.; Zhang, C.G.; Nowack, L.M.; Liu, Z.; Thompson, J.E.
Antisense suppression of deoxyhypusine synthase by vacuum-infiltration of Agrobacterium enhances growth and seed yield of canola
Physiol. Plant.
124
493-503
2005
Brassica napus
-
brenda
Nurhayati, N.; Ober, D.
Recruitment of alkaloid-specific homospermidine synthase (HSS) from ubiquitous deoxyhypusine synthase: Does Crotalaria possess a functional HSS that still has DHS activity?
Phytochemistry
66
1346-1357
2005
Crotalaria juncea, Crotalaria scassellatii (Q4QZB4), Crotalaria scassellatii
brenda
Huang, J.K.; Tsai, S.; Huang, G.H.; Gowda, P.G.; Walzer, A.M.; Wen, L.
Higher activity of recombinant bovine deoxyhypusine synthase vs. human deoxyhypusine synthase
Protein Expr. Purif.
35
32-38
2004
Homo sapiens, Bos taurus (Q6EWQ6), Bos taurus
brenda
Jao, D.L.; Chen, K.Y.
Tandem affinity purification revealed the hypusine-dependent binding of eukaryotic initiation factor 5A to the translating 80S ribosomal complex
J. Cell. Biochem.
97
583-598
2006
Saccharomyces cerevisiae, Saccharomyces cerevisiae KCY307
brenda
Duguay, J.; Jamal, S.; Liu, Z.; Wang, T.W.; Thompson, J.E.
Leaf-specific suppression of deoxyhypusine synthase in Arabidopsis thaliana enhances growth without negative pleiotropic effects
J. Plant Physiol.
164
408-420
2007
Arabidopsis thaliana
brenda
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
Saccharomyces cerevisiae
brenda
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
Saccharomyces cerevisiae, Mus musculus
brenda
Chawla, B.; Jhingran, A.; Singh, S.; Tyagi, N.; Park, M.H.; Srinivasan, N.; Roberts, S.C.; Madhubala, R.
Identification and characterization of a novel deoxyhypusine synthase in Leishmania donovani
J. Biol. Chem.
285
453-463
2010
Leishmania donovani, Leishmania donovani (B5APK2), Leishmania donovani MHOM/IN/1983/AG83 (B5APK2)
brenda
Ober, D.; Kaltenegger, E.
Pyrrolizidine alkaloid biosynthesis, evolution of a pathway in plant secondary metabolism
Phytochemistry
70
1687-1695
2009
Leishmania donovani
brenda
Nurhayati, N.; Gonde, D.; Ober, D.
Evolution of pyrrolizidine alkaloids in Phalaenopsis orchids and other monocotyledons: identification of deoxyhypusine synthase, homospermidine synthase and related pseudogenes
Phytochemistry
70
508-516
2009
Phalaenopsis sp., Zea mays (B7FBH2), Zea mays
brenda
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
brenda
Hyvoenen, M.T.; Keinaenen, T.A.; Khomutov, M.; Simonian, A.; Vepsaelaeinen, J.; Park, J.H.; Khomutov, A.R.; Alhonen, L.; Park, M.H.
Effects of novel C-methylated spermidine analogs on cell growth via hypusination of eukaryotic translation initiation factor 5A
Amino Acids
42
685-695
2012
Homo sapiens
brenda
Nishimura, K.; Lee, S.B.; Park, J.H.; Park, M.H.
Essential role of eIF5A-1 and deoxyhypusine synthase in mouse embryonic development
Amino Acids
42
703-710
2012
Mus musculus, Mus musculus C57/BL6J
brenda
Templin, A.T.; Maier, B.; Nishiki, Y.; Tersey, S.A.; Mirmira, R.G.
Deoxyhypusine synthase haploinsufficiency attenuates acute cytokine signaling
Cell Cycle
10
1043-1049
2011
Mus musculus, Mus musculus C57/BL6J
brenda
Ziegler, P.; Chahoud, T.; Wilhelm, T.; Paellman, N.; Braig, M.; Wiehle, V.; Ziegler, S.; Schroeder, M.; Meier, C.; Kolodzik, A.; Rarey, M.; Panse, J.; Hauber, J.; Balabanov, S.; Bruemmendorf, T.H.
