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6-N-[(R)-4-amino-2-hydroxybutyl]-L-lysine of human translation initiation factor 5A + electron donor + O2
6-N-(4-aminobutyl)-L-lysine of human translation initiation factor 5A + oxidized electron donor + H2O
6-N-[(R)-4-amino-2-hydroxybutyl]-L-lysine of yeast translation initiation factor 5A + electron donor + O2
6-N-(4-aminobutyl)-L-lysine of yeast translation initiation factor 5A + oxidized electron donor + H2O
eIF5A-N6-(4-aminobutyl)-L-lysine + AH2 + O2
eIF5A-N6-(4-amino-2-hydroxybutyl)-L-lysine + A + H2O
eIF5A-Nepsilon-(4-aminobutyl)lysine + AH2 + O2
eIF5A-Nepsilon-(4-amino-2-hydroxybutyl)lysine + A + H2O
eukaryotic translation initiation factor eIF-5A deoxyhypusine + O2 + AH2
eukaryotic translation initiation factor eIF-5A hypusine + H2O + A
N'-(4-aminobutyl)lysine + electron donor + O2
N'-(4-amino-2-hydroxybutyl)lysine + oxidized electron donor + H2O
[eIF5A]-deoxyhypusine + AH2 + O2
[eIF5A]-hypusine + A + H2O
[eIF5A]-deoxyhypusine + NADH + H+ + O2
[eIF5A]-hypusine + NAD+ + H2O
-
-
-
-
?
additional information
?
-
6-N-[(R)-4-amino-2-hydroxybutyl]-L-lysine of human translation initiation factor 5A + electron donor + O2

6-N-(4-aminobutyl)-L-lysine of human translation initiation factor 5A + oxidized electron donor + H2O
-
-
-
-
?
6-N-[(R)-4-amino-2-hydroxybutyl]-L-lysine of human translation initiation factor 5A + electron donor + O2
6-N-(4-aminobutyl)-L-lysine of human translation initiation factor 5A + oxidized electron donor + H2O
-
strong preference of enzyme for binding the 6-N-(4-amino-2-hydroxybutyl)-L-lysine-containing form of translation initiation factor 5A
-
-
?
6-N-[(R)-4-amino-2-hydroxybutyl]-L-lysine of yeast translation initiation factor 5A + electron donor + O2

6-N-(4-aminobutyl)-L-lysine of yeast translation initiation factor 5A + oxidized electron donor + H2O
-
strong preference of enzyme for binding the 6-N-(4-amino-2-hydroxybutyl)-L-lysine-containing form of translation initiation factor 5A
-
-
?
6-N-[(R)-4-amino-2-hydroxybutyl]-L-lysine of yeast translation initiation factor 5A + electron donor + O2
6-N-(4-aminobutyl)-L-lysine of yeast translation initiation factor 5A + oxidized electron donor + H2O
-
-
-
-
?
eIF5A-N6-(4-aminobutyl)-L-lysine + AH2 + O2

