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BRENDA support

Ligand mercury(2+)

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Basic Ligand Information

Molecular Structure
Picture of mercury(2+) (click for magnification)
Molecular Formula
BRENDA Name
InChIKey
Molfile
Hg
mercury(2+)
BQPIGGFYSBELGY-UHFFFAOYSA-N
Synonyms:
cationic mercury, Hg2+

Related pathways

Pathway Source
Pathways
MetaCyc
phenylmercury acetate degradation


Show all pahtways known for Show all BRENDA pathways known for mercury(2+)

Roles as Enzyme Ligand

In Vivo Substrate in Enzyme-catalyzed Reactions (4 results)

EC NUMBER
PROVEN IN VIVO REACTION
REACTION DIAGRAM
LITERATURE
ENZYME 3D STRUCTURE

In Vivo Product in Enzyme-catalyzed Reactions (8 results)

EC NUMBER
PROVEN IN VIVO REACTION
REACTION DIAGRAM
LITERATURE
ENZYME 3D STRUCTURE

Substrate in Enzyme-catalyzed Reactions (13 results)

EC NUMBER
REACTION
REACTION DIAGRAM
LITERATURE
ENZYME 3D STRUCTURE
ATP + H2O + Hg2+/in = ADP + phosphate + Hg2+/out
show the reaction diagram
-

Product in Enzyme-catalyzed Reactions (57 results)

EC NUMBER
REACTION
REACTION DIAGRAM
LITERATURE
ENZYME 3D STRUCTURE
ATP + H2O + Hg2+/in = ADP + phosphate + Hg2+/out
show the reaction diagram
-

Activator in Enzyme-catalyzed Reactions (5 results)

EC NUMBER
COMMENTARY
LITERATURE
ENZYME 3D STRUCTURE
1 mM, about 85% inhibition
-
mercury chloride, and methylmercury, activates PLD, the stimulation is regulated by Ca2+ and calmodulin, mechanism, overview. Calcium chelating agents and calcium depletion, e.g. by EGTA, calmodulin inhibitors, e.g. calmidazolium chloride and trifluoperazine, and L-type calcium channel blockers nifedipine, nimodipine, and diltiazem attenuate the stimulation of PLD by mercury, overview
-
enhances the activity of the enzyme
-
papain activity increases to a maximum of 111.03% (non-competitive type activation) at a concentration of 0.000001x01mol/l Hg2+, but is almost completely deactivated at concentrations above 0.0001 mol/lx01Hg2+. The inhibition of Hg2+ on papain is a competitive and uncompetitive mixed type inhibition
-

Inhibitor in Enzyme-catalyzed Reactions (3534 results)

