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Literature summary for 1.4.1.2 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
Search for more literature for 1.4.1.2

Crystallization (Commentary)

Crystallization (Comment) Organism
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

Inhibitors Comment Organism Structure
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
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
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
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
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
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
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
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
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]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
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
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
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
0.26
-
 NAD+ 0.009 mM inhibitor biothionol, Vmax: 0.05, pH 7.5 Bos taurus
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
0.31
-
 NAD+ without inhibitor biothionol, Vmax: 0.24, pH 7.5 Bos taurus
0.36
-
 NAD+ 0.005 mM inhibitor biothionol, Vmax: 0.13, pH 7.5 Bos taurus
0.39
-
 L-glutamate 0.009 mM inhibitor biothionol, Vmax: 0.05, pH 7.5 Bos taurus
0.43
-
 NAD+ 0.003 mM inhibitor biothionol, Vmax: 0.22, pH 7.5 Bos taurus
1.06
-
 L-glutamate 0.005 mM inhibitor biothionol, Vmax: 0.1, pH 7.5 Bos taurus
1.17
-
 L-glutamate 0.003 mM inhibitor biothionol, Vmax: 0.14, pH 7.5 Bos taurus
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
1.38
-
 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
1.38
-
 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
1.53
-
 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
1.62
-
 L-glutamate without inhibitor biothionol, Vmax: 0.18, pH 7.5 Bos taurus

Organism

Organism UniProt Comment Textmining
Bos taurus P00366
-
-
Escherichia coli
-
-
-
Tetrahymena
-
-
-

Substrates and Products (Substrate)

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

Synonyms

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

pH Optimum

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

IC50 Value

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