eIF5A-N6-(4-amino-2-hydroxybutyl)-L-lysine + A + H2O
-
-
-
-
?
eIF5A-N6-(4-aminobutyl)-L-lysine + AH2 + O2
eIF5A-N6-(4-amino-2-hydroxybutyl)-L-lysine + A + H2O
-
the unique posttranslational modification occurs in only one cellular protein, the eukaryotic translation initiation factor 5A, eIF5A
-
-
?
eIF5A-N6-(4-aminobutyl)-L-lysine + AH2 + O2
eIF5A-N6-(4-amino-2-hydroxybutyl)-L-lysine + A + H2O
-
-
-
-
?
eIF5A-N6-(4-aminobutyl)-L-lysine + AH2 + O2
eIF5A-N6-(4-amino-2-hydroxybutyl)-L-lysine + A + H2O
-
different eIF5A isozymes exist. The unique posttranslational modification occurs in only one cellular protein, the eukaryotic translation initiation factor 5A, eIF5A
-
-
?
eIF5A-N6-(4-aminobutyl)-L-lysine + AH2 + O2
eIF5A-N6-(4-amino-2-hydroxybutyl)-L-lysine + A + H2O
-
-
-
-
?
eIF5A-N6-(4-aminobutyl)-L-lysine + AH2 + O2
eIF5A-N6-(4-amino-2-hydroxybutyl)-L-lysine + A + H2O
-
the unique posttranslational modification occurs in only one cellular protein, the eukaryotic translation initiation factor 5A, eIF5A
-
-
?
eIF5A-N6-(4-aminobutyl)-L-lysine + AH2 + O2
eIF5A-N6-(4-amino-2-hydroxybutyl)-L-lysine + A + H2O
-
-
-
-
?
eIF5A-N6-(4-aminobutyl)-L-lysine + AH2 + O2
eIF5A-N6-(4-amino-2-hydroxybutyl)-L-lysine + A + H2O
-
-
-
-
ir
eIF5A-N6-(4-aminobutyl)-L-lysine + AH2 + O2
eIF5A-N6-(4-amino-2-hydroxybutyl)-L-lysine + A + H2O
-
different eIF5A isozymes exist. The unique posttranslational modification occurs in only one cellular protein, the eukaryotic translation initiation factor 5A, eIF5A
-
-
?
eIF5A-N6-(4-aminobutyl)-L-lysine + AH2 + O2
eIF5A-N6-(4-amino-2-hydroxybutyl)-L-lysine + A + H2O
-
the DOHH reaction is irreversible
-
-
ir
eIF5A-N6-(4-aminobutyl)-L-lysine + AH2 + O2
eIF5A-N6-(4-amino-2-hydroxybutyl)-L-lysine + A + H2O
-
-
-
-
?
eIF5A-N6-(4-aminobutyl)-L-lysine + AH2 + O2
eIF5A-N6-(4-amino-2-hydroxybutyl)-L-lysine + A + H2O
-
-
-
-
?
eIF5A-N6-(4-aminobutyl)-L-lysine + AH2 + O2
eIF5A-N6-(4-amino-2-hydroxybutyl)-L-lysine + A + H2O
-
-
-
-
?
eIF5A-N6-(4-aminobutyl)-L-lysine + AH2 + O2
eIF5A-N6-(4-amino-2-hydroxybutyl)-L-lysine + A + H2O
-
activation of eIF5A
-
-
?
eIF5A-N6-(4-aminobutyl)-L-lysine + AH2 + O2
eIF5A-N6-(4-amino-2-hydroxybutyl)-L-lysine + A + H2O
-
different eIF5A isozymes exist, no activity with eIF5A mutant K51R, that lacks hypusine. The unique posttranslational modification occurs in only one cellular protein, the eukaryotic translation initiation factor 5A, eIF5A
-
-
?
eIF5A-N6-(4-aminobutyl)-L-lysine + AH2 + O2
eIF5A-N6-(4-amino-2-hydroxybutyl)-L-lysine + A + H2O
-
-
-
-
?
eIF5A-N6-(4-aminobutyl)-L-lysine + AH2 + O2
eIF5A-N6-(4-amino-2-hydroxybutyl)-L-lysine + A + H2O
-
the unique posttranslational modification occurs in only one cellular protein, the eukaryotic translation initiation factor 5A, eIF5A
-
-
?
eIF5A-Nepsilon-(4-aminobutyl)lysine + AH2 + O2

eIF5A-Nepsilon-(4-amino-2-hydroxybutyl)lysine + A + H2O
the enzyme catalyzes the maturation of eukaryotic initiation factor 5A, synthesis of hypusine is essential for the function of eIF5A in eukaryotic cell proliferation and survival
-
-
?
eIF5A-Nepsilon-(4-aminobutyl)lysine + AH2 + O2
eIF5A-Nepsilon-(4-amino-2-hydroxybutyl)lysine + A + H2O
eIF5A is the eukaryotic translation initiation factor 5A
-
-
?
eIF5A-Nepsilon-(4-aminobutyl)lysine + AH2 + O2
eIF5A-Nepsilon-(4-amino-2-hydroxybutyl)lysine + A + H2O
-
the enzyme catalyzes the final step of the post-translational synthesis of hypusine, i.e. Nepsilon-(4-amino-2-hydroxybutyl)lysine, in the eukaryotic translation initiation factor 5A, eIF5A
-
-
?
eIF5A-Nepsilon-(4-aminobutyl)lysine + AH2 + O2
eIF5A-Nepsilon-(4-amino-2-hydroxybutyl)lysine + A + H2O
-
eIF5A is the eukaryotic translation initiation factor 5A, specificity of the interaction between eIF5A and DOHH using the isoform eIF5A-1, DOHH displays a strong preference for binding the deoxyhypusine-containing form of eIF5A, over the eIF5A precursor or the hypusine-containing eIF5A, the deoxyhypusine side chain of the substrate is primarily anchored by gamma-carboxyl groups of Glu57 and Glu208 at the DOHH active site, substrate binding modelling, overview
-
-
?
eukaryotic translation initiation factor eIF-5A deoxyhypusine + O2 + AH2

