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1 mM, complete inhibition
-
0.1 mM, complete inhibition
-
94% inhibition at 10 mM
-
0.1 mM, 85% inhibition after 15 min, 200 mM 2-mercaptoethanol restores 70% of enzyme activity within 10 min, 20 mM D-pantoate and 1 mM NAD+ prevent inactivation when added simultaneously
-
0.1 mM, complete inhibition
-
complete inhibition at 1 mM, partial reversible by low concentration of cysteine
-
strong inhibition at 0.1 mM
-
50% inhibition at 0.02 mM
-
32% inhibition at 1 mM, not reversal by GSH
-
0.027 mM, complete inhibition
-
0.2 mM, complete inhibition
-
complete inhibition at 1 mM
-
complete inhibition of cortisol oxidation at 0.01 mM
-
complete inhibition of oxidation of cortisol at 0.01 mM
-
also other sufhydryl reagents like 5,5'-dithiobis-2-nitrobenzoic acid and iodoacetamide strong
-
93% inhibition of the reductive reaction at 0.01 mM
-
1 mM, complete inhibition
-
80% remaining activity at concentration 0.3 mM
-
complete inhibition at 2 mM
-
sulfhydryl reagents, slightly inhibitory
-
slight inhibition at 0.02 mM, combined with 0.26 mM SDS
-
complete inhibition at 0.05 mM
-
complete inhibition at 1 mM concentration
-
no exact differentiation between organisms in the reference
-
17% inhibition at 0.1 mM
-
1 mM, complete inactivation
-
complete inhibition at 1.0 mM
-
complete inhibition at 0.001 mM
-
60% inhibition at 1 mM, reversal by an excess of L-cysteine
-
inhibition can be restored by addition of DTT
-
100% inhibition at 0.021 mM
-
strong inhibition at 0.1 and 1.0 mM
-
non-competitive with respect to dihydrocortisone 46-100% inhibition at 0.01 mM, preincubation with NADH lowers the inhibitory effect
-
complete inhibition at 1 mM
-
0.001 mM, 66% inhibition
-
75% inhibition with two equivalents per subunit
-
0.02 mM, 50% inhibition
-
0.1 mM, complete inhibition
-
biphasic inhibition: first rapid inhibition leading to loss of 70% activity, then within 5 min loss of the remaining 30% activity, inhibition can be partially hindered by thiols and chloride
-
D-carnitine dehydrogenase, 0.1 mM, complete inactivation
-
; D-carnitine dehydrogenase, 0.01 mM, complete inhibition
-
79% inhibition at 0.1 mM, partially reversed by 0.1 mM 2-mercaptoethanol
-
strong inhibition at 0.01 mM
-
activation of enzyme MGR I, inhibition of enzyme MGR II
-
1 mM, complete inhibition
-
0.19 mM, 43% residual activity
-
0.1 mM, 100% inhibition
-
0.001 mM, extremely rapid inhibition, NAD+ and NADH protect against inhibition
-
enzyme extremely sensitive, NADH and Ca2+ protect
-
0.001 mM, 2 min, complete inhibition
-
1 h at 0.01 mM inhibits 78% of enzyme activity
-
complete inhibition at 1 mM and above
-
1 mM, complete inhibition
-
0.0025 mM, 80% inhibition within 2 min
-
0.005 mM, 75% loss of activity after 1 h
-
0.1 mM, complete inhibition
-
can be reversed 100% by dithiothreitol, partially by glutathione
-
can be overcome by addition of gluthathione
-
complete inhibition at 0.03 mM
-
complete inhibition at 0.005 mM, non-competive, Ki: 0.0001 mM
-
slight inhibition, no inhibition below 10 mM
-
non-competitive, Ki: 1 mM
-
95% inhibition at 0.01 mM
-
10 mM leads to 50% inhibition
-
0.1 mM, complete loss of activity
-
1 mM, complete inhibition
-
10 mM, strong inhibition, 5% residual activity is reversed to 65% activity by either 1 mM glutathione or cysteine
-
0.1 mM, 100% inhibition
-
0.1 mM, complete inhibition
-
0.01 mM, complete inhibition
-
0.01 mM, complete inhibition; some protection of partial inhibition resulting from 0.001 mM 4-chloromercuribenzoate in the presence of 1 mM NADP+, almost complete protection with 10 mM hexan-1-ol
-
0.1 mM, 55% inhibition after preincubation for 5 min
-
isoenzyme 2, 1 mM, complete inhibition, 0.1 mM, 88% inhibition, 29% inhibition in the presence of 1 mM dithiothreitol, 21% inhibition in the presence of 1 mM L-cysteine, isoenzyme 1, 1 mM, 59% inhibition
-
10 nM, strong inhibition; reversible by dithiothreitol, 0.001 mM inhibits more than 90% of the enzyme activity
-
0.0001 mM inhibits enzyme over 60%
-
0.05 mM, 100% inhibition
-
10 nM, strong inhibition
-
0.1 mM, reversed by thiols, e.g. dithiothreitol
-
0.1 mM, complete inhibition
-
0.2 mM, 10% inactivation
-
0.5 mM, 45% inactivation
-
1 mM, 4% residual activity
-
completely inhibits at 1 mM
-
o-chloromercuribenzoate, m-chloromercuribenzoate, and p-chloromercuribenzoate inhibit in absence but not in presence of cyanide
-
complete inhibition at molar excess of reagents in relation to alcohol oxidase 20:1
-
1 mM, complete inhibition
-
t1/2: 11 min, beta-mercaptoacetic acid restores activity, substrates or products slow the inactivation rate
-
5 mM, complete loss of activity
-
strong inhibition at 0.01 mM
-
long chain oxidase, 29-42% inhibition at 0.001 mM, short chain oxidase: 70-75% inhibition at 0.001 mM
-
70% loss of activity at 0.1 mM, completely reversible with dithiothreitol