Evaluation of deoxyhypusine synthase inhibitors targeting BCR-ABL positive leukemias
Invest. New Drugs
30
2274-2283
2012
Homo sapiens, Mus musculus
brenda
Wolff, E.C.; Lee, S.B.; Park, M.H.
Assay of deoxyhypusine synthase activity
Methods Mol. Biol.
720
195-205
2011
Homo sapiens
brenda
Woriedh, M.; Hauber, I.; Martinez-Rocha, A.L.; Voigt, C.; Maier, F.J.; Schroeder, M.; Meier, C.; Hauber, J.; Schaefer, W.
Preventing Fusarium head blight of wheat and cob rot of maize by inhibition of fungal deoxyhypusine synthase
Mol. Plant Microbe Interact.
24
619-627
2011
Fusarium graminearum, Triticum aestivum, Zea mays, Fusarium graminearum FG00323.1
brenda
Preukschas, M.; Hagel, C.; Schulte, A.; Weber, K.; Lamszus, K.; Sievert, H.; Paellmann, N.; Bokemeyer, C.; Hauber, J.; Braig, M.; Balabanov, S.
Expression of eukaryotic initiation factor 5A and hypusine forming enzymes in glioblastoma patient samples: implications for new targeted therapies
PLoS ONE
7
e43468
2012
Homo sapiens
brenda
Hyvoenen, M.T.; Khomutov, M.; Petit, M.; Weisell, J.; Kochetkov, S.N.; Alhonen, L.; Vepsaelaeinen, J.; Khomutov, A.R.; Keinaenen, T.A.
Enantiomers of 3-methylspermidine selectively modulate deoxyhypusine synthesis and reveal important determinants for spermidine transport
ACS Chem. Biol.
10
1417-1424
2015
Homo sapiens (P49366)
brenda
Prunetti, L.; Graf, M.; Blaby, I.K.; Peil, L.; Makkay, A.M.; Starosta, A.L.; Papke, R.T.; Oshima, T., Wilson, D.N.; de Crcy-Lagard, V.
Deciphering the translation initiation factor 5A modification pathway in halophilic Archaea
Archaea
2016
7316725
2016
Haloferax volcanii, Haloferax volcanii LSP5021, Saccharomyces cerevisiae, Thermococcus kodakarensis
brenda
Quintas-Granados, L.I.; Carvajal Gamez, B.I.; Villalpando, J.L.; Ortega-Lopez, J.; Arroyo, R.; Azuara-Liceaga, E.; Alvarez-Sanchez, M.E.
Bifunctional activity of deoxyhypusine synthase/hydroxylase from Trichomonas vaginalis
Biochimie
123
37-51
2016
Trichomonas vaginalis (F1AQF9), Trichomonas vaginalis, Trichomonas vaginalis CNCD 147 (F1AQF9)
brenda
Njuguna, J.T.; von Koschitzky, I.; Gerhardt, H.; Laemmerhofer, M.; Choucry, A.; Pink, M.; Schmitz-Spahnke, S.; Bakheit, M.A.; Strube, C.; Kaiser, A.
Target evaluation of deoxyhypusine synthase from Theileria parva the neglected animal parasite and its relationship to Plasmodium
Bioorg. Med. Chem.
22
4338-4346
2014
Theileria parva (Q4UDC3), Theileria parva, Theileria parva Muguga (Q4UDC3)
brenda
Belda-Palazon, B.; Nohales, M.A.; Rambla, J.L.; Acena, J.L.; Delgado, O.; Fustero, S.; Martinez, M.C.; Granell, A.; Carbonell, J.; Ferrando, A.
Biochemical quantitation of the eIF5A hypusination in Arabidopsis thaliana uncovers ABA-dependent regulation
Front. Plant Sci.
5
202
2014
Arabidopsis thaliana (Q9FI94), Arabidopsis thaliana, Arabidopsis thaliana Col-0 (Q9FI94)
brenda
Belda-Palazon, B.; Almendariz, C.; Marti, E.; Carbonell, J.; Ferrando, A.
Relevance of the axis spermidine/eIF5A for plant growth and development
Front. Plant Sci.
