EC Number   |
Inhibitors |
Structure |
|---|
   3.3.2.6 | N-[4-(3-chlorophenyl)-2,5-dioxopiperazin-1-yl]-2-[[4-methyl-5-(pyridin-4-yl)-4H-1,2,4-triazol-3-yl]sulfanyl]acetamide |
compound identified by pharmacophore modeling, binds both human leukotriene hydrolase hLTA4H and the human leukotriene C4 synthase hLTC4S with good binding characteristics |
   |
| 3.3.2.6 | 2-oxo-3-amino carboxylic esters |
contain a transition state mimic of the enzyme-catalyzed amide cleavage as a core and additional complementary components which resemble the hydrophobic nature of the conjugated polyene system of the natural substrate LTA4 |
|
| 3.3.2.6 | more |
drug repurposing of histone deacetylase (HDAC) inhibitors that alleviate neutrophilic inflammation in acute lung injury and idiopathic pulmonary fibrosis via inhibiting leukotriene A4 hydrolase and blocking LTB4 biosynthesis, overview. Analysis of potential inhibitors of LTA4H across a panel of 18 HDAC inhibitors, using enzymatic assay, thermofluor assay, and X-ray crystallographic investigation. Detailed mechanisms of down-regulation of proinflammatory cytokines by SAHA or M344 are determined in vivo. Cotreatment of N-(6-(2-aminophenylamino)-6-oxyhexyl)-4-methylbenzamide and (S)-2-((2S,3R)-3-amino-2-hydroxy-4-phenylbutanamido)-4-methylpentanoic acid synergistically represses the migration of neutrophil and LTB4-induced neutrophil migration is not affected by these treatments. Molecular modeling of HDAC inhibitors against LTA4H hydrolase and aminopeptidase |
|
| 3.3.2.6 | more |
drug repurposing of histone deacetylase (HDAC) inhibitors that alleviate neutrophilic inflammation in acute lung injury and idiopathic pulmonary fibrosis via inhibiting leukotriene A4 hydrolase and blocking LTB4 biosynthesis, overview. Analysis of potential inhibitors of LTA4H across a panel of 18 HDAC inhibitors, using enzymatic assay, thermofluor assay, and X-ray crystallographic investigation. Detailed mechanisms of down-regulation of proinflammatory cytokines by SAHA or M344 are determined in vivo. Cotreatment of N-(6-(2-aminophenylamino)-6-oxyhexyl)-4-methylbenzamide and (S)-2-((2S,3R)-3-amino-2-hydroxy-4-phenylbutanamido)-4-methylpentanoic acid synergistically represses the migration of neutrophil and LTB4-induced neutrophil migration is not affected by these treatments. Molecular modelling of HDAC inhibitors against LTA4H hydrolase and aminopeptidase |
|
| 3.3.2.6 | 1-(2-(4-(2-(trifluoromethyl)phenoxy)phenoxy)ethyl)pyrrolidine |
dual target inhibitor against cyclooxygenase COX-2 and leukotriene A4 hydrolyase in the enzyme assays and the human whole blood assay with IC50 values in the micromolar to submicromolar range. Inhibitor shows good selectivity for COX-2 over COX-1 |
|
| 3.3.2.6 | 1-(2-(4-(2-nitrophenoxy)phenoxy)ethyl)pyrrolidine |
dual target inhibitor against cyclooxygenase COX-2 and leukotriene A4 hydrolyase in the enzyme assays and the human whole blood assay with IC50 values in the micromolar to submicromolar range. Inhibitor shows good selectivity for COX-2 over COX-1 |
|
| 3.3.2.6 | 4-(dimethylamino)-N-[7-(hydroxyamino)-7-oxoheptyl]benzamide |
enzyme binding structure, overview |
|
| 3.3.2.6 | suberanilohydroxamic acid |
enzyme binding structure, overview |
|
| 3.3.2.6 | [6]-gingerol |
from ginger, [6]-gingerol suppresses anchorage-independent cancer cell growth by inhibiting LTA4H activity in HCT116 colorectal cancer cells, overview. [6]-Gingerol specifically binds with LTA4H in vitro and ex vivo |
|
| 3.3.2.6 | [6]-gingerol |
from ginger, [6]-gingerol suppresses anchorage-independent cancer cell growth by inhibiting LTA4H activity in mice, overview. [6]-Gingerol specifically binds with LTA4H in vitro and ex vivo |
|
