Ligand p-chloromercuribenzoic acid

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Basic Ligand Information

Molecular Structure
Picture of p-chloromercuribenzoic acid (click for magnification)
Molecular Formula
BRENDA Name
InChIKey
C7H6ClHgO2
p-chloromercuribenzoic acid
YFZOUMNUDGGHIW-UHFFFAOYSA-M
Synonyms:
4-chlormercurybenzoate, 4-chloromercuribenzoate, 4-chloromercuribenzoic acid, 4-chloromercuribenzonic acid, 4-chloromercurybenzoate, beta-chloromercuribenzoate, chloromercuribenzoate, chloromercuribenzoic acid, p-(chloromercuri)benzoate, p-(chloromercuri)benzoic acid, p-chlormercuribenzoate, p-chloro-mercuribenzoate, p-chloromercuri-benzoic acid, p-chloromercuribenzoate, p-chloromercuric benzoate, p-Chloromercuricbenzoate, p-chloromercuriobenzoate, p-chloromercurybenzoate, p-Chloromeruribenzoate, p-chloroymercuribenzoate, p-mercuric chlorobenzoate, PCMB

Roles as Enzyme Ligand

Substrate in Enzyme-catalyzed Reactions (1 result)

EC NUMBER
REACTION
REACTION DIAGRAM
LITERATURE
ENZYME 3D STRUCTURE
p-chloromercuribenzoate = Hg2+ + p-hydroxybenzoate
show the reaction diagram
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Activator in Enzyme-catalyzed Reactions (31 results)

EC NUMBER
COMMENTARY
LITERATURE
ENZYME 3D STRUCTURE
activation of enzyme MGR I, inhibition of enzyme MGR II
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0.02 mM, 2.5fold increase in oxaloacetate reduction activity
-
at 0.1 mM 133% of the activity without activator
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118% activity at 0.05 mM
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substancial stimulation
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stimulation
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increases oxidase and dehydrogenase activities, maximal rate of oxidation of lysine at 4-5 mol p-chloromercuribenzoate per mol enzyme, for arginine at 3 mol per mol enzyme
-
increases total activity up to 0.005 mM
-
1 mM, completely inhibits activity
-
1 mM, 1.9fold activation
-
potent inhibitory effect indicating that free SH groups are essential for activity
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80 mM, relative activity 118%
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activates in presence of Mg2+, inhibits in presence of Mn2+
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activates
-
9% activation at 1 mM
-
slight stimulation
-
stimulation of hydrolase reaction, no influence on transpeptidase
-
slight stimulation
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1 mM, 18% inhibition
-
0.1-1 mM, about 25% increase in activity
-
0.105 mM, activity 112%
-
inhibits at high concentrations, activates at low concentrations
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Inhibitor in Enzyme-catalyzed Reactions (2087 results)

