Ligand p-hydroxymercuribenzoic acid

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Basic Ligand Information

Molecular Structure
Picture of p-hydroxymercuribenzoic acid (click for magnification)
Molecular Formula
BRENDA Name
InChIKey
C7H7HgO3
p-hydroxymercuribenzoic acid
WMHRYLDWLOGHSG-UHFFFAOYSA-M
Synonyms:
4-(hydroxymercuri)benzoic acid, 4-(hydroxymercuri) benzoic acid, 4-hydroxy-mercuribenzoate, 4-hydroxy mercuribenzoate, 4-hydroxymercuribenzoate, 4-hydroxymercuribenzoic acid, 4-hydroxymeruribenzoate, p-hydroxy-mercuribenzoate, p-hydroxymercuribenzoate, p-hydroxymercuric benzoate, p-hydroxymercurybenzoate, p-hydroxymercurybenzoic acid, p-hydroxy mercurybenzoic acid, para-hydroxy-mercuribenzoate, parahydroxymercuric benzoate

Roles as Enzyme Ligand

Substrate in Enzyme-catalyzed Reactions (1 result)

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EC NUMBER
REACTION
REACTION DIAGRAM
LITERATURE
ENZYME 3D STRUCTURE
p-hydroxymercuribenzoate + H+ = Hg2+ + p-hydroxybenzoate
show the reaction diagram
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Activator in Enzyme-catalyzed Reactions (9 results)

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EC NUMBER
COMMENTARY
LITERATURE
ENZYME 3D STRUCTURE
1 mM, completely inhibits activity
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activation, depending on presence of oxidized or reduced substrates
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slight activation, 0.1-1.0 mM
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0.1 mM, 22% activation. The enzyme may be a 3-phytase, EC 3.1.3.8, or a 6-phytase, EC 3.1.3.26. The product of the hydrolysis of myo-inositol hexakisphosphate i.e. myo-inositol 1,2,3,4,5-pentakisphosphate or myo-inositol 1,3,4,5,6-pentakisphosphate has not been identified
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0.1 mM, 22% activation. The enzyme may be a 3-phytase, EC 3.1.3.8, or a 6-phytase, EC 3.1.3.26. The product of the hydrolysis of myo-inositol hexakisphosphate i.e. myo-inositol 1,2,3,4,5-pentakisphosphate or myo-inositol 1,3,4,5,6-pentakisphosphate has not been identified
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isoform A shows 112% activity at 0.5 mM
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slightly enhances activity
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1 mM: 102% of maximal activity, slight activation
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Inhibitor in Enzyme-catalyzed Reactions (662 results)