EC NUMBER
COMMENTARY
LITERATURE
ENZYME 3D STRUCTURE
complete inhibition at 1 mM
-
0.005 mM, complete inhibition, prevented by 10 mM glutathione
-
40% inhibition of NAD dehydrogenase II at 0.004 mM
-
53% inhibition at 0.002 mM
-
IC50 0.00009 mM
-
irreversible inactivation
-
complete inhibition at 2 mM
-
strong inhibition
-
nearly complete inhibition at 2 mM
-
complete inhibition at 1 mM
-
complete inhibition at 1 mM
-
99% inactivation at 1 mM
-
almost complete inhibition at 0.25 mM
-
almost complete inhibition at 0.25 mM
-
complete inhibition
-
slight inhibition
-
strong inhibitor
-
1 mM, less than 10% residual activity
-
0.1 mM, complete inhibition
-
strong
-
inhibition at 1 mM, and destabilization at 10 mM
-
2 mM, complete inactivation
-
complete inhibition at 0.1 mM
-
0.001 mM, 2 min, complete inhibition
-
complete inhibition at 1 mM
-
completely inhibits reduction of 2-dehydropantolactone
-
0.0005 mM, almost complete inhibition
-
complete inhibition at 1 mM
-
100% inhibition at 5 mM; 5 mM, 100% inhibition
-
30% inhibition at 1 mM
-
0.1 mM, complete inhibition
-
67% inhibition at 1 mM
-
1 mM, complete inhibition
-
strong inhibition at 1 mM
-
strong inhibitor
-
0.1 mM HgCl2 complete inhibition
-
1 mM, 93% inhibition
-
22% inhibition at 2 mM
-
1 mM, complete inhibition
-
0.1 mM concentration 98% inhibition
-
60% inhibition at 1 mM
-
1 mM, complete inhibition
-
2% residual activity at 1 mM
-
2 mM, 20% inhibition after 6 h
100% inhibition at 1 mM
-
strong
-
100% inhibition at 0.1 mM
-
0.01 mM, appreciable inhibition
-
21% inhibition at 0.01 mM
-
inhibition of NADH oxidizing activity
-
10 mM, 14% residual activity
-
complete inhibition at 1 mM
-
complete inhibition at 1 mM
-
0.1 mM, 45% inhibition
-
1 mM, complete inhibition
-
strong inhibition
-
inhibition reversed by glutathione
-
1 mM, 87% loss of activity
-
0.4 mM, 96% inhibition
-
0.5 mM, strong
-
causes a 20-30% fall in activity
-
50% inhibition at 0.005 mM
-
1 mM, 98% inhibition
-
0.01-0.1 mM, 96% loss of activity
-
1 mM, about 5% residual activity
-
0.1 mM HgCl2, complete inhibition
-
0.1 mM, 87% inhibition
-
complete inhibition at 0.01 mM
-
complete inhibition at 0.1 mM
-
63% inhibition at 1 mM, crude enzyme extract
-
82.05% inhibition at 0.03 mM
-
complete inhibition at 5 mM
-
87% inhibition at 0.1 mM
-
severely inhibits enzyme activity
-
0.1 mM concentration, 100% inhibition
-
0.0001 mM, 56% inhibition
-
slight inhibition
-
DELTA12-desaturase system, enzymatic complex
-
0.4 mM, 96% inhibition
-
0.77% residual activity at 1.0 mM
-
complete inhibition of hypoxanthine oxidation at 0.1 mM
-
strong inhibitor
-
62% inhibition at 1 mM
-
almost complete inhibition at 1 mM HgCl2
-
complete inhibition at 1 mM
-
77% inhibition in the presence of 1 mM
-
complete inhibition at 2 mM
-
1 mM causes complete inhibition
-
1 mM, 17.5% inhibition
-
complete inhibition at 1 mM
-
both isoforms
-
1 mM, 12 h, 4°C, 99% loss of activity
-
1 mM, complete inhibition
-
mM concentration
-
strong inhibitor, 4% residual activity at 2 mM Hg2+
-
complete inhibition at 2 mM
-
severely inhibited by 1 mM
-
complete inhibition of both orotate reductase and NADH oxidase reaction
-
1 mM, 86% inhibition
-
0.1 mM, 92% inhibition
-
1 mM, 97.9% loss of activity
-
complete inhibition at 1 mM
-
1 mM, 97% inhibition
-
completely inhibits at 0.1 mM
-
1 mM, 61% inhibition of the recombinant enzyme
-
1 mM, 29% residual activity
-
inactivation due to dissociation of FAD from the enzyme molecule and denaturation of the apoenzyme
-
complete inhibition at 10 mM
-
2.0 mM
-
almost total inhibition at 0.1 mM
-
0.13 mM, complete inhibition
-
strong inhibition at 1 mM Hg2+
-
89% inhibition at 1 mM
-
10 mM, complete loss of activity
-
1 mM, about 80% inhibition
-
strong inhibition at 1 mM
-
1 mM
-
96% inhibition at 0.1 mM
-
complete inhibition at 0.1 mg/ml
-
0.1 mM, complete inhibition
-
0.5 mM, complete inhibition
-
about 70% inhibition
-
about 70% inhibition
-
80% inhibition at 1 mM
-
inhibitory
-
relative activity less than 5%
-
strong inhibition
-
1 mM shows strong inhibitory effect on recombinant rBfmBC activity (more than 80% inhibition)
-
0.01 mM, 100% inhibition
-
1 mM, 12.4% residual activity
-
complete inhibition at 1 mM
-
complete inhibition
-
0.1 mM, complete inhibition
-
5 mM, complete inhibition
-
0.1 mM, 96% inhibition
-
5 mM, complete inhibition
-
0.1 mM, strong inhibition
-
0.1 mM, no resiudal activity
-
