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Literature summary extracted from

  • Li, M.; Smith, C.J.; Walker, M.T.; Smith, T.J.
    Novel inhibitors complexed with glutamate dehydrogenase: allosteric regulation by control of protein dynamics (2009), J. Biol. Chem., 284, 22988-23000.
    View publication on PubMedView publication on EuropePMC

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
1.4.1.2 co-crystallization of GDH with hexachlorophene and 3-(3,5-dibromo)-4-hydroxybenzylidine-5-iodo-1,3-dihydro-indol-2-one is performed using the hanging drop, vapor-diffusion method at room temperature. In both cases, the drops are formed using a 1:1 mix of protein and reservoir solutions Bos taurus

Inhibitors

EC Number Inhibitors Comment Organism Structure
1.4.1.2 3-(3,5-dibromo)-4-hydroxybenzylidine-5-iodo-1,3-dihydro-indol-2-one inhibits GDH in a non-competitive manner with the Vmax being greatly affected without a very large change in Km. Crystal structures discloses that 3-(3,5-dibromo)-4-hydroxybenzylidine-5-iodo-1,3-dihydro-indol-2-one or bithionol, respectively, bind as pairs of stacked compounds at hexameric 2-fold axes between the dimers of subunits Bos taurus
1.4.1.2 3-(3,5-dibromo)-4-hydroxybenzylidine-5-iodo-1,3-dihydro-indol-2-one inhibits GDH in a non-competitive manner with the Vmax being greatly affected without a very large change in Km. Crystal structures discloses that 3-(3,5-dibromo)-4-hydroxybenzylidine-5-iodo-1,3-dihydro-indol-2-one or bithionol, respectively, bind as pairs of stacked compounds at hexameric 2-fold axes between the dimers of subunits Escherichia coli
1.4.1.2 3-(3,5-dibromo)-4-hydroxybenzylidine-5-iodo-1,3-dihydro-indol-2-one inhibits GDH in a non-competitive manner with the Vmax being greatly affected without a very large change in Km. Crystal structures discloses that 3-(3,5-dibromo)-4-hydroxybenzylidine-5-iodo-1,3-dihydro-indol-2-one or bithionol, respectively, bind as pairs of stacked compounds at hexameric 2-fold axes between the dimers of subunits Tetrahymena
1.4.1.2 bithionol inhibits GDH in a non-competitive manner with the Vmax being greatly affected without a very large change in Km. Crystal structures discloses that 3-(3,5-dibromo)-4-hydroxybenzylidine-5-iodo-1,3-dihydro-indol-2-one or bithionol, respectively, bind as pairs of stacked compounds at hexameric 2-fold axes between the dimers of subunits Bos taurus
1.4.1.2 bithionol inhibits GDH in a non-competitive manner with the Vmax being greatly affected without a very large change in Km. Crystal structures discloses that 3-(3,5-dibromo)-4-hydroxybenzylidine-5-iodo-1,3-dihydro-indol-2-one or bithionol, respectively, bind as pairs of stacked compounds at hexameric 2-fold axes between the dimers of subunits Escherichia coli
1.4.1.2 bithionol inhibits GDH in a non-competitive manner with the Vmax being greatly affected without a very large change in Km. Crystal structures discloses that 3-(3,5-dibromo)-4-hydroxybenzylidine-5-iodo-1,3-dihydro-indol-2-one or bithionol, respectively, bind as pairs of stacked compounds at hexameric 2-fold axes between the dimers of subunits Tetrahymena
1.4.1.2 Hexachlorophene inhibits GDH in a non-competitive manner with the Vmax being greatly affected without a very large change in Km. Crystal structures discloses that hexachlorophene forms a ring around the internal cavity in GDH through aromatic stacking interactions between the drug and GDH as well as between the drug molecules themselves Bos taurus
1.4.1.2 Hexachlorophene inhibits GDH in a non-competitive manner with the Vmax being greatly affected without a very large change in Km. Crystal structures discloses that hexachlorophene forms a ring around the internal cavity in GDH through aromatic stacking interactions between the drug and GDH as well as between the drug molecules themselves Escherichia coli
1.4.1.2 Hexachlorophene inhibits GDH in a non-competitive manner with the Vmax being greatly affected without a very large change in Km. Crystal structures discloses that hexachlorophene forms a ring around the internal cavity in GDH through aromatic stacking interactions between the drug and GDH as well as between the drug molecules themselves Tetrahymena

