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2,4-pyridinedicarboxylate
2-hydroxyethyl disulfide
attenuation of reductive amination (forward) activity but a negligible effect on oxidative deamination (reverse) activity
Ag2+
-
at 1 mM, 60% inhibition
AgNO3
-
1 mM, 30°C, complete loss of aminating activity
BaCl2
-
1 mM, 30°C, 15% loss of aminating activity
benzene-1,3-dicarboxamide
-
-
bis(2,2,2-trifluoroethyl) benzene-1,3-dicarboxylate
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-
CaCl2
-
1 mM, 30°C, 11% loss of aminating activity
CH2ICOOH
-
1 mM, 30°C, 15% loss of aminating activity
cystine
strongly and selectively inhibits the reductive amination reaction
dibenzyl benzene-1,3-dicarboxylate
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dimethyl 4,4'-[1,3-phenylenebis(carbonylazanediyl)]di(cyclopent-2-ene-1-carboxylate)
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dimethyl benzene-1,3-dicarboxylate
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dimethyl ester of isophthalic acid
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dimethyl ester of isophthalate (DMIP), but not isophthalate, inhibits Aspergillus niger growth on agar as well as in liquid culture. This is ascribed to the inability of isophthalate to enter fungal mycelia. Dimethyl ester of isophthalic acid is hydrolysed intracellularly to isophthalate. Subsequent to DMIP addition, intracellular isophthalate can be demonstrated. Addition of NH4+ to DMIP-treated Aspergillus niger mycelia results in intensive vacuolation, retraction of cytoplasm and autolysis
dipropan-2-yl benzene-1,3-dicarboxylate
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dithiothreitol
-
1 mM, 30.7% residual activity
EDTA
-
1 mM, 5.3% residual activity
epigallocatechingallate
EGCG
-
FeSO3(NH4)2SO4
-
1 mM, 30°C, 14% loss of aminating activity
glutamate
-
competitive inhibitor of the amination reaction
Glutaric acid
-
at 20 mM, 25% inhibition
glyoxylate
-
at 20 mM, 30% inhibition
Hexachlorophene
15% inhibition at 0.016 mM; 80% inhibition at 0.016 mM
hydroxylamine
-
competitive inhibitor with ammonia and uncompetitive inhibitor with both 2-oxoglutarate and NADPH
iodoacetamide
-
at 4 mM, complete inactivation
isocitrate
10 M, 64% of initial activity
L-glutamate
-
substrate inhibition above 15 mM
L-Glutamic acid
-
at 20 mM 25% inhibition
L-homoserine
-
competitive inhibitor with respect to both ammonia and glutamine
L-tryptophan
-
at 20 mM, 15% inhibition
N-ethylmaleimide
-
at 0.8 mM, 44% inhibition
N1,N1,N3,N3-tetra(propan-2-yl)benzene-1,3-dicarboxamide
-
-
N1,N3-bis(2-amino-2-oxoethyl)isophthalamide
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-
N1,N3-bis(2-chlorophenyl)benzene-1,3-dicarboxamide
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N1,N3-bis(3,5-dichlorophenyl)benzene-1,3-dicarboxamide
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N1,N3-bis(3-fluorophenyl)benzene-1,3-dicarboxamide
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-
N1,N3-bis(3-hydroxyphenyl)benzene-1,3-dicarboxamide
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N1,N3-bis(4-fluorophenyl)benzene-1,3-dicarboxamide
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N1,N3-bis(4-methoxyphenyl)benzene-1,3-dicarboxamide
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N1,N3-bis(5-tert-butyl-2-hydroxyphenyl)benzene-1,3-dicarboxamide
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N1,N3-bis[3,5-bis(trifluoromethyl)phenyl]benzene-1,3-dicarboxamide
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N1,N3-bis[[3,5-bis(trifluoromethyl)phenyl]methyl]benzene-1,3-dicarboxamide
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N1,N3-dihydroxybenzene-1,3-dicarboxamide
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-
N1,N3-dimethoxybenzene-1,3-dicarboxamide
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-
N1,N3-diphenylbenzene-1,3-dicarboxamide
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-
NAD+
-
0.3 mM, 50.5% residual activity
NADH
-
0.3 mM, 5.3% residual activity
NADP+
-
inhibits at higher 2-oxoglutarate levels
NADPH
-
0.3 mM, 3.8% residual activity
nitrogen assimilation control protein
-
represses the transcription of the gene gdhA
-
p-chloromercuriphenyl sulfonate
-
inactivetes, can be reversed by addition of cysteine
p-hydroxymercuribenzoic acid
Pb2+
-
5 mM, 19.8% residual activity
potassium phosphate
-
over 0.1 M at oxidative deamination
propylselen
inhibits glutamate dehydrogenase by binding at the NADP+ binding site. No inhibition of enzyme mutant P320A
-
pyruvate
-
at 10 mM slight inhibitory