-
85% inhibition at 0.1 mM
-
1 mM, 20% inhibition, 0.1 mM, 14% inhibition
-
0.01 mM, complete inhibition
-
the addition of p-chloromercuribenzoic acid partially reduces the activity of the enzyme
-
22% inhibition at 0.1 mM
-
no protection by substrate
-
no inhibition with 2-mercaptoethanol
-
10-20% inhibition at 0.01 mM
-
1 mM, 62% loss of activity
-
100% inhibition at 0.25 mM
-
1 mM, 96, 94 and 95% inhibition of isoenzymes Ia, Ib and II respectively
-
60% inhibition at 0.5 mM, inhibition reversed by glutathione
-
20% inhibition at 0.33 mM
-
95% inhibition at 0.05 mM
-
87% inhibition at 0.005 mM, inactivation is partially reversible, 2-mercaptoethanol protects
-
82% inhibition at 0.2 mM for 5 min
-
84% inhibition at 0.2 mM for 5 min
-
30% inhibition of isoform Gpx-1 at 0.3 mM
-
complete inhibition at 0.33 mM, summation effect with 2-mercaptoethanol
-
0.02 mM, complete inhibition, reversed by addition of glutathione
-
0.15 mM, complete inhibition
-
0.17 mM, 35% inhibition
-
inhibition can almost completely be reversed by addition of glutathione
-
pyrocatechase I: in absence of 2-mercaptoethanol, pyrocatechase II: with 2-mercaptoethanol, 20 hours incubation time
-
64% inactivation, 5 mM, 30 min, 24°C
-
1.0 mM, enzyme from aniline-grown cells loses 20% of its activity, enzyme from L-malate-grown cells loses 10% of its activity
-
0.5 mM, complete inhibition
-
0.5 mM, 30% inhibition, Cu2+ can completely reverse inhibition
-
0.0005 mM, 98.5% inhibition
-
preincubation with substrate protects against inactivation
-
80% inhibition at 0.1 mM
-
0.05 mM, 47% inhibition
-
70% inhibition at 0.1 mM
-
inhibits by competing with Fe2+ for a common enzymic binding site
-
competitive inhibition with respect to Fe2+ but not to homogentisate
-
inhibition reversed by glutathione
-
reversed by glutathione
-
65% residual activity at 0.5 mM
-
excellent competitive inhibitor
-
1 mM, 44% loss of activity
-
increases oxidase and dehydrogenase activities, decreases oxygenase activity
-
conversion of oxygenase to oxidase; increases oxidase and dehydrogenase activities, decreases oxygenase activity
-
conversion of oxygenase to oxidase
-
0.025 mM, complete inhibition
-
100% inhibition at 1.1 mM at pH 8 and 25°C after 30 min, excess of 2-mercaptoethanol protects
-
inactivates enzyme completely at 0.1 mM
-
0.0005 mM, 94% inhibition of ferredoxinNAP reductase
-
17% inhibition at 0.005 mM
-
0.005 mM, complete inhibition
-
50% inhibition at 0.01 mM
-
1 mM, complete inhibition
-
preincubation of the enzyme for 15 min at 14°C, pH 7.7, in the presence of 0.2 mM p-chloromercuribenzoate inhibits the enzymic activity approximately by 90%
-
a mixed inhibitor with respect to ornithine
-
0.015 mM, more than 70% inhibition, partially restored by addition of 0.14 M 2-mercaptoethanol
-
; 0.05 mM, quick and complete inhibition
-
94% inactivation at 0.1 mM
-
complete inhibition at 0.1 mM
-
maximum inactivation at a ratio about 2 mol of p-chloromercuribenzoate per mol of enzyme
-
0.01 mM, 62% inhibition, reversed by dithiothreitol
-
inhibition is reversed by dithiothreitol
-
complete inhibition at 0.4 mM
-
weak, 50% inhibition at 0.4 M
-
5 mM inhibits activity by 58%
-
complete inhibition at 1 mM, but not inhibitory at 0.1 mM
-
inhibition of NADPH-cytochrome c reductase in reconstituted heme oxygenase system
-
at 1 mM complete inhibition
-
complete inhibition at 0.5 mM
-
0.1 mM, 17% residual activity
-
32% inhibition at 0.5 mM
-
complete inhibition at 1 mM
-
complete inhibition at 0.08 mM
-
0.1 mM concentration, 51% inhibition
-
1 mM, complete inhibition after 10 min
-
strong, complete inhibition at 0.02 mM
-
a sulfonate, reversed by beta-mercaptoethanol
-
prevention by stearoyl-CoA; reversed by beta-mercaptoethanol
-
28% residual activity at 2 mM
-
0.1 mM, 22% loss of activity
-
inhibition reversed by addition of GSH or cysteine
-
26.6% inhibition at 1 mM
-
decreases NAD+-dependent activity from 0.01 up to 0.05 mM with simultaneous inactivation of the enzyme
-
89.2% inhibition of hypoxanthine oxidation at 1 mM
-
1 mM, 10 min at 35°C, complete loss of activity
-
0.2 mM, 10.7% inhibition
-
0.2 mM, complete inhibition
-
complete inhibition of enzyme 1 and enzyme 2
-
0.35 mM, 50% inhibition of intact enzyme, 0.15 mM, 50% inhibition of effector-binding subunit, 1.5 mM, 50% inhibition of non-heme iron subunit
-
0.0005 mM, 94% inhibition
-
94% inhibition at 0.0005 mM
-
0.01 mM causes 88-96% inhibition
-
0.005 mM, 75% loss of activity after 1 h
-
5 mM, complete inhibition
-
1 mM, complete inhibition, partially reversed by dithiothreitol; 1 mM, inhibition is partially reversed by dithiothreitol
-
0.33 mM, complete inhibition
-
0.005 mM, 50% inhibition after 270 min, benzaldehyde dehydrogenase II
-
0.10 mM, 50% inhibition after less than 1 min, benzaldehyde dehydrogenase I
-
0.5 mM, complete inhibition
-