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.4.1.2 0.14
-
 NAD+ 0.008 mM inhibitor 3-(3,5-dibromo)-4-hydroxybenzylidine-5-iodo-1,3-dihydro-indol-2-one, Vmax: 0.04, pH 7.5 Bos taurus
1.4.1.2 0.23
-
 NAD+ 0.0015 mM inhibitor 3-(3,5-dibromo)-4-hydroxybenzylidine-5-iodo-1,3-dihydro-indol-2-one, Vmax: 0.13, pH 7.5 Bos taurus
1.4.1.2 0.26
-
 NAD+ 0.004 mM inhibitor 3-(3,5-dibromo)-4-hydroxybenzylidine-5-iodo-1,3-dihydro-indol-2-one, Vmax: 0.09, pH 7.5 Bos taurus
1.4.1.2 0.26
-
 NAD+ 0.009 mM inhibitor biothionol, Vmax: 0.05, pH 7.5 Bos taurus
1.4.1.2 0.31
-
 NAD+ without inhibitor 3-(3,5-dibromo)-4-hydroxybenzylidine-5-iodo-1,3-dihydro-indol-2-one, Vmax: 0.24, pH 7.5 Bos taurus
1.4.1.2 0.31
-
 NAD+ without inhibitor biothionol, Vmax: 0.24, pH 7.5 Bos taurus
1.4.1.2 0.36
-
 NAD+ 0.005 mM inhibitor biothionol, Vmax: 0.13, pH 7.5 Bos taurus
1.4.1.2 0.39
-
 L-glutamate 0.009 mM inhibitor biothionol, Vmax: 0.05, pH 7.5 Bos taurus
1.4.1.2 0.43
-
 NAD+ 0.003 mM inhibitor biothionol, Vmax: 0.22, pH 7.5 Bos taurus
1.4.1.2 1.06
-
 L-glutamate 0.005 mM inhibitor biothionol, Vmax: 0.1, pH 7.5 Bos taurus
1.4.1.2 1.17
-
 L-glutamate 0.003 mM inhibitor biothionol, Vmax: 0.14, pH 7.5 Bos taurus
1.4.1.2 1.27
-
 L-glutamate 0.008 mM inhibitor 3-(3,5-dibromo)-4-hydroxybenzylidine-5-iodo-1,3-dihydro-indol-2-one, Vmax: 0.05, pH 7.5 Bos taurus
1.4.1.2 1.38
-
 L-glutamate 0.0015 mM inhibitor 3-(3,5-dibromo)-4-hydroxybenzylidine-5-iodo-1,3-dihydro-indol-2-one, Vmax: 0.13, pH 7.5 Bos taurus
1.4.1.2 1.38
-
 L-glutamate without inhibitor 3-(3,5-dibromo)-4-hydroxybenzylidine-5-iodo-1,3-dihydro-indol-2-one, Vmax: 0.17, pH 7.5 Bos taurus
1.4.1.2 1.53
-
 L-glutamate 0.004 mM inhibitor 3-(3,5-dibromo)-4-hydroxybenzylidine-5-iodo-1,3-dihydro-indol-2-one, Vmax: 0.09, pH 7.5 Bos taurus
1.4.1.2 1.62
-
 L-glutamate without inhibitor biothionol, Vmax: 0.18, pH 7.5 Bos taurus

Organism

EC Number Organism UniProt Comment Textmining
1.4.1.2 Bos taurus P00366
-
-
1.4.1.2 Escherichia coli
-
-
-
1.4.1.2 Tetrahymena
-
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.4.1.2 L-glutamate + NAD+ + H2O
-
 Escherichia coli 2-oxoglutarate + NADH + NH3
-
 ?
1.4.1.2 L-glutamate + NAD+ + H2O
-
 Bos taurus 2-oxoglutarate + NADH + NH3
-
 ?
1.4.1.2 L-glutamate + NAD+ + H2O
-
 Tetrahymena 2-oxoglutarate + NADH + NH3
-
 ?

Synonyms

EC Number Synonyms Comment Organism
1.4.1.2 GDH
-
 Escherichia coli
1.4.1.2 GDH
-
 Bos taurus
1.4.1.2 GDH
-
 Tetrahymena
1.4.1.2 glutamate dehydrogenase
-
 Escherichia coli
1.4.1.2 glutamate dehydrogenase
-
 Bos taurus
1.4.1.2 glutamate dehydrogenase
-
 Tetrahymena

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
1.4.1.2 7.5
-
 assay at Escherichia coli
1.4.1.2 7.5
-
 assay at Bos taurus
1.4.1.2 7.5
-
 assay at Tetrahymena

IC50 Value

EC Number IC50 Value IC50 Value Maximum Comment Organism Inhibitor Structure
1.4.1.2 0.0015
-
 pH 7.5 Bos taurus 3-(3,5-dibromo)-4-hydroxybenzylidine-5-iodo-1,3-dihydro-indol-2-one
1.4.1.2 0.0019
-
 pH 7.5 Tetrahymena Hexachlorophene
1.4.1.2 0.0026
-
 pH 7.5 Tetrahymena 3-(3,5-dibromo)-4-hydroxybenzylidine-5-iodo-1,3-dihydro-indol-2-one
1.4.1.2 0.0039
-
 pH 7.5 Bos taurus Hexachlorophene
1.4.1.2 0.0048
-
 pH 7.5 Bos taurus bithionol
1.4.1.2 0.0059
-
 pH 7.5 Tetrahymena bithionol
1.4.1.2 0.012
-
 pH 7.5 Escherichia coli Hexachlorophene
1.4.1.2 0.017
-
 pH 7.5 Escherichia coli bithionol
1.4.1.2 0.1
-
 value above 100, pH 7.5 Escherichia coli 3-(3,5-dibromo)-4-hydroxybenzylidine-5-iodo-1,3-dihydro-indol-2-one