0.01 M, strong
-
0.5 mM Hg2+ ions totally inhibit the enzyme, even in the presence of 2 mM dithioerythritol
-
complete inhibition at 1 mM
-
relative activity 0% of control
-
100% inhibition at 0.05 mM
-
0.1 mM, 43% residual activity
-
complete inhibition
-
0.1 mM, 65% inhibition
-
0.1 mM, complete inhibition
-
0.00001 mM, 50% inhibition, noncompetitive, irreversible, probably due to formation of a thiolate
-
complete inhibition at 0.1 mM
-
0.01 mM, complete inhibition
-
strong
-
66% decrease of activity at 0.01 mM
-
strong inhibition
-
19.8% residual activity after 1 h at 1 mM
-
11% remaining activity isoenzyme Nat-b; 36% remaining activity isoenzyme NAT-a
-
noncompetitive with respect to choline, IC50: 0.0004 mM, mixed type inhibition with respect to acetyl-CoA, IC50: 0.0025 mM, activity can be recovered using 2,3-dimercapto-propanol
-
complete inhibition
-
5 mM, complete inhibition
-
95% inhibition at 2 mM
-
complete inactivation
-
1 mM
-
0.1 mM, residual activity 26%
-
strongly inhibits the sterol glucosyltransferase activity, IC50 (mM): 0.5
-
enzyme activity is completely inhibited by 0.1 mM Hg2+
-
at 1 mM
-
10 mM, complete inhibition, reversed by addition of 20 mM 2-mercaptoethanol
-
complete inhibition at 10 mM
-
1 mM, 99% inhibition with quercetin as substrate
-
0.1 mM, complete inhibition. The observed enzyme inhibition by Cu2+ and Hg2+ may not solely be attributed to their effects on the enzyme itself because these heavy metal ions are known to destroy substrate anthocyanins
-
complete inhibition at 5 mM
-
Hg2+ significantly inhibits both enzyme activities, but especially the transferase activity (complete inhibition at 1 mM)
-
slight inhibition at 1 mM
-
10 mM, complete inhibition
-
1 mM, 50°C, 30 min, abolishes the phosphorolytic activity almost completely
-
1 mM, strong
-
97% inhibition at 1 mM
-
complete inhibition at 3 mM after 3 min at 0°C
-
complete inhibition at 0.1 mM
-
complete inhibition at 1 mM
-
strongly inhibites both O-acetyl-L-serine sulfhydrylation and O-phospho-L-serine sulfhydrylation
-
weak
-
1 mM, 0% residual activity
-
strong inhibition, reducing agent reverses
-
strong
-
0.002 mM, 50% inhibition in the presence of 3 mM Mg2+
-
0.01 mM, 25% inhibition, 0.1 mM, almost complete inhibition
-
55% inhibition at 1 mM
-
at PO2 of about 20 mM
-
0.1 mM, complete inhibition
-
0.083 mM, 76% inhibition
-
strong inhibition
-
partially reversed by dithiothreitol
-
strong inhibition at concentrations above 0.5 mM in presence of Mg2+
-
1 mM, almost complete inhibition
-
10 mM, complete inhibition
-
50% inhibition at 0.001 mM
-
1 mM, no residual activity
-
30% residual activity at 1 mM
-
2.1% residual activity at 1 mM
-
0.1 mM, complete inhibition
-
5 mM
-
6% remaining activity after 5 min, 1 mM
-
9% relative residual activity
-
1 mM, 58% inhibition
-
no activity at 1 mM HgCl2
-
with RNA core as substrate
-
susceptible to inhibition by Hg2+
-
50% inhibition at 0.0006 mM, inhibition of both DNA glycosylase and apurinic nicking activities, binding capability not reduced
-
0.1 mM, no residual activity
-
competitive towards Mg2+
-
competitive
-
reduces activity by 30-40%
-
strong inhibition at 1 mM
-
mild inhibition
-
1 mM, complete inhibition
-
potent inhibitor, inhibition reversed by adding an excess of dithiothreitol
-
strong
-
strong
-
1.33 mM, 1.2% relative activity
-
strong, with p-nitrophenyl-beta-D-glucopyranoside as substrate
-
1 mM, 47.47% of initial activity
-
98% inhibition at 1 mM
-
strong
-
inhibits activity at 1 mM, 6% relative activity compared with activity without any addition of effector
-
1 mM complete loss of activity
-
10.37% residual activity at 5 mM
-
1 mM, 77% inhibition
-
1 mM, 88% loss of activity
-
complete inhibition at 1 mM
-
10 mM, significant inhibition
-
10 mM, complete inhibition
-
1 mM, no residual activtiy
-
about 40% residual activity at 5 mM
-
5 mM, 25% loss of activity
-
no activity is detected after 1 h of incubation at 1mM Hg2+
-
0.1 M, 80% loss of activity
-
1 mM, 3% of initial activity
-
complete inhibition at 5 mM
-
noncompetitive
-
5 mM, strong inhibition
-
5 mM complete inactivation
-
more than 90% inhibition
-
5 mM, complete inhibition
-
1 mM, complete inhibition of 2-nitrophenyl beta-D-galactopyranoside hydrolysis and 4-nitrophenyl beta-D-glucopyranoside hydrolysis
-
65% inhibition at 5 mM
-
1 mM,61% inhibition
-
99% inhibition at 1 mM, recombinant enzyme
-