inhibition of the reduction of benzoyladenosine 5'-monophosphate, even in the presence of dithiothreitol
-
equimolar amount inactivates benzaldehyde oxidation completely, 5 mM 2-mercaptoethanol restores activity
-
100% inhibition at 20 mM, 52% inhibition at 0.01 mM, 1 mM cysteine reverses inhibition completely
-
41% remaining activity at an inhibitor concentration of 1 mM; 59% inhibtion at 1 mM
-
completely inhibits in the presence of 1 mM
-
enzyme a, b, c, d and e
-
100% inhibition at 1 mM
-
0.01 mM, 50% inhibition
-
0.1 mM causes 88% inhibition at 30°C
-
0.01 mM causes complete inhibition
-
1 mM causes complete inhibition
-
0.1 mM causes complete inhibition
-
50 microM, 80% inhibition
-
1 mM, complete inhibition
-
41% residual activity at 1 mM
-
0.1 mM, 21% residual activity
-
96% inhibition at 0.1 mM
-
61% inhibition at 0.05 mM
-
95% inhibition of sulfoxide reductase and aldehyde oxidase activity at 0.1 mM
-
0.1 mM concentration 100% inhibition
-
0.026 mM, complete inactivation after 80 s
-
8 mol per mol enzyme, complete inhibition
-
3.0 mM, 100% inhibition, 0.33 mM, 37% inhibition
-
0.002 mM, 65% inhibition
-
completely inhibited by 0.1 mM
-
complete inhibition of both orotate reductase and NADH oxidase reaction
-
0.01 mM, 90% inhibition, 0.001 mM, 30% inhibition
-
stronger effect on isoform F1
-
pretreatment of the enzyme with NADPH and biliverdins fully protects
-
16.7 mM, 87% inhibition
-
0.0035 mM, competitive, 85% inhibition
-
0.1 mM, complete inhibition
-
0.0001 mM, 85% inhibition
-
tested at 0.1 mM, 100% inhibition
-
enzyme preincubated with the inhibitor, 0.00166 mM, for 60 min at room temperature before the addition of the substrate, 48% inhibition
-
a 30-min incubation of crotonyl-CoA reductase with p-chloromercuribenzoate at 0.008 mM leads to approximately 8.5% inhibition of enzyme activity
-
87% inhibition at 0.1 mM
-
complete inhibition at 0.1 mM, inhibition can be prevented by preincubation with crotonyl-CoA
-
reduced by addition of 2-mercapthoethanol
-
complete inhibition at 1 mM
-
inhibition is reversible by glutathione
-
at 0.1 mM 18% activity remains
-
inhibition of apo-enzyme
-
inhibition of enzyme-catalyzed C-2 proton-deuteron exchange reactions
-
completely inhibits at 1 mM, 2-mercaptoethanol protects against inhibition
-
inhibits the glutamine-dependent reaction
-
complete inhibition at 0.1 mM
-
complete inhibition at 0.1 mM
-
0.001 mM, complete inhibition
-
complete inhibition at 0.01 mM after 10 min incubation, reversible with 2-mercaptoethanol or dithiothreitol
-
0.02 mM, complete inhibition
-
0.001 mM, complete inhibition
-
1.0 mM, 98% loss of activity
-
0.1 mM, strong inhibition
-
0.01 mM, 83% loss of activity
-
0.001 mM, 95% inhibition
-
progressive decrease in enzyme activity of both isoenzymes, inhibition is not affected by addition of GTP or ADP
-
at 1 mM, 86% inhibition
-
at 0.01 mM, 35% inhibition
-
at 1 mM and 10 mM, 30% inhibition and 100% inhibition
-
completely inhibited at 0.005 mM
-
strong inhibition, partially abolished in presence of 2-mercaptoethanol
-
0.01 mM in assay buffer
-
0.5 mM, complete inhibition
-
1 mM, 16% loss of activity
-
91% inhibition at 0.0005 mM, partially reversed by glutathione
-
moderate inhibition (61.2% residual activity at 1 mM)
-
0.1 mM, 90-95% inhibition
-
95% inhibition at 0.1 mM
-
74% inhibition at 0.01 mM
-
0.1 mM, complete inhibition
-
90% inhibition of the methylene blue specific, 70% inhibition of the dichlorophenolindophenol specific enzyme at 0.5 mM
-
complete inactivation at 1 mM
-
complete inhibition at 0.125 mM, can be prevented by addition of dithiothreitol
-
60% inhibition of the methylenetetrahydrofolate reductase activity at 0.04 mM, 83% inhibition of the menadione reductase activity at 0.04 mM
-
almost total inhibition at 0.1 mM
-
with 1 mM 15.6% activity
-
0.2 mM, 50% inhibition, enzyme from brain
-
complete inactivation at inhibitor/enzyme ratios greater than 6/1, NADH protects
-
0.01 mM, 70% inhibition
-
inhibition reversible by dimercaptopropanol
-
inhibition reversed by 2-mercaptoethanol
-
0.01 mM, 0% relative activity
-
100% inhibition at 1 mM
-
complete inhibition of ubiquinone reductase activity, 70% inhibition of disproportion activity
-
2 mM, 59% loss of activity
-
2 mM, 100% loss of activity
-
0.044 mM, 40-50% inhibition after 30 min, activity can be restored by adding 2-mercaptoethanol
-
0.003 mM, 25% inhibition
-
0.005 mM, complete inhibition
-
0.001 mM, complete inhibition
-
complete inhibition at 0.4 mM
-
cells grown on alkane or glycerol, presence of NADPH provides protection against inhibition
-
incubation with NADPH provides protection against inhibition
-
0.05 mM, complete inhibition
-
0.05 mM, complete inhibition
-
74% residual activity at 0.15 mM
-
PpMDHAR1 is almost completely inactivated after a 20 min preincubation with 0.25 mM beta-chloromercuribenzoate. At 0.05 mM the enzyme retains 11% of the initial activity.
