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Literature summary for 1.1.1.3 extracted from

  • Zhan, D.; Wang, D.; Min, W.; Han, W.
    Exploring the molecular basis for selective binding of homoserine dehydrogenase from Mycobacterium leprae TN toward inhibitors: a virtual screening study (2014), Int. J. Mol. Sci., 15, 1826-1841.
    View publication on PubMedView publication on EuropePMC

Inhibitors

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/ Products (Substrates)

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

Organism UniProt Comment Textmining
Mycobacterium leprae P46806
-
-
Mycobacterium leprae TN P46806
-
-

Substrates and Products (Substrate)

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

Subunits Comment Organism
More structure homology modelling, three-dimensional structure analysis and molecular dynamics simulation, overview Mycobacterium leprae

Synonyms

Synonyms Comment Organism
HSD
-
Mycobacterium leprae

Cofactor

Cofactor Comment Organism Structure
NADP+
-
Mycobacterium leprae
NADPH
-
Mycobacterium leprae

Ki Value [mM]

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 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

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