EC NUMBER
COMMENTARY
LITERATURE
ENZYME 3D STRUCTURE
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
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0.2 mM, 92% inhibition
-
complete inhibition at 1 mM, partial reversible by low concentration of cysteine
-
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
-
25% inhibition at 1 mM
-
complete inhibition at 1 mM
-
also other sufhydryl reagents like 5,5'-dithiobis-2-nitrobenzoic acid and iodoacetamide strong
-
strong inhibition
-
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 1 mM concentration
-
17% inhibition at 0.1 mM
-
complete inhibition at 1.0 mM
-
complete inhibition at 0.001 mM
-
60% inhibition at 1 mM, reversal by an excess of L-cysteine
-
strong inhibition at 0.1 and 1.0 mM
-
complete inhibition at 1 mM
-
0.5 mM
-
0.1 mM, complete inhibition
-
100% inhibition
-
79% inhibition at 0.1 mM, partially reversed by 0.1 mM 2-mercaptoethanol
-
strong
-
0.19 mM, 43% residual activity
-
0.001 mM, 2 min, complete inhibition
-
complete inhibition at 1 mM and above
-
weak inhibition
-
1 mM, complete inhibition
-
0.1 mM, 72% inhibition
-
0.005 mM, 75% loss of activity after 1 h
-
can be overcome by addition of gluthathione
-
10 mM leads to 50% inhibition
-
10 mM, strong inhibition, 5% residual activity is reversed to 65% activity by either 1 mM glutathione or cysteine
-
0.1 mM, complete inhibition
-
1 mM, 4% residual activity
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weak
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o-chloromercuribenzoate, m-chloromercuribenzoate, and p-chloromercuribenzoate inhibit in absence but not in presence of cyanide
-
21% inhibition at 1 mM
-
1 mM, 95% inhibition
-
22% inhibition at 0.1 mM
-
1 mM, 40% inhibition
-
1 mM, 41.0% inhibition
-
10-20% inhibition at 0.01 mM
-
100% inhibition at 0.25 mM
-
1 mM, 96, 94 and 95% inhibition of isoenzymes Ia, Ib and II respectively
-
20% inhibition at 0.33 mM
-
30% inhibition of isoform Gpx-1 at 0.3 mM
-
complete inhibition at 0.33 mM, summation effect with 2-mercaptoethanol
-
0.17 mM, 35% inhibition
-
80% inhibition at 0.1 mM
-
0.05 mM, 47% inhibition
-
70% inhibition at 0.1 mM
-
0.1 mM, 30% inhibition
-
65% residual activity at 0.5 mM
-
excellent competitive inhibitor
-
10 mM, 24% inhibition
-
1 mM, 44% loss of activity
-
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
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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
-
0.1 mM, 14% inhibition
-
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
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at low concentrations
-
; 0.05 mM, quick and complete inhibition
-
0.1 mM, 87% inhibition
-
81% inhibition at 1 mM
-
0.01 mM, 62% inhibition, reversed by dithiothreitol
-
partial inhibition
-
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
-
at 1 mM complete inhibition
-
0.1 mM, 17% residual activity
-
92% inhibition at 1 mM
-
32% inhibition at 0.5 mM
-
0.1 mM concentration, 51% inhibition
-
1 mM, complete inhibition after 10 min
-
slight at 0.5 mM
-
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
-
91% inhibition at 1 mM
-
1 mM, 10 min at 35°C, complete loss of activity
-
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
-
94% inhibition at 0.0005 mM
-
0.01 mM causes 88-96% inhibition
-
0.005 mM, 75% loss of activity after 1 h
-
0.33 mM, complete inhibition
-
0.1 mM, 36% inhibition
-
inhibition of the reduction of benzoyladenosine 5'-monophosphate, even in the presence of dithiothreitol
-
100% inhibition at 1 mM
-
1 mM, complete inhibition
-
41% residual activity at 1 mM
-
0.1 mM, 21% residual activity
-
0.1 mM concentration 100% inhibition
-
3.0 mM, 100% inhibition, 0.33 mM, 37% inhibition
-
0.01 mM, 90% inhibition, 0.001 mM, 30% inhibition
-
stronger effect on isoform F1
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1 mM, 90% inhibition
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16.7 mM, 87% inhibition
-
protection by FAD
-