-
at 0.05 mM PpMDHAR3 retains 80% of the initial activity; PpMDHAR2 is almost completely inactivated after a 20 min preincubation with 0.25 mM chloromercuribenzoate. At 0.05 mM the enzyme retains 14% of the initial activity. The C69A mutant is more resistant to the inhibitory effects of chloromercuribenzoate than the wild type PpMDHAR2 protein
-
0.1 mM, complete inhibition
-
0.05 mM, 82% inhibition
-
both NADPH and NADP1 suppress the inhibition, but NADH does not
-
0.1 mM, complete inhibition
-
complete inhibition at 0.001 mM
-
0.005 mM, 50% inhibition
-
0.01 mM, complete inhibition
-
inactivation is concentration independent
-
0.1 mM, 67% inhibition of hydroxylamine reductase activity
-
1 mM, complete inhibition
-
0.05 mM, complete inhibition, subsequent addition of 3 mM cysteine restores the activity
-
0.1 mM, complete inhibition
-
the reduction of cytochrome c, K3Fe(CN)6 and hydroxylamine is completely inhibited (more than 99%) by 0.02 mM p-chloromercuribenzoate
-
inhibition of diaphorase activity; NADH or NADPH protect
-
reversion of the inhibition by addition of reduced glutathione
-
reversed by cysteine or glutathione
-
0.02 mM, complete inactivation, partially prevented by 10 mM cysteine
-
0.001 mM, 83% inhibition
-
completely reversed by glutathione
-
1 mM, 79% inhibition after 5 min, dithiothreitol completely reverses activity, reduced glutathione, L-cysteine and 2-mercaptoethanol reverse activity to 86%, 64% and 82% respectively
-
2% inhibition of inducible enzyme and 50-60% inhibition of constitutive enzyme at 5 mM
-
nitrite partially protects the inhibition
-
complete inhibition at 0.1 mM
-
47% inhibition at 0.5 mM
-
NADPH-dependent activities
-
complete inhibition at 1 mM
-
chloroplast enzyme, 96% inhibition at 1 mM
-
0.054 mM, 88% inhibition
-
1 mM, complete inhibition
-
1 mM, 47% loss of activity
-
47% inhibition at 1 mM, 7% inhibition at 0.1 mM
-
72.8% inhibition at 1 mM
-
32% inhibition at 0.1 mM
-
0.02 mM, 100% inhibition. Inhibition can be partially or completely reversed by cysteine
-
complete inhibition at 1 mM
-
0.05 mM, reversed by thiol reagents
-
1 mM, 32% loss of activity
-
1 mM, 23% loss of the activity with ferricyanide, complete loss of activity with cytochrome c
-
1 mM, complete inhibition
-
0.3 mM, completely inhibits, can be reversed by cysteine or glutathione
-
recombinant enzyme: over 95% inhibition at 1.33 mM, completely reversible by 5.3 mM DTT
-
recombinant enzyme: 23% inhibition at 1.33 mM, completely reversible by 5.3 mM DTT
-
complete inhibition at 0.5 mM, 30% inhibition at 0.05 mM
-
complete inhibition at 0.5 mM, 23% inhibition at 0.05 mM
-
0.5 mM, 30% inhibition, production of methyl iodide
-
1 mM, about 90% inhibition
-
complete inhibition at 1 mM, reversible by addition of glutathione
-
0.01 mM, 85% inhibition
-
0.01 mM, complete inhibition
-
at 2.5 mM, complete inhibition, completely reversed by addition of 5 mM dithiothreitol
-
at 2 mM, complete inhibition
-
5 mM, complete inhibition
-
strong, reversible by cysteine
-
complete inhibition at 1 mM
-
1 mM, complete inhibition
-
90% inhibition at 0.01 mM
-
0.4 mM, 40% inhibition, can be reversed by 12 mM 2-mercaptoethanol
-
more than 50% inhibition at 0.1 mM
-
6 mM, almost complete inhibition
-
0.1 mM, complete inhibition, activity can be restored by incubation with 2 mM dithiothreitol for 30 min at 0°C
-
1 mM, 90% inhibition after 40 min, 20% activity can be recovered by adding 20fold excess of dithiothreitol, benzoyl-CoA protects
-
0.005 mM, complete inhibition of retinol-(cellular-retinol-binding-protein)type II esterification
-
10 mM, 88% inhibition in sonicated vesicles, 1 mM, 98% inhibition in vesicles treated with 0.3% toluene, 2-mercaptoethanol partially restores activity, not inhibited by p-chloromercuriphenylsulfonic acid
-
90% inhibition at 0.1 mM, complete inhibition at 1 mM
-
1 mM, complete inhibition
-
complete inhibition, DTT protects
-
partially restorable by dithiothreitol
-
complete inhibition at 1 mM
-
0.1 mM, complete inhibition
-
strong inhibitor at 1 mM
-
pyridoxal 5'-phosphate protects
-
2-mercaptoethanol protect partly
-
0.001 mM, 50% inhibition, 0.01 mM, complete inhibition, reversed by cysteine
-
1 mM, complete inhibition
-
complete inhibition at 1 mM
-
100% inhibition at 1 mM
-
strongly inhibits activity of enzyme form B, formation of acyl-enzyme complex
-
enzyme form B less sensitive than enzyme form A
-
50% inhibition at 2.5 mM
-
activity abolished at 5 mM
-
binding site is not the active site
-
complete inhibition of type II fatty acid synthase at 1 mM
-
35.2% residual activity after 1 h at 1 mM
-