7
245
2016
Arabidopsis thaliana (Q9FI94), Arabidopsis thaliana, Arabidopsis thaliana Col-0 (Q9FI94)
brenda
Nguyen, S.; Jones, D.C.; Wyllie, S.; Fairlamb, A.H.; Phillips, M.A.
Allosteric activation of trypanosomatid deoxyhypusine synthase by a catalytically dead paralog
J. Biol. Chem.
288
15256-15267
2013
Trypanosoma brucei brucei (Q38BX0), Trypanosoma brucei brucei (Q4GZD1), Trypanosoma brucei brucei 927 / 4 GUTat10.1 / TREU927 (Q38BX0), Trypanosoma brucei brucei 927 / 4 GUTat10.1 / TREU927 (Q4GZD1)
brenda
Mittal, N.; Morada, M.; Tripathi, P.; Gowri, V.S.; Mandal, S.; Quirch, A.; Park, M.H.; Yarlett, N.; Madhubala, R.
Cryptosporidium parvum has an active hypusine biosynthesis pathway
Mol. Biochem. Parasitol.
195
14-22
2014
Cryptosporidium parvum (A3FQA5), Cryptosporidium parvum
brenda
Muramatsu, T.; Kozaki, K.I.; Imoto, S.; Yamaguchi, R.; Tsuda, H.; Kawano, T.; Fujiwara, N.; Morishita, M.; Miyano, S.; Inazawa, J.
The hypusine cascade promotes cancer progression and metastasis through the regulation of RhoA in squamous cell carcinoma
Oncogene
35
5304-5316
2016
Homo sapiens (P49366), Homo sapiens
brenda
Kaltenegger, E.; Eich, E.; Ober, D.
Evolution of homospermidine synthase in the convolvulaceae: a story of gene duplication, gene loss, and periods of various selection pressures
Plant Cell
25
1213-1227
2013
Convolvulus arvensis, Ipomoea neei, Ipomoea hederifolia, Ipomoea alba, Ipomoea meyeri, Distimake quinquefolius, Convolvulus tricolor
brenda
Galvao, F.C.; Rossi, D.; Silveira, W.d.a..S.; Valentini, S.R.; Zanelli, C.F.
The deoxyhypusine synthase mutant dys1-1 reveals the association of eIF5A and Asc1 with cell wall integrity
PLoS ONE
8
e60140
2013
Saccharomyces cerevisiae
brenda
Khomutov, M.; Keinanen, T.; Hyvonen, M.; Weisell, J.; Vepsalainen, J.; Alhonen, L.; Kochetkov, S.; Khomutov, A.
Enantioselective synthesis of (R)- and (S)-3-methylspermidines
Russ. J. Bioorg. Chem.
41
548-553
2015
Homo sapiens (P49366)
-
brenda
Martinez-Rocha, A.L.; Woriedh, M.; Chemnitz, J.; Willingmann, P.; Kroeger, C.; Hadeler, B.; Hauber, J.; Schaefer, W.
Posttranslational hypusination of the eukaryotic translation initiation factor-5A regulates Fusarium graminearum virulence
Sci. Rep.
6
24698
2016
Fusarium graminearum (D5L6Z2), Fusarium graminearum
brenda
Bassani, F.; Romagnoli, A.; Cacciamani, T.; Amici, A.; Benelli, D.; Londei, P.; Maertens, B.; Blaesi, U.; La Teana, A.
Modification of translation factor aIF5A from Sulfolobus solfataricus
Extremophiles
22
769-780
2018
Saccharolobus solfataricus (Q97ZF1), Saccharolobus solfataricus, Saccharolobus solfataricus DSM 1617 (Q97ZF1)
brenda
Burnat, M.; Li, B.; Kim, S.; Michael, A.; Flores, E.
Homospermidine biosynthesis in the cyanobacterium Anabaena requires a deoxyhypusine synthase homologue and is essential for normal diazotrophic growth
Mol. Microbiol.
109
763-780
2018
Nostoc sp. PCC 7120 = FACHB-418 (Q8YQL7)
brenda
Ganapathi, M.; Padgett, L.R.; Yamada, K.; Devinsky, O.; Willaert, R.; Person, R.; Au, P.B.; Tagoe, J.; McDonald, M.; Karlowicz, D.; Wolf, B.; Lee, J.; Shen, Y.; Okur, V.; Deng, L.; LeDuc, C.A.; Wang, J.; Hanner, A.; Mirmira, R.G.; Park, M.H.; Mastracci, T.L.; Chung, W.K.
