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5,5'-dithiobis(2-nitrobenzoate)
ACMX
-
competitive inhibitor versus acetyl-CoA
Ag+
almost complete inhibition at 2 mM
Cations
-
monovalent and divalent
-
dethiaacetyl-CoA
partial substrate
dithiothreitol
2 mM, almost complete loss of activity
EDTA
2 mM, 59% residual activity
elongation factor 1alpha
-
causes polymerization of 49K protein, reduced activity
-
Guanidinium chloride
-
irreversible inactivation of recombinant wild-type at 1.6 M and of recombinant mutant G196V at 0.2 M, at 0.5 M activation of the wild-type
H2O2
about 54% inhibition at 0.4 mM
Hg2+
95% inhibition at 2 mM
MnCl2
-
56% inhibition at 10 mM
N-ethylmaleimide
-
strong
NAD+
-
10 mM, 9% inhibition
p-hydroxymercuribenzoate
-
60% inhibition at 0.1 mM, protection by oxaloacetate
Pb2+
almost complete inhibition at 2 mM
phosphoenolpyruvate
5 mM, 14% residual activity
propionyl-CoA
-
competitive against acetyl-CoA
S-carboxymethyl-CoA
competitive inhibition versus acetyl-CoA, non-competitive inhibition versus oxaloacetate; inhibits the native enzyme competitively versus acetyl-CoA and non-competitively versus oxaloacetate
succinyl-CoA
-
mixed-type inhibition
Urea
-
irreversible inactivation of recombinant wild-type at 9.3 M and of recombinant mutant G196V at 5 M, at up to 8 M activation of the wild-type
2-oxoglutarate
-
30% inhibition at 1 mM
2-oxoglutarate
-
no inhibition
2-oxoglutarate
-
competitive against oxaloacetate
2-oxoglutarate
-
wild-type and mutants
2-oxoglutarate
-
no inhibition
2-oxoglutarate
-
no inhibition
2-oxoglutarate
-
no inhibition
2-oxoglutarate
-
no inhibition
2-oxoglutarate
-
competitive against oxaloacetate; no inhibition
2-oxoglutarate
5 mM, 2% residual activity
5,5'-dithiobis(2-nitrobenzoate)
-
inactivation of the glyoxysomal isozyme, half-life: approx. 1 min, not mitochondrial isozyme
5,5'-dithiobis(2-nitrobenzoate)
-
no inhibition
5,5'-dithiobis(2-nitrobenzoate)
-
inactivation, half-lifes at 0.4 mM: 2.8 min for CS 1, 50 min for CS II
acetyl-CoA
-
no inhibition
acetyl-CoA
-
no inhibition
acetyl-CoA
-
substrate inhibition at high concentration
acetyl-CoA
-
no inhibition
acetyl-CoA
-
no inhibition
ADP
-
-
ADP
5 mM, 64.8% residual activity
ADP
-
25% inhibition at 5 mM
ADP
-
10 mM, 64% inhibition; 64% inhibition at 10 mM
ADP
-
30% inhibition at 1 mM, only CS II
ADP
-
CS II insensitive, CS I inhibited competitively with acetyl-CoA, noncompetitively with oxaloacetate
ADP
14% inhibition at 5 mM
AMP
-
-
AMP
5 mM, 60% residual activity
AMP
-
8% inhibition at 5 mM
AMP
-
10 mM, 36% inhibition; 36% inhibition at 10 mM
AMP
-
CS II insensitive, CS I inhibited competitively with acetyl-CoA, noncompetitively with oxaloacetate
ATP
-
possibly involved in enzyme regulation
ATP
-
50% inhibition at 7.5 mM, acetyl-CoA protects
ATP
10 mM, 83% inhibition
ATP
-
possibly involved in enzyme regulation
ATP
-
possibly involved in enzyme regulation
ATP
-
30% inhibition at 1 mM
ATP
-
competitive against acetyl-CoA
ATP
-
44% inhibition at 5 mM
ATP
-
25% inhibition at 10 mM
ATP
-
competitive against acetyl-CoA; no inhibition
ATP
5 mM, 89% residual activity
ATP
-
50% inhibition at 5 mM, competitive against acetyl-CoA; feed back inhibition
ATP
-
10 mM, 79% inhibition; 79% inhibition at 10 mM
ATP
-
isoenzyme CSII, 30% activity at 1 mM, isoenzyme CSI not inhibited at 1 mM
ATP
-
CS II insensitive, CS I inhibited
ATP
-
competitive against acetyl-CoA
ATP
32% inhibition at 5 mM
ATP
-
competitive against acetyl-CoA
ATP
-
competitive against acetyl-CoA, inhibition reduced by Mg2+
ATP
-
competitive against acetyl-CoA
ATP
-
20%, 40%, and 60% inhibition at 1 mM, 2 mM, and 5 mM ATP, respectively