slight 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
-
60% inhibition at 1 mM
-
at 0.1 mM 18% activity remains
-
inhibition of enzyme-catalyzed C-2 proton-deuteron exchange reactions
-
1 mM, 43% inhibition
-
progressive decrease in enzyme activity of both isoenzymes, inhibition is not affected by addition of GTP or ADP
-
completely inhibited at 0.005 mM
-
91% inhibition at 0.0005 mM, partially reversed by glutathione
-
2.0 mM
-
0.1 mM, 90-95% inhibition
-
0.1 mM, complete inhibition
-
strong inhibition
-
90% inhibition of the methylene blue specific, 70% inhibition of the dichlorophenolindophenol specific enzyme at 0.5 mM
-
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
-
0.1 mM, 97% inhibition
-
inhibition reversed by 2-mercaptoethanol
-
100% inhibition at 1 mM
-
complete inhibition of ubiquinone reductase activity, 70% inhibition of disproportion activity
-
inhibition at 1 mM
-
0.044 mM, 40-50% inhibition after 30 min, activity can be restored by adding 2-mercaptoethanol
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0.05 mM, complete inhibition
-
0.1 mM, 40% inhibition
-
0.1 mM
-
completely inhibits at 0.1 mM
-
both NADPH and NADP1 suppress the inhibition, but NADH does not
-
0.2 mM, 81% inhibition
-
the reduction of cytochrome c, K3Fe(CN)6 and hydroxylamine is completely inhibited (more than 99%) by 0.02 mM p-chloromercuribenzoate
-
at 1 mM 85% inhibition
-
47% inhibition at 0.5 mM
-
0.1 mM, 50% inhibition
-
0.054 mM, 88% inhibition
-
with NADPH
-
0.02 mM, 100% inhibition. Inhibition can be partially or completely reversed by cysteine
-
complete inhibition at 1 mM
-
0.3 mM, completely inhibits, can be reversed by cysteine or glutathione
-
0.5 mM, 51% inhibition
-
5 mM, 84% inhibition
-
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
-
complete inhibition at 1 mM, reversible by addition of glutathione
-
0.01 mM, 85% inhibition
-
strong
-
5 mM, complete inhibition
-
0.001 50% inhibition
-
strong
-
0.4 mM, 40% inhibition, can be reversed by 12 mM 2-mercaptoethanol
-
reversible by cysteine
-
1 mM, strong
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0.1 mM, complete inhibition, activity can be restored by incubation with 2 mM dithiothreitol for 30 min at 0°C
-
0.005 mM, complete inhibition of retinol-(cellular-retinol-binding-protein)type II esterification
-
weak
-
90% inhibition at 0.1 mM, complete inhibition at 1 mM
-
0.5 mM: 95% inhibition
-
0.2 mM, 64% inhibition
-
1 mM, complete inhibition
-
complete inhibition, DTT protects
-
partially restorable by dithiothreitol
-
complete inhibition at 1 mM
-
strong inhibition
-
strong inhibitor at 1 mM
-
complete inhibition at 1 mM
-
above 2.0 mM
-
strong
-
50% inhibition at 2.5 mM
-
activity abolished at 5 mM
-
complete inhibition of type II fatty acid synthase at 1 mM
-
35.2% residual activity after 1 h at 1 mM
-
reversible by GSH, 2-mercaptoethanol or 2,3-dimercaptopropanol, not L-cysteine
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0.1 mM
-
0.1 mM. 100% inhibition
-
0.1 mM, 2% residual activity
-
0.05 mM, 9% residual activity
-
0.1 mM, 97% inhibition
-
90% inactivation at 0.01 mM, dithiothreitol reverses
-
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
-
weak
-
10 mM, 25% inhibition
-
47% inhibition at 1 mM, 10 mM dithiothreitol protects
-
0.01 mM, 94% inhibition
-
complete inhibition at 0.02 mM
-
at 0.05 mM: almost 30% of the original enzyme activity remains
-
1 mM, 100% inhibition, 14 mM 2-mercaptoethanol completely restores activity
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10 mM, completely inhibited
-
0.1 mM, complete inhibition
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1 mM, 4% residual activity
-
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
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strong
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5-10 mM, more than 90% inhibition
-
0.2 mM, complete inhibition
-
reversed by cysteine
-
0.05 mM, complete inhibition
-
at 1 mM inhibits the reaction completely