strong, reversible by dialysis against 2 mM DTT
-
1 mM, complete inhibition, IC50: 0.67 mM
-
100% inhibition at 1 mM
-
1 mM, 90% inhibition
-
1 mM, complete inhibition
-
26% inhibition of amidolytic activity at 1 mM
-
inhibition of amidolytic activity
-
1 mM, 50% inhibition
-
1 mM, strong inhibition
-
order of decreasing inhibitory effect: Cu2+, Hg2+, Zn2+, Ni2+, Co2+
-
papain activity increases to a maximum of 111.03% (non-competitive type activation) at a concentration of 0.000001x01mol/l Hg2+, but is almost completely deactivated at concentrations above 0.0001 mol/lx01Hg2+. The inhibition of Hg2+ on papain is a competitive and uncompetitive mixed type inhibition
-
0.1 mM: 85.5% decrease of activity
-
1 mM, almost complete inhibition
-
25.27% residual activity at 5 mM
-
0.81% residual activity at 5 mM
-
5 mM completely inhibits
-
inhibitory below 5 mM
-
74.8% residual activity at 10 mM
-
weak
-
0.001-0.05 mM, modifies the recombinant enzyme conformation, and highly reduces the enzyme activity. Hg2+ incubation increases NEP protein levels, but does not change NEP mRNA levels nor the levels of the amyloid intracellular domain peptide, a protein fragment with transcriptional activity. The Hg2+-induced inhibition of the enzyme activity may be mediated by a conformational change resulting in reduced amyloid beta1-42 degradation
-
protease II
-
complete inhibition at 0.05 mM
-
5 mM, 15% inhibition
-
1 mM, complete inhibition
-
1 mM HgCl2, complete inhibition
-
decreases enzyme activity to 50%
-
0.5 mM, complete inhibition
-
52% inhibition at 1 mM
-
complete inhibition at concentrations above 15 mM
-
0.01 mM, 15 min, 82% activity remains
-
complete inhibition at 1 mM
-
complete inhibition
-
2 mM, complete inhibition
-
complete inhibition at the ionic strength of 0.1 mM HgCl, 20-30% activity restored at 20 mM 2-mercaptoethanol
-
1 mM, complete enzyme inhibition
-
0.1 mM
-
0.2 mM, 87% inhibition
-
0.5 mM, complete inhibition of deamination of ATP
-
0.01 mM
-
98.6% inhibition at 2 mM
-
5 mM, reduces activity by 78.8%
-
10 mM, inhibition 39%
-
2-mercaptoethanol partially protects
-
slightly inhibits
-
0.2 mM
-
98% inhibition at 1 mM
-
1-5 mM, strong inhibition
-
strong
-
0.15 mM, 50% inhibition
-
10 mM, complete inhibition
-
0.1 mM, strong inhibition
-
5 mM, in presence of 5 mM Mg2+
-
over 90% inhibition at 1 mM
-
86% inhibition at 1.08 mM, complete inhibition at 10.8 mM
-
81% inhibition with 1 mM Hg2+
-
1 mM, 40% inhibition of fHBP HA B
-
10 mM, in presence of 2.5 mM Mg2+, 30% inhibition
-
complete inhibition at 1 mM
-
leads to complete inhibition at 10 mM
-
1 mM, complete loss of activity
-
reactivity of Co(III) hCBS with HgCl2 is consistent with a loss of the cysteine(thiolate) ligand. 2-Mercaptoethanol is unable to reverse the Hg-induced ligand switch, in contrast to some other heme-thiolate proteins
-
0.1 mM HgCl2, apoenzyme: complete loss of activity, inactive enzyme complex with hydroxocobalamin: 70% loss of activity
-
0.1 mM, 94% inhibition
-
1 mM, complete inactivation
-
94% reduced activity at 1 mM
-
1 mM, strong
-
both enzyme forms IM3796 and IM1634 are completely inhibited by 5 mM Hg2+
-
about 90% residual activity at 5 mM
-
1 mM, no residual activity
-
strongly inhibited (to 50%) by 10 mM Hg2+
1 mM
-
1 mM, 96% inhibition
-
0.2 mM, 99% inhibition
-
complete
-
10 mM, 95% loss of activity
-
10 microM 100% inhibition, 1 microM 67% activity left
-
1 mM, complete inactivation
-
strong inhibition
-
complete inhibition at 1 mM
-
1 mM, complete inhibition
-
complete inhibition, recombinan t enzyme
-
1 mM, about 90% inhibition
-
weak
-
5% residual activity at 1 mM
-
MCM activity is inhibited completely by the addition of 3 mM Hg2+
-
about 45% residual activity at 1 mM
-
inhibits ATPase activity, IC50: 49 nM, targets the cysteine residue in the DECH box, competitive, cysteine or DTT protect at large concentrations
-
10 mM, complete inhibition in presence of 10 mM Mg2+, no activation in absence of Mg2+
-
-
-
-
-
1 mM, 95% inhibition
-
up to 1 mM complete inhibition
-
-
-
-
-
inhibits activation by Mn2+
-
1 mM, 100% inhibition
-
reversed by addition of DTT
-
cytochrome c oxidase activities of strains AP19-3 and ATCC 23270 are completely inhibited by 0.001 mM and 0.005 mM. Strain MON-1 is inhibited 33% by 0.005 mM, and 70% by 0.010 mM
-
0.25 mM, 50% inhibition
-
complete inactivation at 1 mM, buffer-dependend, interaction with alpha-subunit
-