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EC NUMBER
COMMENTARY
LITERATURE
ENZYME 3D STRUCTURE
20% loss of activity, saturated
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0.4 mM and 1 mM inhibit activity to 21% and 41% respectively
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26% inhibition at 0.1 mM
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96% inactivation after 5 min preincubation; 96% inactivation within 5 min, complete reactivation by dithiothreitol
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0.005 mM, complete inhibition, prevented by 10 mM glutathione
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complete inhibition at 0.01 mM
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complete inhibition at 0.0075 mM
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40% inhibition at 0.1 mM
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50% inhibition at 0.05 mM
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97% inactivation at 1 mM
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14% inhibition at 0.01 mM, 56% inhibition at 0.1 mM, 100% inhibition at 1.0 mM
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almost complete inhibition at 0.05 mM
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almost complete inhibition at 0.05 mM
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complete inhibition at 0.025 nM
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slight inhibition
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complete inhibition at 1 mM
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moderate
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decarboxylation of isocitrate and oxalosuccinate
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0.1 mM, strong
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strong inhibition
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0.1 mM, 49% residual activity
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2 mM, 5% residual activity
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1 mM, complete inhibition
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0.1 mM, complete inhibition
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no activity
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100% inhibition at 1 mM
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43% inhibition at 0.005 mM, 100% inhibition at 0.05 mM
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0.1 mM, 13% inhibition
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1 mM, 87% inhibition after 10 min
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1 mM, 75% inhibition
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0.1 mM, complete loss of activity
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0.02 mM, no residual activity
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96% inhibition at 0.5 mM
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at least 90% inhibition at 0.2 mM
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partial protection in presence of 2-hydroxybiphenyl, reversed by excess of dithiothreitol
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12% residual activity at 1 mM
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1 mM, 35% inhibition
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0.052 mM, 39% inhibition
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partially reversible by thiol compounds
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slightly
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0.1 mM, 89% inhibition
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completely inhibited at 1 mM; Mn-SOD
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50% inhibition at 1.5 mM
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1-3 mM
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complete inhibition at 1 mM in absence of DTT, 2 mM DTT protect nearly completely; strongly suppress enzyme reaction, reversed by addition of DTT
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0.1 mM, 3 min, complete inhibition
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1-3 mM
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62% residual activity at 0.1 mM
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0.1 mM, complete inhibition
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total inhibition, reversed by thiol
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1 mM, 77% inhibition
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44% inhibition of anaerobic, 23% inhibition of aerobic enzyme at 0.5 mM
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0.1 mM, 97% inhibition, 4 min half-time at 0.067 mM, enzyme is protected from inactivation by the prior addition of butyryl-CoA
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little effect
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0.1 mM, almost complete inhibition of the apo-enzyme
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strong inhibition of the apoenzyme at 0.1 mM, not inhibitory for the holo form even at higher concentrations like 1 mM
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98% inhibition after 5 min at 0.00227 mM
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no effect on aminating activity, inhibition of deaminating activity
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complete inhibition at 1 mM, 5 min
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complete inhibition at 0.1-1 mM, at 0.0005 mM 33% inhibition or 75% inhibition after preincubation in presence of glutamine and 2-oxoglutarate, substrates induce a conformation, which makes essential sulfhydryl groups more accessible to reagent
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0.01 mM, 100% inhibition
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5 mM, moderate inhibition of isozymes 1-3
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significant inhibition (6.2% residual activity at 1 mM)
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0.1 mM, 78.6% inhibition
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90% inhibition at 0.008 mM, inhibition can be prevented by addition of excess dithiothreitol
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0.2 mM, complete inhibition
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0.001 M, 80% inhibition
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0.001 M, 49% inhibition
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92% inhibition at 1 mM
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presence of mercaptoethanol or NADPH provides slight protection against inhibition
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0.5 mM, slight inhibition
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0.067 mM, 50% inhibition
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48% inhibition at 2 mM
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1 mM, 46% residual activity
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50% inhibition at 1 mM, 40% inhibition at 0.5 mM and 10% inhibition at 0.1 mM
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activity can be restored by cysteine
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1 mM, 70% inhibition
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100% inhibition at 0.5 mM, inhibition can be reversed by reduced glutathione or cysteine
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0.1 mM; 97% inhibition
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0.00001 mM, 75% loss of activity
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70-100% inhibition at 0.2 mM
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complete inhibition at 0.1 mM
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95% inhibition at 10 mM, reversed in presence of 20 mM Cys
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inhibition is completely reversed by 2-mercaptoethanol
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complete inhibition at concentrations higher than 0.5 mM
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weak
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0.1 mM, total inhibition
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1 mM, 24°C, 90% inhibition after 40 min
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activity inhibited at 2 and 6 mM
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strong
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99% inactivation
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weak
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2 mM, complete inhibition
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0.0001 mM, complete inhibition
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60% inhibition at 0.1 mM, protection by oxaloacetate