sodium dodecylsulfate
-
at 0.7% w/v after 1 h 5% activity
succinate
-
competitive inhibitor with 2 oxoglutarate, uncompetitive with NADPH and non-competitive with ammonia
2,4-pyridinedicarboxylate
-
-
2,4-pyridinedicarboxylate
-
inhibits less efficiently
2,4-pyridinedicarboxylate
-
weak inhibitor
2-Methyleneglutarate
-
-
2-Methyleneglutarate
-
weak inhibitor
2-oxoglutarate
-
shows allosteric properties and a sigmoid response (nH=2.5) towards 2-oxoglutarate saturation
2-oxoglutarate
-
substrate inhibition above 2.0 mM
2-oxoglutarate
-
competitive inhibitor of the deamination
4-chloromercuribenzoate
-
at 1 mM, 86% inhibition
4-chloromercuribenzoate
-
at 1 mM and 10 mM, 30% inhibition and 100% inhibition
4-chloromercuribenzoate
-
at 0.01 mM, 35% inhibition
ADP
-
at 4 mM slight inhibitory
ADP
-
at 0.3 mM, 22% inhibition of oxidative deamination
ADP
-
at 1 mM, 57% inhibition for oxidative deamination and 23% inhibition for reductive amination respectively
AlCl3
-
1 mM, 30°C, 23% loss of aminating activity
AlCl3
-
at 1 mM, 30% inhibition
AlCl3
-
at 1 mM, 21% inhibition
AMP
-
slight inhibitory
AMP
-
inhibitory at higher concentrations than 1 mM
AMP
-
at 0.3 mM 33% inhibition of oxidative deamination
ATP
-
at 4 mM slight inhibitory
ATP
-
1 mM, 14.4% residual activity
Ca2+
-
at 1 mM 27% inhibition
Ca2+
-
5 mM, 93.5% residual activity
fumarate
-
at 5 mM 20% inhibition
fumarate
-
at 20 mM 30% inhibition
guanidine hydrochloride
-
complete loss of activity
guanidine hydrochloride
-
complete loss of activity
Hg2+
-
at 1 mM, 70% inhibition
Hg2+
-
at 1 mM, 100% activity loss
Hg2+
-
at 1 mM, 10% inhibition
Hg2+
-
at 1 mM, 100% activity loss
Hg2+
1 mM, 76% residual activity
Hg2+
-
at 0.1 mM, complete activity loss
HgCl2
-
1 mM, 30°C, 48% loss of aminating activity
HgCl2
-
at 1 mM, 64% inhibition
HgCl2
-
at 1 mM, 45% inhibition
HgCl2
-
at 0.01 mM, 27% inhibition
HgCl2
-
at 1 mM, no activity, oxidative deamination
isophthalate
-
-
isophthalate
-
a competitive inhibitor of glutamate dehydrogenase, is involved in C and N metabolism
isophthalate
-
potent in vitro inhibitor
isophthalate
-
weak inhibitor
isophthalate
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a competitive inhibitor of glutamate dehydrogenase, is involved in C and N metabolism
isophthalic acid
-
-
KCl
-
500 mM, 80-90% inhibition, by high ionic strength
KCl
100 mM, 45% residual activity
KCl
1 M, 30% loss of activity
malate
-
at 5 mM, 20% inhibition
malate
-
at 20 mM, 30% inhibition
Mg2+
-
at 1 mM, 16% activity loss
Mg2+
-
5 mM, 68% residual activity
Mn2+
-
at 1 mM, 19% activity loss
Mn2+
-
5 mM, 51.8% residual activity
MnCl2
-
at 1 mM, 63% inhibition
MnCl2
-
at 1 mM, 20% inhibition
NaCl
-
50 mM, 50% inhibition. 100 mM, about 60% inhibition. 500 mM, about 90% inhibition by high ionic strength
NaCl
100 mM, 59% residual activity
NH4+
-
-
NH4+
-
inhibits the oxidative deamination activity as a product, inhibition is non-competitive with respect to L-glutamate
oxaloacetate
-
at 20 mM slight inhibitory
oxaloacetate
-
at 20 mM, 60% inhibition
oxaloacetate
10 mM, 63% residual activity
p-hydroxymercuribenzoic acid
-
at 0.08 mM, 50% inhibition
p-hydroxymercuribenzoic acid
-
at 10 mM, 90% inhibition after 40 min
Pb(CH3COO)2
-
at 1 mM, 59% inhibition
Pb(CH3COO)2
-
at 1 mM, 64% inhibition
pyridoxal 5'-phosphate
-
at 10 mM, 90% inhibition, complete protection when 16.8 mM 2-oxoglutarate and 1.68 mM NADP+ are added
pyridoxal 5'-phosphate
-
at 1 mM, 35% inhibition
pyridoxal 5'-phosphate
-
at 1 mM, 45% inhibition
Urea
-
at 0°C 1 h at 2 M 65% inhibition
Urea
-
at 8 M stable for 10 min
Urea
-
no activity at 6 mM
Urea
-
inactivation with 2 mM urea
Urea
-
fully active at 20°C in 8 mM urea
Zn2+
-
at 1 mM, 64% activity loss
Zn2+
-
at 1 mM, 40% inhibition
additional information
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not inhibited by D-glutamate, L-glutamine or DL-2-hydroxyglutarate
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additional information
not inhibitory/activating: oxidized glutathione
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additional information
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not inhibitory/activating: oxidized glutathione
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additional information