eukaryotic translation initiation factor eIF-5A hypusine + H2O + A
-
-
-
-
?
eukaryotic translation initiation factor eIF-5A deoxyhypusine + O2 + AH2
eukaryotic translation initiation factor eIF-5A hypusine + H2O + A
-
-
-
-
?
N'-(4-aminobutyl)lysine + electron donor + O2

N'-(4-amino-2-hydroxybutyl)lysine + oxidized electron donor + H2O
-
i.e. deoxyhypusine
i.e. hypusine
?
N'-(4-aminobutyl)lysine + electron donor + O2
N'-(4-amino-2-hydroxybutyl)lysine + oxidized electron donor + H2O
-
i.e. deoxyhypusine
i.e. hypusine
?
N'-(4-aminobutyl)lysine + electron donor + O2
N'-(4-amino-2-hydroxybutyl)lysine + oxidized electron donor + H2O
-
i.e. deoxyhypusine
i.e. hypusine
?
N'-(4-aminobutyl)lysine + electron donor + O2
N'-(4-amino-2-hydroxybutyl)lysine + oxidized electron donor + H2O
-
i.e. deoxyhypusine
i.e. hypusine
?
N'-(4-aminobutyl)lysine + electron donor + O2
N'-(4-amino-2-hydroxybutyl)lysine + oxidized electron donor + H2O
-
i.e. deoxyhypusine
i.e. hypusine
?
N'-(4-aminobutyl)lysine + electron donor + O2
N'-(4-amino-2-hydroxybutyl)lysine + oxidized electron donor + H2O
-
i.e. deoxyhypusine
i.e. hypusine
?
N'-(4-aminobutyl)lysine + electron donor + O2
N'-(4-amino-2-hydroxybutyl)lysine + oxidized electron donor + H2O
-
i.e. deoxyhypusine
i.e. hypusine
?
N'-(4-aminobutyl)lysine + electron donor + O2
N'-(4-amino-2-hydroxybutyl)lysine + oxidized electron donor + H2O
-
i.e. deoxyhypusine
i.e. hypusine
?
N'-(4-aminobutyl)lysine + electron donor + O2
N'-(4-amino-2-hydroxybutyl)lysine + oxidized electron donor + H2O
-
i.e. deoxyhypusine
i.e. hypusine
?
N'-(4-aminobutyl)lysine + electron donor + O2
N'-(4-amino-2-hydroxybutyl)lysine + oxidized electron donor + H2O
-
i.e. deoxyhypusine
i.e. hypusine
?
N'-(4-aminobutyl)lysine + electron donor + O2
N'-(4-amino-2-hydroxybutyl)lysine + oxidized electron donor + H2O
-
i.e. deoxyhypusine
i.e. hypusine
?
N'-(4-aminobutyl)lysine + electron donor + O2
N'-(4-amino-2-hydroxybutyl)lysine + oxidized electron donor + H2O
-
i.e. deoxyhypusine
i.e. hypusine
?
[eIF5A]-deoxyhypusine + AH2 + O2

[eIF5A]-hypusine + A + H2O
-
-
-
?
[eIF5A]-deoxyhypusine + AH2 + O2
[eIF5A]-hypusine + A + H2O
-
-
-
?
[eIF5A]-deoxyhypusine + AH2 + O2
[eIF5A]-hypusine + A + H2O
-
-
-
?
[eIF5A]-deoxyhypusine + AH2 + O2
[eIF5A]-hypusine + A + H2O
-
-
-
-
?
[eIF5A]-deoxyhypusine + AH2 + O2
[eIF5A]-hypusine + A + H2O
-
-
-
?
[eIF5A]-deoxyhypusine + AH2 + O2
[eIF5A]-hypusine + A + H2O
-
-
-
-
?
[eIF5A]-deoxyhypusine + AH2 + O2
[eIF5A]-hypusine + A + H2O
-
-
-
ir
[eIF5A]-deoxyhypusine + AH2 + O2
[eIF5A]-hypusine + A + H2O
-
-
-
-
?
[eIF5A]-deoxyhypusine + AH2 + O2
[eIF5A]-hypusine + A + H2O
-
product analysis by GC/MS and gel filtration
-
?
[eIF5A]-deoxyhypusine + AH2 + O2
[eIF5A]-hypusine + A + H2O
-
product analysis by GC/MS and gel filtration
-
?
additional information

