1.14.99.29: deoxyhypusine monooxygenase
This is an abbreviated version!
For detailed information about deoxyhypusine monooxygenase, go to the full flat file.
Word Map on EC 1.14.99.29
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1.14.99.29
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eif-5a
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spermidine
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hypusine-containing
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gc7
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mimosine
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ciclopirox
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nepsilon-4-amino-2-hydroxybutyllysine
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drug development
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deferiprone
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eif5a-1
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polyamine-derived
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4-aminobutyl
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diiron
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n1-guanyl-1,7-diaminoheptane
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heat-repeats
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heat-like
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peroxo
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deoxyhypusine-containing
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medicine
- 1.14.99.29
-
eif-5a
- spermidine
-
hypusine-containing
- gc7
- mimosine
- ciclopirox
-
nepsilon-4-amino-2-hydroxybutyllysine
- drug development
- deferiprone
-
eif5a-1
-
polyamine-derived
-
4-aminobutyl
-
diiron
- n1-guanyl-1,7-diaminoheptane
-
heat-repeats
-
heat-like
-
peroxo
-
deoxyhypusine-containing
- medicine
Reaction
Synonyms
deoxyhypusine hydroxylase, deoxyhypusine hydroxylase homologue nero, deoxyhypusine synthase/hydroxylase, deoxyhypusyl hydroxylase, DOHH, DOOH, hDOHH, Lia1, More, nero, oxygenase, deoxyhypusine di-
ECTree
1.14.99.29 deoxyhypusine monooxygenaseAdvanced search results
results (
results (Engineering
Engineering on EC 1.14.99.29 - deoxyhypusine monooxygenase
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PROTEIN VARIANTS 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
E57G
site-directed mutagenesis, the substitution located at one of the four conserved His-Glu pairs, the potential metal coordination sites, results in severe reduction of deoxyhypusine hydroxylase activity compared to the wild-type enzyme
E208A
E208D
E208N
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site-directed mutagenesis, the mutant shows severely impairment in eIF5A(deoxyhypusine) binding
E208Q
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site-directed mutagenesis, the mutant shows severely impairment in eIF5A(deoxyhypusine) binding
E241A
E57A
E57D
E57N
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site-directed mutagenesis, the mutant shows severely impairment in eIF5A(deoxyhypusine) binding
E57Q
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site-directed mutagenesis, the mutant shows severely impairment in eIF5A(deoxyhypusine) binding
E90A
E93A
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site-directed mutagenesis, the mutant shows reduced eIF5A(deoxyhypusine) binding
G214A
G247A
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site-directed mutagenesis, the mutant shows 50-80% reduced activity compared to the wild-type enzyme, but is capable of binding both iron and substrate
G63A
H207A
H240A
H56A
H89A
M237A
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site-directed mutagenesis, the mutant shows reduced, but existing eIF5A(deoxyhypusine) and iron binding, but is catalytically inactive
Q215
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site-directed mutagenesis, the mutant shows 50-80% reduced activity compared to the wild-type enzyme, but is capable of binding both iron and substrate
R183a
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site-directed mutagenesis, the mutant shows 50-80% reduced activity compared to the wild-type enzyme, but is capable of binding both iron and substrate
R26A
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site-directed mutagenesis, the mutant shows 50-80% reduced activity compared to the wild-type enzyme, but is capable of binding both iron and substrate
R88A
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site-directed mutagenesis, the mutant shows 50-80% reduced activity compared to the wild-type enzyme, but is capable of binding both iron and substrate
S202A
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site-directed mutagenesis, the mutant shows 50-80% reduced activity compared to the wild-type enzyme, but is capable of binding both iron and substrate
E113A
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site-directed mutagenesis, the mutant is completely inactive in deoxyhypusine hydroxylation, structure comparison to the wild-type enzyme
E116A
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site-directed mutagenesis, the mutant is completely inactive in deoxyhypusine hydroxylation, structure comparison to the wild-type enzyme
E116D
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site-directed mutagenesis, the mutant is completely inactive in deoxyhypusine hydroxylation, structure comparison to the wild-type enzyme
E238A
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site-directed mutagenesis, the mutant is completely inactive in deoxyhypusine hydroxylation, structure comparison to the wild-type enzyme
E271A
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site-directed mutagenesis, the mutant is completely inactive in deoxyhypusine hydroxylation, structure comparison to the wild-type enzyme
E80A
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site-directed mutagenesis, the mutant is completely inactive in deoxyhypusine hydroxylation, structure comparison to the wild-type enzyme
H112A
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site-directed mutagenesis, the mutant is completely inactive in deoxyhypusine hydroxylation, structure comparison to the wild-type enzyme
H237A
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site-directed mutagenesis, the mutant is completely inactive in deoxyhypusine hydroxylation, structure comparison to the wild-type enzyme
H270A
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site-directed mutagenesis, the mutant is completely inactive in deoxyhypusine hydroxylation, structure comparison to the wild-type enzyme
H79A
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site-directed mutagenesis, the mutant is completely inactive in deoxyhypusine hydroxylation, structure comparison to the wild-type enzyme
E66K
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mutation E66K in the DOHH homologue gene, Mmd1, causes a temperature-sensitive growth phenotype and altered mitochondrial morphology and distribution
additional information
E208A
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severe impairment in binding of substrate translation initiation factor 5A, complete loss of activity
E208A
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site-directed mutagenesis, the mutant shows severely impairment in eIF5A(deoxyhypusine) binding
E208D
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impairment in binding of substrate translation initiation factor 5A, retains some activity
E208D
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site-directed mutagenesis, the mutant shows reduced but not fully abolished eIF5A(deoxyhypusine) binding
E241A
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severe impairment in binding of substrate translation initiation factor 5A
E241A
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site-directed mutagenesis, the mutant shows severely impairment in eIF5A(deoxyhypusine) binding
E57A
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severe impairment in binding of substrate translation initiation factor 5A, complete loss of activity
E57A
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site-directed mutagenesis, the mutant shows severely impairment in eIF5A(deoxyhypusine) binding
E57D
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impairment in binding of substrate translation initiation factor 5A, retains some activity
E57D
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site-directed mutagenesis, the mutant shows reduced but not fully abolished eIF5A(deoxyhypusine) binding
E90A
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severe impairment in binding of substrate translation initiation factor 5A
E90A
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site-directed mutagenesis, the mutant shows severely impairment in eIF5A(deoxyhypusine) and iron binding
G214A
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severe impairment in binding of substrate translation initiation factor 5A
G214A
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site-directed mutagenesis, the mutant shows reduced eIF5A(deoxyhypusine) but unaltered iron binding
G63A
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severe impairment in binding of substrate translation initiation factor 5A
G63A
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site-directed mutagenesis, the mutant shows reduced eIF5A(deoxyhypusine), but unaltered iron binding
additional information
a deletion at the HEAT-repeats 1-3, potential metal coordination sites, results in complete losses of deoxyhypusine hydroxylase activity, the different clones encoding the enzyme show differing activity, overview
additional information
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a deletion at the HEAT-repeats 1-3, potential metal coordination sites, results in complete losses of deoxyhypusine hydroxylase activity, the different clones encoding the enzyme show differing activity, overview
additional information
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construction of a polycistronic vector encoding eIF5A, DHS and DOHH, overview
additional information
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enzyme deletion mutant grows similar to wild-type in rich and minimal medium despite lack of 6-N-[(R)-4-amino-2-hydroxybutyl]-L-lysine
additional information
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single copy gene dohh inactivation of deoxyhypusine hydroxylase
