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2-methyl-2,4-pentanediol
8.5 mM, 94% residual activity. the sequence contains several binding sites for 2-methyl-2,4-pentanediol
2-Methyleneglutarate
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potent competitive inhibitor
3,3'-[(2-bromobenzene-1,4-diyl)di(E)ethene-2,1-diyl]bis(6-hydroxybenzoic acid)
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i.e. BSB
3-(3,5-dibromo)-4-hydroxybenzylidine-5-iodo-1,3-dihydro-indol-2-one
5,5'-dithiobis(2-nitrobenzoate)
alpha,gamma-Diethyl glutamate
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ATP/GTP-competitive inhibitor of casein kinase-2
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aurintricarboxylic acid
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D-asparagine
93% activity in the presence of 10 mM D-asparagine
D-Aspartate
90% activity in the presence of 10 mM D-aspartate
D-glutamine
95% activity in the presence of 10 mM D-glutamine
diethyl dicarbonate
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inactivation follows pseudo-first-order kinetics
DTNB
inactivation via blocking of the only two Cys residues, Cys144 in helix alpha7a of domain I, the substrate-binding domain, and Cys320 in a loop that connects betak and alpha13 in domain II, the coenzyme-binding domain
epicatechin-3-monogallate
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epicatechin-monogallate
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epigallocatechin-3,5-digallate
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epigallocatechin-3-gallate
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ethaverine hydrochloride
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ethyl acetimidate
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inactivation with ethyl acetimidate shows pseudo-first-order kinetics
glutathione
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reduces increase in GDH activity due to Hg
glycogen accumulation regulator
GarA, native or unphosphorylated GarA is able to interact with NAD+-GDH causing a reduction in NAD+-GDH activity by altering the affinity of the enzyme for its substrate. This binding is prevented by the phosphorylation of GarA by PknG
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guanidine hydrochloride
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72°C, almost complete loss of activity by addition of more than 3 M
KCl
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3 M, 75% inhibition
L-glutamate
substrate inhibition at L-glutamate concentrations above 20 mM
L-glutamine
89% activity in the presence of 10 mM L-glutamine
L-ornithine
83% activity in the presence of 10 mM L-ornithine
N-alpha-p-tosyl-L-lysine chloromethyl ketone
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TLCK
NaCl
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3 M, 89% inhibition
NADP+
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non-competitive versus L-glutamate, non-competitive versus NAD+
NADPH
the wrong cofactor, NADPH, without the correct binding pocket to receive its 2'-phosphate, finds an alternative and catalytically unproductive way of occupying the coenzyme site
p-Aminomercuribenzoate
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p-chloromercuribenzoate
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phosphoenolpyruvate
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weak
Tetranitromethane
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rapid loss of enzymatic activity versus time at various concentrations of modifier, showing pseudo-first-order kinetics
2-oxoglutarate
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non-competitive versus L-glutamate, competitive versus NAD+
2-oxoglutarate
substrate inhibition
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
3-(3,5-dibromo)-4-hydroxybenzylidine-5-iodo-1,3-dihydro-indol-2-one
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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
3-(3,5-dibromo)-4-hydroxybenzylidine-5-iodo-1,3-dihydro-indol-2-one
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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
5,5'-dithiobis(2-nitrobenzoate)
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5,5'-dithiobis(2-nitrobenzoate)
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5,5'-dithiobis(2-nitrobenzoate)
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5,5'-dithiobis(2-nitrobenzoate)
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ADP
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Al3+
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as increasing the Al3+ concentration, the activity of GDH is firstly inhibited (at less than 0.03 mM), then activated (0.03-0.08 mM), and finally inhibited (above 0.08 mM) in the Tris-HCl buffer solution at pH 6.5 and 7.5
Al3+
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inhibits the enzyme activity in the absence of Hg
AMP
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ATP
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weak
bithionol
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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
bithionol
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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
bithionol
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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
Ca2+
0.1 mM, 82% residual activity; 8% inhibition at 0.1 mM, 23% at 1 mM
Ca2+
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activation of reductive amination; slight inhibition of oxidative deamination
Ca2+
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activation of reductive amination; no effect on oxidative deamination
citrate
67% activity in the presence of 10 mM citrate
citrate
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inhibition of amination, no effect on deamination
Co2+
0.1 mM, 77% residual activity; 23% inhibition at 0.1 mM
Co2+
82% activity in the presence of 1 mM Co2+
Cu2+
0.1 mM, 65% residual activity; 35% inhibition at 0.1 mM
D-glutamate
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non-competitive versus L-glutamate, non-competitive versus NAD+
D-glutamate
94% activity in the presence of 10 mM D-glutamate
EDTA
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fumarate
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amination
fumarate
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non-competitive versus L-glutamate, competitive versus NAD+
fumarate
32% activity in the presence of 10 mM fumarate
glutamate
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glutamine
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amination
glutamine
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reduces increase in GDH activity due to Hg
Glutarate
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uncompetitive versus L-glutamate, competitive versus NAD+
Glutarate
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competitive inhibitor
GTP
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Hexachlorophene
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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
Hexachlorophene
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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
Hexachlorophene
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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
Hg2+
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Hg2+
no activity in the presence of 1 mM Hg2+
Hg2+
1 mM, complete loss of activtiy for wild-type. 8fold increase in activity for mutant C1141T
isocitrate
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isocitrate
49% activity in the presence of 10 mM isocitrate
isophthalate
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isophthalate
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potent in vitro inhibitor
L-aspartate
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weak
malate
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non-competitive versus L-glutamate, non-competitive versus NAD+
malate
65% activity in the presence of 10 mM malate
malate
10 mM, 75% residual activity
Mg2+
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Mg2+
64% activity in the presence of 1 mM Mg2+
Mn2+
52% activity in the presence of 1 mM Mn2+
N-ethylmaleimide
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NAD+
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NADH
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NH4+
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Ni2+
77% activity in the presence of 1 mM Ni2+
oxaloacetate
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amination
oxaloacetate
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non-competitive versus L-glutamate, non-competitive versus NAD+
oxaloacetate
10 mM, 60% residual activity
p-hydroxymercuribenzoate
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p-hydroxymercuribenzoate
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pyridoxal 5'-phosphate
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pyridoxal 5'-phosphate
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pyridoxal 5'-phosphate
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Pyruvic acid
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succinate
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non-competitive versus L-glutamate, non-competitive versus NAD+
succinate
36% activity in the presence of 10 mM succinate
Zn2+
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Zn2+
0.1 mM, 51% residual activity; 49% inhibition at 0.1 mM
additional information
not inhibitory: Mn2+
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additional information
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not inhibitory: Mn2+
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additional information
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no inhibition or activation in the presence of 500 mM AMP, ADP, ATP, cyclic-AMP, GMP, GDP or GTP
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additional information
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GTP, ATP, ADP and AMP do not affect the activity
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additional information
not inhibited by NAD+
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additional information
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not inhibited by NAD+
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additional information
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Met sulfoximine and azaserine do not affect the aminating and deaminating activities of GDH
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additional information
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strong inhibition by increasing ionic strength
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additional information
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increase in GDH activity due to Hg remains unaffected by the supply of sucrose
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additional information
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no inhibition by GTP
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