?
-
eIF5A occurs in tumor cells, and it also acts as a cofactor of the Rev transactivator protein in HIV-1-infected cells
-
-
?
additional information
?
-
-
eIF5A occurs in tumor cells, and it also acts as a cofactor of the Rev transactivator protein in HIV-1-infected cells
-
-
?
additional information
?
-
-
DOHH hydroxylates deoxyhypusine and irreversibly completes the hypusination process, the eukaryotic translation initiation factor eIF-5A is the sole known target of hypusination
-
-
?
additional information
?
-
-
substrate specifc bindign of recombinant wild-type and mutant enzymes, overview
-
-
?
additional information
?
-
-
DOHH hydroxylates the deoxyhypusyl-eukaryotic translation initiation factor eIF5A intermediate to hyposine-containing mature eIF5A using molecular oxygen
-
-
?
additional information
?
-
DOHH activity completes hypusine biosynthesis via hydroxylation and thereby completes eukaryotic translation initiation factor eIF-5A formation
-
-
?
additional information
?
-
-
DOHH activity completes hypusine biosynthesis via hydroxylation and thereby completes eukaryotic translation initiation factor eIF-5A formation
-
-
?
additional information
?
-
-
purified DOHH protein displays no phycocyanin lyase activity
-
-
?
additional information
?
-
-
following mutants of human eIF-5A are substrates for DOHH - K47A, K47R, G49A, G52A, K55A, P74A, L91A and L101A
-
-
?
additional information
?
-
-
Lia1 contains HEAT-like repeats with a role for mediating protein-protein interactions
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
eIF5A-N6-(4-aminobutyl)-L-lysine + AH2 + O2
eIF5A-N6-(4-amino-2-hydroxybutyl)-L-lysine + A + H2O
eIF5A-Nepsilon-(4-aminobutyl)lysine + AH2 + O2
eIF5A-Nepsilon-(4-amino-2-hydroxybutyl)lysine + A + H2O
eukaryotic translation initiation factor eIF-5A deoxyhypusine + O2 + AH2
eukaryotic translation initiation factor eIF-5A hypusine + H2O + A
[eIF5A]-deoxyhypusine + AH2 + O2
[eIF5A]-hypusine + A + H2O
[eIF5A]-deoxyhypusine + NADH + H+ + O2
[eIF5A]-hypusine + NAD+ + H2O
-
-
-
-
?
additional information
?
-
eIF5A-N6-(4-aminobutyl)-L-lysine + AH2 + O2