reversible by glutathione
-
21% inhibition of chondrosarcoma transglutaminase B
-
10 mM, complete inhibition
-
reversible by GSH, 2-mercaptoethanol or 2,3-dimercaptopropanol, not L-cysteine
-
0.1 mM. 100% inhibition
-
can be restored by dithiothreitol treatment
-
0.1 mM, 100% inhibition
-
0.1 mM, 2% residual activity
-
0.1 mM, 2% residual activity
-
0.04 mM, 73% inhibition
-
0.04 mM, 27% inhibition
-
1 mM and 5 mM, 35 and 42% inhibition in extracts of Barker strain, respectively
-
0.05 mM, 9% residual activity
-
0.5 mM, 60% inhibition, reversible by 10 mM 2-mercaptoethanol
-
90% inactivation at 0.01 mM, dithiothreitol reverses
-
0.1 mM, complete inhibition
-
1.25 mM, 93% inhhibition, 2-mercaptoethanol or cysteine restores activity
-
3 mM, 25% inhibition, 2-mercpatoethanol or cysteine does not protect
-
100% inhibition at 1 mM, activity can be restored up to 50% by addition of 10 mM dithiothreitol, 24% inhibition at 0.1 mM, activity can be completely restored by 10 mM dithiothreitol
-
0.001-0.01 mM: 50-70% inhibition
-
activity can be restored by addition of DTT or 2-mercaptoethanol
-
50% inhibition at 0.60 mM
-
potent inhibitory effect at 0.1 mM indicating that free SH groups are essential for activity
-
strong and irreversible inhibition by thiol directed reagents like 4-chloromercuribenzoate, N-methylmaleimide and iodoacetamide suggest the requirement of free-SH groups for the catalytic activity
-
47% inhibition at 1 mM, 10 mM dithiothreitol protects
-
0.01 mM, 94% inhibition
-
complete inhibition at 0.02 mM
-
0.002 mM, 50% inhibition, 0.01 mM, 90% inhibition
-
7 mM, complete inhibition
-
at 0.05 mM: almost 30% of the original enzyme activity remains
-
1 mM, 100% inhibition, 14 mM 2-mercaptoethanol completely restores activity
-
1 mM, 97% inhibition, 14 mM 2-mercaptoethanol partially restores activity
-
1 mM, 91% inhibition, 14 mM 2-mercaptoethanol restores activity
-
0.1 mM, 2.5% residual activity
-
10 mM, completely inhibited
-
D-enzyme, 30% inhibition
-
0.1 mM, complete inhibition
-
1 mM, 4% residual activity
-
complete inhibition at 1 mM
-
membrane-bound enzyme, 6 and 10 mM: 54% inhibition
-
5 mM, complete inhibition, inhibition can be very significantly prevented by GDP-fucose, GDP or GnGnGp
-
5-10 mM, more than 90% inhibition
-
over 90% inhibition at 2 mM
-
0.12 mM, 22% inhibition
-
0.03 mM, 63% inhibition
-
adenosine-specific phosphorylase
-
no inhibition of PUNPII
-
0.1 mM, 85% loss of activity within 15 min
-
dithiothreitol restores activity
-
0.01 mM, complete inhibition
-
0.2 mM, complete inhibition
-
0.05 mM, complete inhibition
-
at 1 mM inhibits the reaction completely
-
strong, partially reversed by dithiothreitol
-
reversed by 2-mercaptoethanol and excess Mg2+
-
complete inhibition at 1 mM, DTT or glutathione protect
-
reversed by dithiothreitol or 2-mercaptoethanol
-
0.036 mM, 50% inhibition, 0.1 mM, 97% inhibition
-
0.15 mM, 882% inhibition of wild-type farnesyl diphosphate synthase, 11% inhibition of C73S/C289S mutant enzyme
-
50% of inhibition at 0.2 mM and inhibits reactivation by pyridine
-
complete inhibition at 0.001 mM
-
50 mM, strong inhibition
-
in the absence of sulfhydryl compounds
-
1 mM, 90% inhibition, 30% inhibition in the presence of 800 mM KCl
-
0.01 mM, 98.5% inhibition, inhibition prevented by addition of 2-mercaptoethanol in 10fold molar excess
-
95% inhibition at 0.01 mM
-
14% and 4% inhibition at 1 mM, isoenzymes 1 and 2, respectively
-
1 mM, 97% loss of activity
-
0.001 mM, about 90% inhibition
-
complete inhibition at 0.02 mM, reversible by cysteine
-
1 mM, complete inhibition
-
alpha and beta isoenzymes completely inhibited, gamma isoenzyme slightly inhibited
-
reduces MAT I/III activity
-
0.002 mM, 74% inhibition
-
0.025 mM, 62% inhibition
-
results in a rapid loss of the component B activity. Component A is resistant, retaining the initial activity almost completely. Farnesyl diphosphate, isopentenyl diphosphate, farnesyl monophosphate and inorganic diphosphate protect the synthase against the inactivation by N-ethylmaleimide, farnesyl diphosphate being the most effective. The presence of Mg2+ is essential for the protection by isopentenyl diphosphate and inorganic diphosphate. For protection of the synthase activity against the inactivation by 2,3-butanedione, the presence of farnesyl diphosphate, isopentenyl diphosphate and Mg2+ is more effective than that of the individual substrates and Mg2+. Inorganic diphosphate provides substantial protection. In the absence of component A, the component B activity is not protected by any substrates or its analogue
-
complete inhibition at 0.15 mM
