Inhibitors | Comment | Organism | Structure |
---|---|---|---|
(2S)-2-[[4-(propan-2-yl)phenyl]sulfanyl]propanenitrile | - |
Mycobacterium leprae | |
1-tert-butyl-4-[(difluoromethyl)sulfanyl]benzene | - |
Mycobacterium leprae | |
1-[(1S,2S)-2-(bromomethyl)cyclopropyl]-4-[(trifluoromethyl)sulfanyl]benzene | - |
Mycobacterium leprae | |
3-[(4-tert-butylphenyl)sulfanyl]propane-1-thiol | - |
Mycobacterium leprae | |
4,4'-sulfanediylbis[2-(propan-2-yl)phenol] | - |
Mycobacterium leprae | |
4-(4-hydroxy-3-isopropylphenylthio)-2-isopropylphenol | competitive to L-aspartate 4-semialdehyde, enzyme binding structure anaysis from crystal structure, overview | Mycobacterium leprae | |
additional information | inhibitor docking study, overview | Mycobacterium leprae |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
L-homoserine + NADP+ | Mycobacterium leprae | - |
L-aspartate 4-semialdehyde + NADPH + H+ | - |
r | |
L-homoserine + NADP+ | Mycobacterium leprae TN | - |
L-aspartate 4-semialdehyde + NADPH + H+ | - |
r |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Mycobacterium leprae | P46806 | - |
- |
Mycobacterium leprae TN | P46806 | - |
- |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
L-homoserine + NADP+ | - |
Mycobacterium leprae | L-aspartate 4-semialdehyde + NADPH + H+ | - |
r | |
L-homoserine + NADP+ | - |
Mycobacterium leprae TN | L-aspartate 4-semialdehyde + NADPH + H+ | - |
r |
Subunits | Comment | Organism |
---|---|---|
More | structure homology modelling, three-dimensional structure analysis and molecular dynamics simulation, overview | Mycobacterium leprae |
Synonyms | Comment | Organism |
---|---|---|
HSD | - |
Mycobacterium leprae |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
NADP+ | - |
Mycobacterium leprae | |
NADPH | - |
Mycobacterium leprae |
Ki Value [mM] | Ki Value maximum [mM] | Inhibitor | Comment | Organism | Structure |
---|---|---|---|---|---|
0.00963 | - |
1-[(1S,2S)-2-(bromomethyl)cyclopropyl]-4-[(trifluoromethyl)sulfanyl]benzene | pH and temperature not specified in the publication | Mycobacterium leprae | |
0.01 | - |
4-(4-hydroxy-3-isopropylphenylthio)-2-isopropylphenol | pH and temperature not specified in the publication | Mycobacterium leprae | |
0.01307 | - |
1-tert-butyl-4-[(difluoromethyl)sulfanyl]benzene | pH and temperature not specified in the publication | Mycobacterium leprae | |
0.0131 | - |
(2S)-2-[[4-(propan-2-yl)phenyl]sulfanyl]propanenitrile | pH and temperature not specified in the publication | Mycobacterium leprae | |
0.01568 | - |
3-[(4-tert-butylphenyl)sulfanyl]propane-1-thiol | pH and temperature not specified in the publication | Mycobacterium leprae |
IC50 Value | IC50 Value Maximum | Comment | Organism | Inhibitor | Structure |
---|---|---|---|---|---|
0.0051 | - |
pH and temperature not specified in the publication | Mycobacterium leprae | 4-(4-hydroxy-3-isopropylphenylthio)-2-isopropylphenol |
General Information | Comment | Organism |
---|---|---|
additional information | structure homology modelling using the template, homoserine dehydrogenase from Thiobacillus denitrificans, PDB ID 3MTJ, three-dimensional structure analysis and molecular dynamics simulation, overview. Identification of substrate- and cofactor-binding regions. In L-aspartate semialdehyde binding, the substrate docks to the protein involving residues Thr163, Asp198, and Glu192, which may be important because they form a hydrogen bond with the enzyme. Key recognition residues are Lys107 and Lys207 | Mycobacterium leprae |