eIF5A-N6-(4-amino-2-hydroxybutyl)-L-lysine + A + H2O
-
-
-
-
?
eIF5A-N6-(4-aminobutyl)-L-lysine + AH2 + O2
eIF5A-N6-(4-amino-2-hydroxybutyl)-L-lysine + A + H2O
-
the unique posttranslational modification occurs in only one cellular protein, the eukaryotic translation initiation factor 5A, eIF5A
-
-
?
eIF5A-N6-(4-aminobutyl)-L-lysine + AH2 + O2
eIF5A-N6-(4-amino-2-hydroxybutyl)-L-lysine + A + H2O
-
different eIF5A isozymes exist. The unique posttranslational modification occurs in only one cellular protein, the eukaryotic translation initiation factor 5A, eIF5A
-
-
?
eIF5A-N6-(4-aminobutyl)-L-lysine + AH2 + O2
eIF5A-N6-(4-amino-2-hydroxybutyl)-L-lysine + A + H2O
-
-
-
-
?
eIF5A-N6-(4-aminobutyl)-L-lysine + AH2 + O2
eIF5A-N6-(4-amino-2-hydroxybutyl)-L-lysine + A + H2O
-
the unique posttranslational modification occurs in only one cellular protein, the eukaryotic translation initiation factor 5A, eIF5A
-
-
?
eIF5A-N6-(4-aminobutyl)-L-lysine + AH2 + O2
eIF5A-N6-(4-amino-2-hydroxybutyl)-L-lysine + A + H2O
-
-
-
-
?
eIF5A-N6-(4-aminobutyl)-L-lysine + AH2 + O2
eIF5A-N6-(4-amino-2-hydroxybutyl)-L-lysine + A + H2O
-
different eIF5A isozymes exist. The unique posttranslational modification occurs in only one cellular protein, the eukaryotic translation initiation factor 5A, eIF5A
-
-
?
eIF5A-N6-(4-aminobutyl)-L-lysine + AH2 + O2
eIF5A-N6-(4-amino-2-hydroxybutyl)-L-lysine + A + H2O
-
the DOHH reaction is irreversible
-
-
ir
eIF5A-N6-(4-aminobutyl)-L-lysine + AH2 + O2
eIF5A-N6-(4-amino-2-hydroxybutyl)-L-lysine + A + H2O
-
-
-
-
?
eIF5A-N6-(4-aminobutyl)-L-lysine + AH2 + O2
eIF5A-N6-(4-amino-2-hydroxybutyl)-L-lysine + A + H2O
-
-
-
-
?
eIF5A-N6-(4-aminobutyl)-L-lysine + AH2 + O2
eIF5A-N6-(4-amino-2-hydroxybutyl)-L-lysine + A + H2O
-
-
-
-
?
eIF5A-N6-(4-aminobutyl)-L-lysine + AH2 + O2
eIF5A-N6-(4-amino-2-hydroxybutyl)-L-lysine + A + H2O
-
activation of eIF5A
-
-
?
eIF5A-N6-(4-aminobutyl)-L-lysine + AH2 + O2
eIF5A-N6-(4-amino-2-hydroxybutyl)-L-lysine + A + H2O
-
different eIF5A isozymes exist, no activity with eIF5A mutant K51R, that lacks hypusine. The unique posttranslational modification occurs in only one cellular protein, the eukaryotic translation initiation factor 5A, eIF5A
-
-
?
eIF5A-N6-(4-aminobutyl)-L-lysine + AH2 + O2
eIF5A-N6-(4-amino-2-hydroxybutyl)-L-lysine + A + H2O
-
-
-
-
?
eIF5A-N6-(4-aminobutyl)-L-lysine + AH2 + O2
eIF5A-N6-(4-amino-2-hydroxybutyl)-L-lysine + A + H2O
-
the unique posttranslational modification occurs in only one cellular protein, the eukaryotic translation initiation factor 5A, eIF5A
-
-
?
eIF5A-Nepsilon-(4-aminobutyl)lysine + AH2 + O2

eIF5A-Nepsilon-(4-amino-2-hydroxybutyl)lysine + A + H2O
the enzyme catalyzes the maturation of eukaryotic initiation factor 5A, synthesis of hypusine is essential for the function of eIF5A in eukaryotic cell proliferation and survival
-
-
?
eIF5A-Nepsilon-(4-aminobutyl)lysine + AH2 + O2
eIF5A-Nepsilon-(4-amino-2-hydroxybutyl)lysine + A + H2O
-
the enzyme catalyzes the final step of the post-translational synthesis of hypusine, i.e. Nepsilon-(4-amino-2-hydroxybutyl)lysine, in the eukaryotic translation initiation factor 5A, eIF5A
-
-
?
eukaryotic translation initiation factor eIF-5A deoxyhypusine + O2 + AH2

eukaryotic translation initiation factor eIF-5A hypusine + H2O + A
-
-
-
-
?
eukaryotic translation initiation factor eIF-5A deoxyhypusine + O2 + AH2
eukaryotic translation initiation factor eIF-5A hypusine + H2O + A
-
-
-
-
?
[eIF5A]-deoxyhypusine + AH2 + O2

[eIF5A]-hypusine + A + H2O
-
-
-
?
[eIF5A]-deoxyhypusine + AH2 + O2
[eIF5A]-hypusine + A + H2O
-
-
-
?
[eIF5A]-deoxyhypusine + AH2 + O2
[eIF5A]-hypusine + A + H2O
-
-
-
?
[eIF5A]-deoxyhypusine + AH2 + O2
[eIF5A]-hypusine + A + H2O
-
-
-
-
?
[eIF5A]-deoxyhypusine + AH2 + O2
[eIF5A]-hypusine + A + H2O
-
-
-
?
[eIF5A]-deoxyhypusine + AH2 + O2
[eIF5A]-hypusine + A + H2O
-
-
-
-
?
[eIF5A]-deoxyhypusine + AH2 + O2
[eIF5A]-hypusine + A + H2O
-
-
-
ir
[eIF5A]-deoxyhypusine + AH2 + O2
[eIF5A]-hypusine + A + H2O
-
-
-
-
?
[eIF5A]-deoxyhypusine + AH2 + O2
[eIF5A]-hypusine + A + H2O
-
-
-
?
[eIF5A]-deoxyhypusine + AH2 + O2
[eIF5A]-hypusine + A + H2O
-
-
-
?
additional information

