EC Number |
Inhibitors |
Structure |
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1.14.99.29 | more |
no inhibition by CuSO4, HgCl2, MgCl2, CdSO4 at 0.005 mM; partial reconstitution of 0.01 mM 1,10-phenanthroline inhibited activity with Co(C2H3O2)2 at 0.03 mM or FeSO4 at 0.005 mM |
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1.14.99.29 | more |
no inhibition by 2-oxoglutarate, 2-oxoadipinate, 2-oxosuccinate, 3-oxoglutarate, glutarate, malonate, pyruvate |
|
1.14.99.29 | more |
no inhibition by S-isomers of kojic acid, 3-pyridylalanine, 4-pyridylalanine at 0.3 mM in vitro and at 0.2 mM in cells, no inhibition by 2-(2-aminophenyl)-1,3-thiazole-4-carboxylic acid at 0.4 mM in cells |
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1.14.99.29 | more |
partial reconstitution of chelator inhibited activity with CuCl2 or Zn(C2H3O2)2 |
|
1.14.99.29 | more |
no inhibition at 2 mM N-(2-cyanopropyl)-3-cyanopropylamine |
|
1.14.99.29 | more |
partial reconstitution of 0.01 mM 1,10-phenanthroline inhibited activity with Co(C2H3O2)2 at 0.03 mM or FeSO4 at 0.005 mM |
|
1.14.99.29 | more |
a number of metal-chelating inhibitors of DOHH causes growth inhibition and G1 cell cycle arrest in mammalian cells |
|
1.14.99.29 | more |
design of inhibitors against the human parasite enzyme from Plasmodium falciparum might profit from structural differences and the five HEAT-like repeats present in the parasite DOHH that differ in number and amino acid identity from its human orthologue, which contains four repeats |
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1.14.99.29 | more |
design of inhibitors against the parasite enzyme might profit from structural differences and the five HEAT-like repeats present in the parasite DOHH that differ in number and amino acid identity from its human orthologue, which contains four repeats. Compounds related structurally to dihydropyrimidines, like the plant amino acid mimosine and the antifungal drug ciclopiroxolamine, are toxic and/or not effective in vivo as anti-malarial drugs in rodents |
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1.14.99.29 | more |
the active site is blocked by two catecholpeptides containing alpha 3,4-dihydroxybenzoyl- and alpha 2,3-dihydroxybenzoyl moiety. The 3,4-dihydroxybenzoyl-containing compound is more potent with a Ki of 32 mM |
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