-
cytosolic isozyme, 50% inhibition after 10 min at 30°C, 1 mM
-
84% inhibition at 0.1 mM
-
reactivation by dithiothreitol
-
4 mM, 36% inhibition, D-alanine and pyridoxal 5'-phosphate protect to some extent
-
77% inhibition at 0.5 mM
-
reduced by preincubation with L-phenylalanine and pyridoxal phosphate and reversed by a subsequent preincubation with 2-mercaptoethanol
-
0.1 mM, complete inhibition
-
isoenzyme I, complete inhibition, isoenzyme III only partially inhibited
-
5 mM, complete inhibition
-
0.25 mM: 48% inhibition, reactivation by addition of 2-mercaptoethanol
-
1.0 mM, complete inhibition
-
100% inhibition at 1 mM
-
irreversible and complete inhibition is observed at concentrations about 0.1 mM
-
5% activity retained at 1 mM, 1% activity retained at 10 mM
-
0.05 mM, 72% inhibition
-
0.01 mM, 79% inhibition, NAD+ and ATP protect from inactivation
-
0.02 mM, 35% inhibition
-
0.25 mM, 67% inhibition
-
0.5 mM, 74% inhibition of isoenzyme 1, 23% inhibition of isoenzyme 2
-
0.005 mM, 50% inhibition
-
0.1 mM, 83% inhibition, completely reversed by reduced glutathione
-
activity can be almost completely restored by incubation with an excess of cysteine
-
1 mM, almost complete inhibition
-
0.1 mM, 95% inhibition, 1 mM, complete inhibition
-
0.17 mM, 67% inhibition, 0.69 mM, 82% inhibition, glutathione protects
-
0.01 mM, 98.5% inhibition, inhibition prevented by addition of 2-mercaptoethanol
-
strong, addition of GSH reduces inhibition to 13%
-
complete inhibition at 0.4 mM; reversible with cysteine or 2-mercaptoethanol
-
reversible with cysteine or 2-mercaptoethanol
-
0.005 mM, complete inactivation
-
0.1 mM, complete inhibition, activity is completely restored by 1 mM dithiothreitol
-
1.0 mM, complete inhibition
-
2-mercaptoethanol protects from inactivation
-
0.1 mM, complete loss of activity
-
5 mM, complete inhibition
-
0.01 mM, 74% inhibition
-
0.1 mM, complete inhibition
-
thiol reagents protect or reverse
-
0.0007 mM, 50% inhibition of ribavirin and deoxadenosine kinase activity
-
reversible by 2-mercaptoethanol
-
0.01 mM, 42% residual activity
-
0.5 mM, 3% residual activity
-
0.125 mM, complete inhibition. Preincubation with 0.25 mM dithiothreitol for 5 min partially protects
-
0.83 mM, 95% inhibition
-
0.1 mM, 69% loss of activity
-
0.5 mM, 79.5% inhibition
-
10 mM, complete inhibition
-
2-mercaptoethanol reverses
-
pI 7.3-isoform, DTT restores, but not in the presence of urea, ATP or dTDP protects
-
bovine liver mitochondrial and human erythrocytic enzymes: substrates protect
-
1,4-dithiothreitol reverses
-
dithiothreitol prevents inhibition
-
0.1 mM, complete inhibition, completely restored by 10 mM dithiothreitol
-
1 mM, 55.1% inhibition, activity is recovered to approximately 90% on incubation with a 10fold excess of dithiothreitol
-
42% inhibition at 0.2 mM
-
80% inhibition at 0.0006 mM
-
completely reversible with cysteine
-
ADP/phosphate-exchange, reversible by cysteine
-
ADP/phosphate-exchange and ADPribose phosphorolysis
-
5 mM, inhibits reaction with diphosphate and adenylylsulfate
-
0.03 mM, 90% inhibition
-
inhibition is reversed by incubation with an excess amount of dithiothreitol and 2-mercaptoethanol. PCMB-inhibited enzyme is unable to synthesize RNA, but still maintains template-binding ability
-
very potent inhibitor, partially reversible by thiol-containing reagents
-
protected to the extent of about 50% when all of the substrates, UDP-GlcNAc, dolichyl phosphate anf Mn2+ are added before addition of the sulfhydryl reagent
-
the enzyme from tunicamycin-resistant cells is equally sensitive to tunicamycin as the wilde-type enzyme
-
at pH 9.5, not at pH 8.0
-
preincubation dramatically inhibits enzyme activity
-
50% inhibition at 0.000025 mM
-
91% inhibition at 1 mM, causes precipitation
-
modifies selectively cysteinyl side chains at or near the active site, one molecule per alphabeta-protomer inactivates, DTT restores
-
0.1 mM, strong inhibition; strong
-
5 mM, 30°C, 30 min, 72% inhibition
-
0.1 mM, 40% residual activity
-
84% inhibition at 0.25 mM
-
1 mM, 78% residual activity
-
1 mM, 75% residual activity
-
1 mM, 87% residual activity
-
1 mM, 78% residual activity
-
irreversible, 92.6% inhibition at 1 mM, 1 h preincubation at pH 7.0 and 30°C
-
0.1 mM, no inactivation
-
complete inhibition at 0.2 mM
-
23% residual activity in the presence of 5 mM p-chloromercuribenzoate, after 30 min at 30°C
-
inhibits both isozymes TAH I and TAH II
-
45% residual activity at 1 mM
-
completely inactivated after 49 h at 22°C, activity can not be recovered by adding dithiothreitol
-