?
-
eIF5A occurs in tumor cells, and it also acts as a cofactor of the Rev transactivator protein in HIV-1-infected cells
-
-
?
additional information
?
-
-
eIF5A occurs in tumor cells, and it also acts as a cofactor of the Rev transactivator protein in HIV-1-infected cells
-
-
?
additional information
?
-
-
DOHH hydroxylates deoxyhypusine and irreversibly completes the hypusination process, the eukaryotic translation initiation factor eIF-5A is the sole known target of hypusination
-
-
?
additional information
?
-
-
DOHH hydroxylates the deoxyhypusyl-eukaryotic translation initiation factor eIF5A intermediate to hyposine-containing mature eIF5A using molecular oxygen
-
-
?
additional information
?
-
DOHH activity completes hypusine biosynthesis via hydroxylation and thereby completes eukaryotic translation initiation factor eIF-5A formation
-
-
?
additional information
?
-
-
DOHH activity completes hypusine biosynthesis via hydroxylation and thereby completes eukaryotic translation initiation factor eIF-5A formation
-
-
?
additional information
?
-
-
following mutants of human eIF-5A are substrates for DOHH - K47A, K47R, G49A, G52A, K55A, P74A, L91A and L101A
-
-
?
additional information
?
-
-
Lia1 contains HEAT-like repeats with a role for mediating protein-protein interactions
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Fe3+
-
1.5-fold activation at 0.001 mM
Fe2+

-
required, active site-bound
Fe2+
-
the enzyme contains a nonheme diiron active center that activates O2
Fe2+
-
the enzyme contains a nonheme diiron active center that activates O2
Fe2+
-
required, active site-bound
Fe2+
-
the enzyme contains a nonheme diiron active center that activates O2
Fe2+
-
1.5-fold activation at 0.001 mM
Fe2+
-
a non-heme iron enzyme, DOHH probably contains one binuclear, diiron, active center, iron-binding active site structure of DOHH and mode of iron binding, the strictly conserved His-Glu motifs His56-Glu57, His89-Glu90, His207-Glu208 and His240-Glu241, are involved in iron binding, overview
Fe2+
-
required, active site-bound
Fe2+
-
the enzyme contains a nonheme diiron active center that activates O2
Fe2+
non-heme diiron enzyme
Fe2+
-
required, active site-bound
Fe2+
-
required, active site-bound
Fe2+
-
required, active site-bound
Fe2+
-
required, essential structural role for iron binding in addition to its contribution to the catalysis of hypusine formation in the eIF-5A precursor. Lia1 is an iron metalloenzyme. Determination of metal contents in purified enzyme samples, overview. The apoenzyme has a larger hydrodynamic size than the holoenzyme
Fe2+
-
the enzyme contains a nonheme diiron active center that activates O2
Fe2+
-
required, active site-bound
Fe2+
-
the enzyme contains a nonheme diiron active center that activates O2
Iron

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Iron
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2 mol of iron per mol of enzyme
Iron
dinuclear iron enzyme
Iron
non-heme diiron enzyme
additional information