CaCl2
-
29% inhibition at 10 mM
CaCl2
-
50% inhibition at 10 mM, not reversible by KCl
citrate
-
competitive with acetyl-CoA, noncompetitive with oxaloacetate
citrate
-
competitive with acetyl-CoA, noncompetitive with oxaloacetate
citrate
-
competitive with acetyl-CoA, noncompetitive with oxaloacetate
citrate
-
50% inhibition at 2.5 mM
citrate
product inhibition, competitive. Citrate binds tightly to the substrate binding site and its binding induces a compact closed conformation
citrate
5 mM, 1% residual activity
Co2+
2 mM, 50% residual activity
Co2+
22% inhibition at 2 mM
CoA
-
competitive with acetyl-CoA, noncompetitive with oxaloacetate
CoA
-
competitive with acetyl-CoA, noncompetitive with oxaloacetate
CoA
-
competitive with acetyl-CoA, noncompetitive with oxaloacetate
CoA
-
competitive with acetyl-CoA, noncompetitive with oxaloacetate
CoA
-
50% inhibition at 0.2 mM
Cu2+
2 mM, 12% residual activity
Cu2+
2 mM, almost complete loss of activity
Cu2+
-
87% decrease in activity
Cu2+
10% inhibition at 2 mM
HgCl2
-
-
iodoacetamide
-
10% inhibition at 0.002 mM
KCl
at 0.2 M KCl, approximately 60% of its maximal activity
KCl
-
9% inhibition at 50 mM
KCl
-
CS I inhibited competitively with acetyl-CoA, noncompetitively with oxaloacetate
Mg2+
2 mM, 0.29% residual activity
MgCl2
-
32% inhibition at 10 mM
MgCl2
-
50% inhibition at 7 mM, not reversible by KCl
Mn2+
2 mM, 72% residual activity
Mn2+
40% inhibition at 2 mM
Mn2+
100 mM, 48% residual activity
NaCl
-
15% inhibition at 50 mM
NADH
-
12% inhibition at 1 mM
NADH
-
not, only gram-negative facultative methylotrophs
NADH
-
70% inhibition at 2 mM, completely reversed by 0.17 mM 5'-AMP
NADH
-
reactivation by AMP
NADH
-
reactivation by AMP
NADH
allosteric; CS II, strong and specific allosteric inhibition
NADH
-
inhibition of wild-type enzyme. Inhibition is extremenly weak in mutant enzymes Y145A, R163L, and K167A
NADH
about 95% inhibition at 0.1 mM
NADH
-
0.1 M, 92% inhibition of wild-type, 25% inhibition of K283 acetylated variant, 88% inhibition of K295 acetylated variant, 7% inhibition of K168 acetylated variant
NADH
-
not, only gram-negative facultative methylotrophs
NADH
-
complete inhibition at 1 mM, completely reversible by NAD+
NADH
-
not, only gram-negative facultative methylotrophs
NADH
5 mM, 45% residual activity
NADH
-
10 mM, 31% inhibition; 1-10 mM; non-specific, 31% inhibition at 10 mM
NADH
-
78% inhibition by 0.1 mM of CS I, 15% inhibition of CS II at 1 mM; isoenzyme CSI 78% at 0.1 mM, allosteric, isoenzyme CSII 15% activity at 1 mM
NADH
-
inhibits large isoenzyme, reactivation by AMP
NADH
-
inhibits large isoenzyme, reactivation by AMP
NADH
-
inhibits the large form of the isoenzym, reactivation by AMP
NADH
-
CS II inhibited, CS II insensitive; weak inhibition, reversible by AMP, hinders the activation by AMP, CS II
NADH
-
inhibits large isoenzyme, reactivation by AMP
NADH
-
competitive against acetyl-CoA
NADH
-
51% inhibition of peroxisomal isozyme, 12% inhibition of mitochondrial isozyme at 5 mM
NADH
-
competitive against acetyl-CoA
NADH
-
competitive against acetyl-CoA
NADH
-
inhibition only with gram-negative bacterial enzymes; no effect
NADP+
-
no inhibition
NADP+
-
10 mM, 32% inhibition
NADP+
-
only CS II slightly
NADPH
-
29% inhibition at 0.25 mM
NADPH
-
10 mM, 57% inhibition; 57% inhibition at 10 mM
NADPH
-
40% inhibition by 5 mM, both isoenzymes
NADPH
-
competitive against acetyl-CoA
NADPH
-
competitive against acetyl-CoA
Ni2+
2 mM, 71% residual activity
Ni2+
2 mM, 74% residual activity
Ni2+
21% inhibition at 2 mM
oxaloacetate
-
no inhibition
oxaloacetate
-
no inhibition
oxaloacetate
-
substrate inhibition
oxaloacetate