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complete
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above 0.01 mM
-
reversed by dithiothreitol or 2-mercaptoethanol
-
weak
-
weak
-
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
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50 mM, strong inhibition
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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
-
0.001 mM, about 90% inhibition
-
complete inhibition at 0.02 mM, reversible by cysteine
-
1 mM, complete 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
-
4 mM, 36% inhibition, D-alanine and pyridoxal 5'-phosphate protect to some extent
-
77% inhibition at 0.5 mM
-
1 mM, 99% inhibition
-
0.25 mM: 48% inhibition, reactivation by addition of 2-mercaptoethanol
-
1.0 mM, complete inhibition
-
0.2 mM, 92% inhibition
-
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
-
2 mM, 15% inhibition
-
cysteine reverses
-
0.005 mM, 50% 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%
-
2-mercaptoethanol protects from inactivation
-
0.1 mM, complete inhibition
-
thiol reagents protect or reverse
-
0.0007 mM, 50% inhibition of ribavirin and deoxadenosine kinase activity
-
1 mM, 17% inhibition
-
0.5 mM, 3% residual activity
-
0.125 mM, complete inhibition. Preincubation with 0.25 mM dithiothreitol for 5 min partially protects
-
0.1 mM, 66% inhibition
-
0.83 mM, 95% inhibition
-
0.1 mM, 69% loss of activity
-
2-mercaptoethanol reverses
-
1,4-dithiothreitol reverses
-
5 mM, inhibits reaction with diphosphate and adenylylsulfate
-
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
-
inactivation
-
preincubation dramatically inhibits enzyme activity
-
1 mM
-
50% inhibition at 0.000025 mM
-
sensitive above 1 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
-
0.1 mM, 81% inhibition
-
little effect on the activity
-
complete inhibition at 25 mM
-
0.1 mM, 26% inhibition
-
50% inhibition of DNA phosphatase activity, 90% loss of exonuclease activity
-
slight
-
50% inhibition at 0.001 mM
-
70-80% inhibition in presence of 0.0004 M
-
2 mM, 100% inhibition
-
partially restored by addition of cysteine
-
0.2 mM, 35% inhibition
-
lung enzyme
-
inhibition of cytosolic and membrane-bound enzyme
-
reversible with excess of cysteine
-
slight inhibition
-
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
-
1 mM, 30-50% inhibition
-
1 mM: complete inhibition, 0.001 mM: 50% inhibition
-
3.3 mM, 15 min at 37°C, 88% inhibition
-
0.5% residual activity at 0.5 mM
-
97% inhibition at 1 mM
-
4 mM, complete inhibition
-
0.2 mM 60% residual activity
-
2 mM, complete inhibition
-
1.8 mM, complete loss of activity
-
complete inhibition at 0.005 mM
-
0.5 mM, 29% inhibition
-
more than 90% inhibition
-
53% inactivation at 1 mM, 93% inactivation at 5 mM
-
1 mM, 26% inhibition
-
IFO 3134, slight inhibition
-
5 mM, 94% inhibition of 2-nitrophenyl beta-D-galactopyranoside hydrolysis, 90% inhibition of 4-nitrophenyl beta-D-glucopyranoside hydrolysis
-
50% inhibition at 3 mM
-
mM PCMB causes quantitative inhibition
-
80% inhibition at 0.5 mM
-
reversal by sulfhydryl agents
-
20% inhibition at 1 mM
-
81% inhibition at 0.1 mM
-
30°C, 10 min, 1 mM, 95% loss of activity
-
complete inhibition at 1 mM
-
domain 1B and domain
-
irreversible inhibition, no reactivation by addition of bivalent metal ions or SH-protecting reagents like cysteine and beta-mercaptomethanol
-
100% inhibition at 1 mM
-
slight
-
slight inhibition
-
partial inhibition
-
partial
-
non-peptide irreversible serine-peptidase inhibitor
-
strong inhibition
-
0.6 mM, 6% inhibition
-
46% inhibition at 1 mM
-
82% inhibited by 0.01 mM
-
complete inhibition at 0.1 mM
-
weak
-
6% inhibition at 0.5 mM, 98.1% at 5 mM
-
complete inhibition at 0.1 mM
-
affects specifically MPP, dithioerythritol protects
-
inactivates the partially purified enzyme, with 0.005 mM substantial inhibition
-
1 mM, incubation at 30°C for 10 min, complete inhibition
-
1 mM, 67% inhibition
-
noncompetitive
-