completely inactivated at a concentration of 0.005 mM, 95% of the activity can be recovered by addition of 10 mM dithiothreitol in the reaction mixture; inhibition can not be prevented in the presence of beta-ketoadipate
-
5 mM, 51% residual activity
-
5 mM, 30 min, 70°C, pH 8.5, 70% inhibition
-
20% residual activity after 30 min at 8 mM
-
inactivation completely reversed by dithiothreitol
-
Pseudomonas putida AC866
-
little effect on the activity
-
complete inhibition at 25 mM
-
1 mM inhibits 10% of the activity
-
no inhibition below 1 mM
-
complete inhibition at 0.1 mM
-
dithiothreitol protects against inhibition
-
0.5 mM, strong inhibition
-
0.5 mM, complete inhibition
-
50% inhibition of DNA phosphatase activity, 90% loss of exonuclease activity
-
inhibitor of acyl-CoA thioesterase 2
-
50% inhibition at 0.001 mM
-
0.3 mM, complete inhibition
-
70-80% inhibition in presence of 0.0004 M
-
in absence of 2-mercaptoethanol
-
in absence of 2-mercaptoethanol, isoenzyme I and III are completely inhibited by 0.2 mM PCMB, Activity of isoenzyme II is inhibited 20%
-
2 mM, complete inhibition of Mn2+-dependent enzyme and Mg2+-dependent enzyme
-
0.1-0.2 mM, 85%-100% inhibition
-
1 mM, 54% inhibition of isoenzyme I, 33% inhibition of isoenzyme II, 9% inhibition of isoenzyme III
-
62.99% residual activity at 0.1% (w/v); 69.39% residual activity at 0.1% (w/v); 72.81% residual activity at 0.1% (w/v)
-
partially restored by addition of cysteine
-
0.2 mM, 100% inhibition of acid phytase, 78% inhibition of alkaline phytase
-
0.05 mM, 90% inhibition
-
inhibition of cytosolic and membrane-bound enzyme
-
reversible with excess of cysteine
-
enzyme is very sensitive to
-
plasma membrane and microsomes
-
at 0.1 mM, about 25% inhibition
-
98% inhibition at 0.2 mM
-
7.2% inhibition at 25 mM
-
completely inhibited by 1 mM
-
strongly inhibits the enzyme of all brain regions
-
complete inhibition at 0.1 mM
-
23% residual activity in the presence of 5 mM p-chloromercuribenzoate, after 30 min at 30°C
-
92% inhibition at 0.1 mM
-
strong inhibition at 1 mM
-
98% inhibition of isozyme alpha-amylase I at 0.5 mM
-
0.05 mM, 52% inhibition of intestine alpha-amylase, 68% inhibition of muscle alpha-amylase
-
1 mM, 92% loss of activity
-
no inhibition by 2 mM with p-nitrophenyl-alpha-D-glucopyranoside as substrate
-
complete inhibition by 0.1 mM
-
1 mM, 30-50% inhibition
-
1 mM: complete inhibition, 0.001 mM: 50% inhibition
-
3.3 mM, 15 min at 37°C, 88% inhibition
-
0.25 mM, complete inhibition
-
1 mM, complete inhibition
-
4 micromol complete inhibition
-
1 mM complete inhibition
-
0.5% residual activity at 0.5 mM
-
complete inhibition at 2 mM
-
complete inhibition at 2 mM
-
0.06 mM, 91% inhibition
-
80% inhibition at 0.1 mM, 94% at 0.5 mM
-
0.1 M, complete inactivation
-
45% inhibition by 0.1 mM, 65% inhibition by 0.5 mM. Inhibition can be reversed by DTT
-
4 mM, complete inhibition
-
0.2 mM 60% residual activity
-
88% residual activity at 1 mM
-
50% inhibition at 0.065 mM
-
18% residual activity at 10 mM
-
inactivation, the enzyme can be reactivated by L-cysteine
-
1 mM, 97% inhibition, exogenous thiols like dithiothreitol, 2-mercaptoethanol or cysteine HCl reactivate
-
0.01 mM, 100% inhibition
-
0.001-0.1 mM, inactivation is partly reversed by adding 10fold to 20fold excess of glutathione or 1,2-dithiopropanol
-
0.5 mM, 75% loss of activity after 30 min at 22°C, cysteine reactivates
-
restored by mercaptoethanol or dithiothreitol
-
-
208595, 208599, 208601, 208602, 208604, 208608, 208609, 208616, 208622, 208628, 208635, 208636, 208638
-
0.1 mM, complete inhibition of mutant enzyme M185L/S295A/I297V/S350P/S351P/Q352D/A376S
-
0.1 mM, complete inhibition of recombinant enzyme
-
complete inhibition at 2 mM
-
95% inhibition of isozyme MG4, no inhibition of isozyme MG6
-
1 mM, 5% loss of activity
-
2 mM, complete inhibition
-
63.1% residual activity of cellobiase produced in the presence of 2-deoxy-D-glucose at 0.5 mM
-
56.34% inhibitory effect at 1 mM
-
1 mM, complete inhibition
-
33.3% inhibition at 2 mM
-
complete inhibition at 0.085 mM
-
strong inhibition at 0.1 mM
-
70% inihibition at 0.5 mM
-
strong inhibition at 1.25 mM
-
53% inhibition at 0.5 mM
-
strong inhibition at 1 mM
-
sensitivity only for cellobiase activity
-
the mycelial extract shows 66.9% residual activity at 0.5 mM, the purified enzyme shows 36.9% residual activity at 0.5 mM
-
alpha-Gal III shows less than 8% of the original activity by treatment with 0.1 mM p-chloromercuribenzoate at 20°C for 1 h; alpha-Gal II shows less than 6% of the original activity by treatment with 0.1 mM p-chloromercuribenzoate at 20°C for 1 h
-
