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Information on EC 2.5.1.46 - deoxyhypusine synthase and Organism(s) Senecio vernalis and UniProt Accession Q9SC14

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IUBMB 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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This record set is specific for:
Senecio vernalis
UNIPROT: Q9SC14
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The taxonomic range for the selected organisms is: Senecio vernalis
The expected taxonomic range for this enzyme is: Archaea, Bacteria, Eukaryota
Synonyms
deoxyhypusine synthase, dhs34, cpdhs, pf3d7_1412600, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
deoxyhypusine synthase (Caulobacter crescentus gene CC0359)
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-
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deoxyhypusine synthase (Halobacterium strain NRC-1 gene dhs)
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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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deoxyhypusine synthase (Senecio vernalis gene DHS1)
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DHS
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synthase, deoxyhypusine
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-
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-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
aminobutyl group transfer
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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.
CAS REGISTRY NUMBER
COMMENTARY hide
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
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
homospermidine + putrescine
homospermidine + ?
show the reaction diagram
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-
-
?
spermidine + putrescine
homospermidine + ?
show the reaction diagram
[eIF5A-precursor]-L-lysine + spermidine
[eIF5A-precursor]-deoxyhypusine + propane-1,3-diamine
show the reaction diagram
-
-
-
?
[eIF5A-precursor]-lysine + spermidine
[eIF5A-precursor]-deoxyhypusine + propane-1,3-diamine
show the reaction diagram
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
[eIF5A-precursor]-lysine + spermidine
[eIF5A-precursor]-deoxyhypusine + propane-1,3-diamine
show the reaction diagram
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0013
[eIF5A-precursor]-L-lysine
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-
additional information
additional information
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0022
[eIF5A-precursor]-L-lysine
+ spermidine
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.0101
with acceptor eIF5A-prcursor
0.0442
with acceptor putrescine
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
9.3
glycine-NaOH buffer
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
8.8 - 9.9
pH 8.8: about 35% of maximal activity, pH 9.9: about 60% of maximal activity
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
SwissProt
Manually annotated by BRENDA team
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
-
low level
Manually annotated by BRENDA team
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young, low level
Manually annotated by BRENDA team
-
high activity
Manually annotated by BRENDA team
-
young or old, low level
Manually annotated by BRENDA team
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
DHYS_SENVE
371
0
41387
Swiss-Prot
other Location (Reliability: 2)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
41000
x * 41000, SDS-PAGE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
x * 41000, SDS-PAGE
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant enzyme
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team