-
no inhibition
oxaloacetate
-
no inhibition
p-chloromercuribenzoate
-
can be restored by dithiothreitol treatment
p-chloromercuribenzoate
-
6% loss at 0.002 mM
p-chloromercuribenzoate
-
strong
Zn2+
2 mM, 27% residual activity
Zn2+
2 mM, 16.8% residual activity
Zn2+
55% inhibition at 2 mM
additional information
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the activity is not affected by O2, pCMB (0.05 mM), or EDTA (0.05 mM)
-
additional information
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not inhibitory: NADH, AMP
-
additional information
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tricarboxylic acid cycle intermediates
-
additional information
allosteric inhibition mechanism, structure relationship
-
additional information
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allosteric inhibition mechanism, structure relationship
-
additional information
no inhibition by NADH or 2-oxaloacetate
-
additional information
-
low salt concentrations inactivate reversibly
-
additional information
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isocitrate, (R)-3-hydroxybutyrate, malonate, pyruvate, acetoacetyl, NaCl, NH4Cl, CsCl, and RbCl have no effect
-
additional information
-
not affected by EDTA
-
additional information
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NADH and AMP not inhibitory for small isoenzyme
-
additional information
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NADH and AMP not inhibitory for small isoenzyme
-
additional information
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NADH and AMP not inhibitory for small isoenzyme
-
additional information
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NADH and AMP not inhibitory for small isoenzyme
-
additional information
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NADH and AMP not inhibitory for small isoenzyme
-
additional information
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NADH and AMP not inhibitory for the small isoenzyme
-
additional information
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NADH and AMP not inhibitory for small isoenzyme
-
additional information
-
limited proteolysis of citrate synthase from Sulfolobus solfataricus by trypsin reduces the rate of the overall reaction (acetyl-CoA + oxaloacetate + H2O -> citrate + CoASH) to 4% but does not affect the hydrolysis of citryl-CoA. A connecting link between the enzyme's ligase and hydrolase activity becomes impaired specifically on treatment with trypsin. Other proteolytic enzymes like chymotrypsin and subtilisin inactivate catalytic functions of citrate synthase, ligase and hydrolase, equally well
-
additional information
limited proteolysis of citrate synthase from Sulfolobus solfataricus by trypsin reduces the rate of the overall reaction (acetyl-CoA + oxaloacetate + H2O -> citrate + CoASH) to 4% but does not affect the hydrolysis of citryl-CoA. A connecting link between the enzyme's ligase and hydrolase activity becomes impaired specifically on treatment with trypsin. Other proteolytic enzymes like chymotrypsin and subtilisin inactivate catalytic functions of citrate synthase, ligase and hydrolase, equally well
-
additional information
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no inhibition by NAD+
-
additional information
not inhibited by EDTA
-
additional information
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NADH and AMP are not inhibitory for isoenzyme small
-
additional information
not influenced by NADH
-
additional information
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inhibited by a specific antibody against 49K protein
-