16% residual activity at 0.01 mM, at pH 5.8
-
complete inhibition at 5 mM
-
1 mM, 30°C, 30 min, complete inhibition of wild-type enzyme, no inhibition of mutant enzyme C159A
-
complete inhibition at 10 mM
-
1 mM, complete inhibition
-
inhibition of 86.2% enzyme activity
-
10 mM, 20% loss of activity
-
1 mM, complete inhibition
-
0.5 mM, 62% inhibition of isozyme IT I, 86% inhibition of isozyme IT II
-
0.1 mM, 94% inhibition of the CM-cellulose adsorbed enzyme, enzyme embedded within a polyacrylamide gel is inhibited 16.7%
-
0.1 mM, significant inhibition
-
0.002 mM, 21% inhibition of invertase I, 79% inhibition of invertase II
-
6 mM, complete inhibition
-
1 mM, 80% inhibition of beta-fructofuranosidase activity, 65% inhibition of invertase activity
-
1 mM is required for inhibition of more than 50%
-
complete inhibition at 10 mM, 72% inhibition at 1 mM
-
slight inhibition of isozyme GA-II at 1 mM, no inhibition of isozyme GA-I
-
inhibition of beta-xylosidase A
-
complete inhibition at 2 mM
-
1 mM, 2% residual activity
-
strong inhibition between 0.01 mM and 0.001 mM
-
strong inhibition at 1 mM
-
slight inhibition on laminarin hydrolysis, strong inhibition on disruption of living cells
-
5 mM, 90% of initial activity
-
0.01 mM, 20% inhibition
-
0.1 mM, 90% loss of activity of cellulase 4.5, 50% loss of activity of cellulase 4.8
-
1 mM, 11% residual activity
-
0.1 mM, 50% residual activity
-
1.8 mM, complete loss of activity
-
complete inhibition at 0.005 mM
-
50% inhibition at 0.0015 mM, totally reversal by addition of 4 mM DTT
-
92% inhibition at 0.1 mM
-
43% inhibition with 0.5 mM
-
with 1 mM 20% of activity remains
-
0.025 and 0.05 mM cause 70 and 83% inhibition
-
inhibits forms II, III and IV, competitive inhibition
-
concentration of 2 mM causes 28.5% inhibition
-
0.1 mM cause 16% inhibition
-
form A: 93% inhibition with 0.1 mM, form P: 98% inhibition with 0.1 mM
-
reversible inactivation
-
1 mM 34% inhibition; 1 mM, complete inhibition
-
more than 90% inhibition
-
at 50 mM 50% inhibition of PhX20, 40% inhibition of PhX33
-
20 mM, complete inhibition
-
1 mM, complete inhibition, xylanase A
-
presence of cysteine protects against inactivation but no recovery
-
1.0 mM, pH 5.0, at 30ºC, 65% inhibition
-
53% inactivation at 1 mM, 93% inactivation at 5 mM
-
1 mM, 30% loss of activity
-
native enzyme: 46% inhibition, immobilized enzyme: 15% inhibition
-
extracellular enzyme, 1 mM: 46% inactivation
-
IFO 3134, slight inhibition
-
5 mM, 94% inhibition of 2-nitrophenyl beta-D-galactopyranoside hydrolysis, 90% inhibition of 4-nitrophenyl beta-D-glucopyranoside hydrolysis
-
mM PCMB causes quantitative inhibition
-
80% inhibition at 0.5 mM
-
reversal by sulfhydryl agents
-
inhibition of isozymes LAP1, LAP2, and LAP3
-
81% inhibition at 0.1 mM
-
100% inhibition at 1 mM
-
0.1 mM, relative activity: 6%
-
61% remaining activity at 1 mM
-
-
35973, 35979, 35981, 35984, 35986, 35991, 35994, 35998, 36000, 36005, 36007, 36008
-
2 mM, complete inactivation
-
inhibits cleavage of Arg-Pro-Pro
-
100% inhibition at 1 mM
-
100% inhibition at 0.1 mM
-
inhibition is reversed by 2-mercaptoethanol
-
30°C, 10 min, 1 mM, 95% loss of activity
-
not with Leu-enkephalin as substrate
-
complete inhibition at 0.001 mM
-
1.0 mM, 15 min, 40°C, complete inhibition
-
complete inhibition at 1 mM
-
complete inhibition at 1 mM, at 30°C and pH 3.1
-
1 mM, 28% inhibition, isoenzyme MpiCP-1; 1 mM, 97% inhibition, isoenzyme MpiCP-2
-
irreversible inhibition, no reactivation by addition of bivalent metal ions or SH-protecting reagents like cysteine and beta-mercaptomethanol
-
100% inhibition at 1 mM
-
1 mM, activity is completely lost
-
reversible reactivation by mercaptoethanol
-
14% residual activity at 0.2 mM
-
enzyme from kidney and brain
-
enzyme from brain and skin
-
inhibition is partly reversed by Cys
-
non-peptide irreversible serine-peptidase inhibitor
-
activity is completely inhibited by the cysteine-group specific inhibitor
-
cysteine restores activity
-
15% residual activity at 2 mM
-
activity restored by cysteine
-
82% inhibited by 0.01 mM
-
complete inhibition at 0.1 mM
-
0.1 mM, 100% inhibition
-
weak, caseinolytic activity
-
6% inhibition at 0.5 mM, 98.1% at 5 mM
-
complete inhibition at 0.1 mM
-
2.5 mM; peptide I as substrate
-
affects specifically MPP, dithioerythritol protects
-
0.1 mM, 6.4% inhibition
-
inactivates the partially purified enzyme, with 0.005 mM substantial inhibition
-
complete inhibition at 0.5 mM
-
reversed by mercaptoethanol
-
1 mM, incubation at 30°C for 10 min, complete inhibition
-
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