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iron cannot be replaced by Cd2+, Co2+, Cr2+, Cu2+, Mg2+, Mn2+, Ni2+, Zn2+
additional information
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Lia1 contains no cadmium, cobalt, chromium, copper, magnesium, manganese, nickel and zinc
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1,10-Diaminodecane
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94% of initial activity at 2 mM
1,10-phenanthroline
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complete inhibition at 0.01 mM
1,3-diaminopropane
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86% of initial activity at 0.5 mM
1,6-diaminohexane
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97% of initial activity at 2 mM
1,7-Diaminoheptane
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91% of initial activity at 2 mM
1,8-diaminooctane
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93% of initial activity at 2 mM
2,3-Dihydroxybenzoic acid
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slight inhibition at 2 mM
2-(2-hydroxy-5-methylphenyl)-1,3-thiazole-4-carboxylic acid
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inhibition in vitro and in cells
2-(2-hydroxy-5-methylphenyl)-4,5-dihydro-1,3-thiazole-4-carboxylic acid
2-(4-methoxyphenyl)-6-[[2-(4-methoxyphenyl)-3H-benzimidazol-5-yl]methyl]-1H-benzimidazole
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94.1% inhibition at 0.002 mM
3,4-dihydroxybenzoic acid
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above 50% inhibition at 2 mM
4,6-diphenyl-1-hydroxy-pyridine-2-one
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IC50 0.0007 mM
alkyl 4-oxo-piperidine 3 carboxylates
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structurally related to dihydropyrimidines, most potent, putative DOHH inhibitors in vitro
CaCl2
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98% of initial activity at 0.005 mM
cadaverine
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87% of initial activity at 0.5 mM
caldine
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47% of initial activity at 0.5 mM
deferoxamine
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targets the active metalloenzyme and inhibits DOHH in human vascular endothelial cells
desferrioxamine B
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IC50 0.016 mM
desferrioxamine mesylate
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ethyl 3,4-dihydroxybenzoate
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IC50 0.5 mM
FeCl3
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65% of initial activity at 0.005 mM
FeSO4
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13% of initial activity at 0.005 mM
Lys-Thr-Gly-deoxyhypusine-His-Gly-His-Ala-Lys
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competitive inhibition
methyl 2,3-dihydroxybenzoate
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IC50 1.6 mM
metipirox
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IC50 0.0028 mM
Mn(C2H3O2)2
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above 0.001 mM
MnCl2
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64% of initial activity at 0.005 mM
N''-guanyl-1,7-diaminoheptane
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competitive inhibition
N-(2-cyanoethyl)butane-1,4-diamine
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80% of initial activity at 2 mM
N-(3-cyanopropyl)propane-1,3-diamine
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79% of initial activity at 2 mM
N-phenyl-1-[1-(phenylmethyl)benzimidazol-2-yl]diazenylnaphthalen-2-amine
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87.6% inhibition at 0.002 mM
N-[4-(3,4-diethoxyphenyl)-1,2,5-oxadiazole-3-yl]-3-methylbenzamide
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92.6% inhibition at 0.002 mM
N1-acetyl-L-Orn-L-Pro-Gly
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above 2 mM
N1-acetyl-N4-(2,3-dihydroxybenzoyl)-L-Orn-L-Pro-Gly
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IC50 0.2 mM
N1-acetyl-N4-(3,4-dihydroxybenzoyl)-L-Orn-L-Pro-Gly
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IC50 0.03 mM
Ni(C2H3O2)2
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above 0.001 mM
NiSO4
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72% of initial activity at 0.005 mM
putrescine
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85% of initial activity at 0.5 mM
pyridine 2,3-dicarboxylate
Pyridine 2,4-dicarboxylate
Pyridine 2,5-dicarboxylate
Pyridine 3,4-dicarboxylate
Pyridine 3,5-dicarboxylate
spermidine
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58% of initial activity at 0.5 mM
spermine
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41% of initial activity at 0.5 mM
thermine
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35% of initial activity at 0.5 mM
Zn(C2H3O2)2
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above 0.01 mM
ZnCl2
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93% of initial activity at 0.005 mM
2,2'-dipyridyl

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2,2'-dipyridyl
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IC50 0.026 mM
2,2'-dipyridyl
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IC50 0.029 mM
2,2'-dipyridyl
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targets the active metalloenzyme and inhibits DOHH in human vascular endothelial cells
2-(2-hydroxy-5-methylphenyl)-4,5-dihydro-1,3-thiazole-4-carboxylic acid

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inhibition in vitro and in cells
2-(2-hydroxy-5-methylphenyl)-4,5-dihydro-1,3-thiazole-4-carboxylic acid
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inhibition in vitro and in cells
ciclopirox

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IC50 0.005 mM, complete inhibition above 0.01 mM
ciclopirox
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IC50 0.0006 mM
ciclopirox
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CPX, topical fungicide
ciclopirox
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targets the active metalloenzyme and inhibits DOHH in human vascular endothelial cells
Co(C2H3O2)2

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above 0.01 mM