structural analogues of L-glutamate, dimethyl esters of isophthalic acid (DMIP) and its derivatives are designed, synthesized and screened for inhibition of NADP-GDH activity as well as YeH transition in Benjaminiella poitrasii, and also in human pathogenic Candida albicans strains, effect of dimethyl esters of isophthalate (DMIP) derivatives on Benjaminiella poitrasii yeast-hypha transition in vivo, overview. The dimethyl esters of isophthalic acid (DMIP) compounds show a more pronounced effect on H-form specific BpNADPGDH II and inhibit YeH transition as well as growth in Benjaminiella poitrasii and Candida albicans strains; structural analogues of L-glutamate, dimethyl esters of isophthalic acid (DMIP) and its derivatives are designed, synthesized and screened for inhibition of NADP-GDH activity as well as YeH transition in Benjaminiella poitrasii, and also in human pathogenic Candida albicans strains, effect of dimethyl esters of isophthalate (DMIP) derivatives on Benjaminiella poitrasii yeast-hypha transition in vivo, overview. The dimethyl esters of isophthalic acid (DMIP) compounds show a more pronounced effect on H-form specific BpNADPGDH II and inhibit YeH transition as well as growth in Benjaminiella poitrasii and Candida albicans strains
-
additional information
structural analogues of L-glutamate, dimethyl esters of isophthalic acid (DMIP) and its derivatives are designed, synthesized and screened for inhibition of NADP-GDH activity as well as YeH transition in Benjaminiella poitrasii, and also in human pathogenic Candida albicans strains, effect of dimethyl esters of isophthalate (DMIP) derivatives on Benjaminiella poitrasii yeast-hypha transition in vivo, overview. The dimethyl esters of isophthalic acid (DMIP) compounds show a more pronounced effect on H-form specific BpNADPGDH II and inhibit YeH transition as well as growth in Benjaminiella poitrasii and Candida albicans strains; structural analogues of L-glutamate, dimethyl esters of isophthalic acid (DMIP) and its derivatives are designed, synthesized and screened for inhibition of NADP-GDH activity as well as YeH transition in Benjaminiella poitrasii, and also in human pathogenic Candida albicans strains, effect of dimethyl esters of isophthalate (DMIP) derivatives on Benjaminiella poitrasii yeast-hypha transition in vivo, overview. The dimethyl esters of isophthalic acid (DMIP) compounds show a more pronounced effect on H-form specific BpNADPGDH II and inhibit YeH transition as well as growth in Benjaminiella poitrasii and Candida albicans strains
-
additional information
-
structural analogues of L-glutamate, dimethyl esters of isophthalic acid (DMIP) and its derivatives are designed, synthesized and screened for inhibition of NADP-GDH activity as well as YeH transition in Benjaminiella poitrasii, and also in human pathogenic Candida albicans strains, effect of dimethyl esters of isophthalate (DMIP) derivatives on Benjaminiella poitrasii yeast-hypha transition in vivo, overview. The dimethyl esters of isophthalic acid (DMIP) compounds show a more pronounced effect on H-form specific BpNADPGDH II and inhibit YeH transition as well as growth in Benjaminiella poitrasii and Candida albicans strains; structural analogues of L-glutamate, dimethyl esters of isophthalic acid (DMIP) and its derivatives are designed, synthesized and screened for inhibition of NADP-GDH activity as well as YeH transition in Benjaminiella poitrasii, and also in human pathogenic Candida albicans strains, effect of dimethyl esters of isophthalate (DMIP) derivatives on Benjaminiella poitrasii yeast-hypha transition in vivo, overview. The dimethyl esters of isophthalic acid (DMIP) compounds show a more pronounced effect on H-form specific BpNADPGDH II and inhibit YeH transition as well as growth in Benjaminiella poitrasii and Candida albicans strains
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additional information
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2-oxoglutarate and NH3 show substrate inhibition
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additional information
inhibitors hexachlorophene, GW5074, and bithionol are more effective on PfGDH2 than on PfGDH1; inhibitors hexachlorophene, GW5074, and bithionol are more effective on PfGDH2 than on PfGDH1
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additional information
inhibitors hexachlorophene, GW5074, and bithionol are more effective on PfGDH2 than on PfGDH1; inhibitors hexachlorophene, GW5074, and bithionol are more effective on PfGDH2 than on PfGDH1
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additional information
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no effect: EDTA, o-phenanthroline, sodium azide, 8-hydroxyquinoline in the concentration raneg of 1-10 mM
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