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complete inhibition at 0.1 mM
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strong
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strong, 0.1 mM, 99.3% inhibition with quercetin as substrate, 14 mM 2-mercaptoethanol protects and addition after 15 min also reduces the inhibitory effect
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40% inhibition at 0.2 mM and 80% inhibition at 2 mM
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18.45% residual activity at 1 mM
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0.01 mM, 65% inhibition
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10 mM, 50% inhibition
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1 mM: complete inhibition
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0.5 mM, complete inhibition
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1 mM, 25% inhibition
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complete inhibition at 0.1 mM
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reduces specific activity by 50%
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no protection by substrate, protection but not reversal of inhibition by thioethanol, complete inhibition above 0.00125 mM, cysteine reverses inhibition
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2-mercaptoethanol prevents inhibition
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0.0001 mM, complete inhibition
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weak
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0.02 mM, 50% inhibition
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1 mM, complete inhibition
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complete inhibition at 0.001 mM
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95% inhibition at 0.4 mM
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reversal by monothioglycerol
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inhibition at 0.4 mM, can be reversed by 2-mercaptoethanol
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0.1 mM, 2% remaining activity
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0.1 mM, about 65% loss of activity
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0.2 mM, at 37°C, 2 min, 80% loss of activity, 2-mercaptoethanol partially restores activity
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5 mM lead to 90% inhibition
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the enzyme is relatively insensitive to sulfhydryl reagents
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1 mM, 5% residual activity
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at very low concentration
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lysosomal enzyme
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in absence of sulfhydryl compounds
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slight
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0.5 mM, 96% inhibition
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86% inhibition of isozyme MG4, 22% inhibition of isozyme MG6
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strong inhibition at 1 mM
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0.25 mM, 97.8% inhibition
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complete inhibition at 1 mM
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strong inhibition at 1 mM
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weak
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83.4% of control activity at 1 mM, 12.2% at 2 mM
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1 mM, 94% inhibition
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bestatin protects inactivation
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5 mM, 90% inhibition
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1 mM, 2% residual activity
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reactivated by DTT
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1 mM, complete inhibition
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10 mM, 80% inhibition
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complete inhibition at 0.2 mM, both enzyme forms
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0.2 mM, 68% inhibition
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100% inhibition with 0.1 mM
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0.002 mM, 71% residual activity
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0.022 mM, 99% inhibition
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1 mM, 67% inhibition
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26% inhibition at 1 mM
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1 mM, 49% loss of activity
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0.00001 mM: 4% inhibition, 0.0001 mM: 60% inhibition, 0.001 mM: complete inhibition
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complete inhibition at 1 mM
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complete inhibition at 1 mM
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0.0005 mM, 2.5% of maximal activity
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1 mM, complete inhibition; complete inhibition at 1 mM
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5 mM, complete inhibition
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no inhibition in presence of 25 mM beta-mercaptoethanol
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1 mM, 35% of inhibition
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60% inhibition at 1 mM, reversal by GSH
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14% inhibition at 1 mM
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weak
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1 mM, 40% inhibition
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glutathione protects
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1 mM, 59% residual activity
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2-mercaptoethanol or dithiothreitol prevent inactivation
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complete inhibition at 0.016 mM
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ternary complex stable, apoenzyme unstable
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on addition of glutathione or mercaptoethanol the activity is regained
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inhibition is reversed by presence of cysteine
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0.0001 mM, 50% inhibition; even in the presence of ethanolamine
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0.5 mM, 43% inhibition of isoenzyme with pI 5.1
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1 mM, 92% inhibition
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reactivation by NAD+ and 2-mercaptoethanol
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tRNA or DTT protects against heat inactivation
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inhibition is reversible by either CoA or mercaptoethanol
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partial protection by ATP
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70% inhibition at 5 mM
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3D Structure of Enzyme-Ligand-Complex (PDB) (21 results)

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Enzyme Kinetic Parameters

KM Value (2 results)

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EC NUMBER
KM VALUE [MM]
KM VALUE MAXIMUM [MM]
COMMENTARY
LITERATURE

Ki Value (7 results)

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EC NUMBER
KI VALUE [MM]
KI VALUE MAXIMUM [MM]
COMMENTARY
LITERATURE
TABLE ID
0.002
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5611
0.01
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5760
0.2
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pH 8.0, 37°C
17410
0.05
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34356
4
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39588
0.005
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pH 6.3, 30°C
39776
0.0001
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39954

IC50 Value (7 results)

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EC NUMBER
IC50 VALUE
IC50 VALUE MAXIMUM
COMMENTARY
LITERATURE
0.24
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at pH 7.5 and 30°C
0.17
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pH 6.0, 70°C
0.0035
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pH 6.8, 30°C
0.0019
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pH 7.8, temperature not specified in the publication
0.0019
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pH 7.8, temperature not specified in the publication

References & Links

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