Recessive rare variants in deoxyhypusine synthase, an enzyme involved in the synthesis of hypusine, are associated with a neurodevelopmental disorder
Am. J. Hum. Genet.
104
287-298
2019
Homo sapiens (P49366)
brenda
Park, M.H.; Mandal, A.; Mandal, S.; Wolff, E.C.
A new non-radioactive deoxyhypusine synthase assay adaptable to high throughput screening
Amino Acids
49
1793-1804
2017
Homo sapiens (P49366), Homo sapiens
brenda
Schultz, C.R.; Geerts, D.; Mooney, M.; El-Khawaja, R.; Koster, J.; Bachmann, A.S.
Synergistic drug combination GC7/DFMO suppresses hypusine/spermidine-dependent eIF5A activation and induces apoptotic cell death in neuroblastoma
Biochem. J.
475
531-545
2018
Homo sapiens (P49366)
brenda
Wator, E.; Wilk, P.; Grudnik, P.
Half way to hypusine-structural basis for substrate recognition by human deoxyhypusine synthase
Biomolecules
10
522
2020
Homo sapiens (P49366), Homo sapiens
brenda
Liu, J.; Chang, X.; Ding, B.; Zhong, S.; Peng, L.; Wei, Q.; Meng, J.; Yu, Y.
PhDHS is involved in chloroplast development in petunia
Front. Plant Sci.
10
284
2019
Petunia x hybrida
brenda
Tanaka, Y.; Kurasawa, O.; Yokota, A.; Klein, M.G.; Ono, K.; Saito, B.; Matsumoto, S.; Okaniwa, M.; Ambrus-Aikelin, G.; Morishita, D.; Kitazawa, S.; Uchiyama, N.; Ogawa, K.; Kimura, H.; Imamura, S.
Discovery of novel allosteric inhibitors of deoxyhypusine synthase
J. Med. Chem.
63
3215-3226
2020
Homo sapiens (P49366)
brenda
Aroonsri, A.; Posayapisit, N.; Kongsee, J.; Siripan, O.; Vitsupakorn, D.; Utaida, S.; Uthaipibull, C.; Kamchonwongpaisan, S.; Shaw, P.J.
Validation of Plasmodium falciparum deoxyhypusine synthase as an antimalarial target
PeerJ
7
e6713
2019
Plasmodium falciparum (Q8ILW8), Plasmodium falciparum
brenda
Imam, S.; Prathibha, R.; Dar, P.; Almotah, K.; Al-Khudhair, A.; Hasan, S.A.; Salim, N.; Jilani, T.N.; Mirmira, R.G.; Jaume, J.C.
eIF5A inhibition influences T cell dynamics in the pancreatic microenvironment of the humanized mouse model of type 1 diabetes
Sci. Rep.
9
1533
2019
Mus musculus (Q3TXU5), Mus musculus
brenda
Levasseur, E.M.; Yamada, K.; Pineros, A.R.; Wu, W.; Syed, F.; Orr, K.S.; Anderson-Baucum, E.; Mastracci, T.L.; Maier, B.; Mosley, A.L.; Liu, Y.; Bernal-Mizrachi, E.; Alonso, L.C.; Scott, D.; Garcia-Ocana, A.; Tersey, S.A.; Mirmira, R.G.
Hypusine biosynthesis in beta cells links polyamine metabolism to facultative cellular proliferation to maintain glucose homeostasis
Sci. Signal.
12
eaax0715
2019
Mus musculus (Q3TXU5), Mus musculus
brenda
Afanador, G.A.; Tomchick, D.R.; Phillips, M.A.
Trypanosomatid deoxyhypusine synthase activity is dependent on shared active-site complementation between pseudoenzyme paralogs
Structure
26
1499-1512
2018
Trypanosoma brucei brucei (Q38BX0 and Q4GZD1), Trypanosoma brucei brucei 927/4 GUTat10.1 (Q38BX0 and Q4GZD1)
brenda
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