Metals and Ions (265 results)

EC NUMBER
COMMENTARY
LITERATURE
ENZYME 3D STRUCTURE
strong inhibition
-
complete inhibition at 0.1 mM
-
inhibitory
-
induces the enzyme in cut roots treated with HgCl2
-
25% inhibition of activity
-
activates
-
enhances enzyme activity
-
increases NADH-GDH activity substantially, however, specific activity of the enzyme decreases at lower concentration of Hg, and increases to lesser extent at higher concentration of Hg
-
complete inhibition at 1 mM
-
strong inhibition
-
increase of enzyme mRNA expression, via a transcriptional mechanism
-
activation of bilirubin UDP-glucuronyltransferase
-
10 mM, complete inhibition
-
4% activity compared to Mn2+
-
a dose of 1-3 mg/kg increases the basal activity of the enzyme and decreases its induction by dexamethasone
-
requirement of a divalent metal ion, 1 mM, 13% of activity compared to Mg2+
-
increases tyrosine phosphorylation in vivo, genistein decreases the activating effect
-
activates
-
significantly inhibits enzyme activity
-
1 mM, block of essential SH-groups
-
activates
-
decreases activity
-
inhibitory effect
-
low concentrations stimulate the oxidized enzyme form, but not the reduced enzyme form many hundred-fold. Half-maximal stimulation at 0.2 femtoM: Hg2+ stimulates by binding to an enzyme thiol group, thereby stabilizing the oxidized enzyme in an active conformation
-
exposure of newborn rats to mercury increases the hepatic alanine aminotransferase activity by fold and glucose 6-phosphatase activity by 75%. Zinc pre-exposure prevents totally and partially these mercury alterations, respectively. In vitro, HgCl2 inhibits the serum and liver alanine aminotransferase by 22% and 54%, respectively, serum and liver lactate dehydrogenase by 53% and 64%, respectively, and liver and kidney glucose 6-phosphatase from 10- to 13-day-old rats by 53% and 41%, respectively
-
maximal activity at 0.01-1 mM at pH 3.5-5.0
-
complete inhibition
-
deleterious for enzyme activity
-
inhibits activity at 1 mM
-
complete inhibition at 1 mM
-
110.4% relative activity at 2 mM
-
42% residual activity at 1 mM HgCl2
-
activates
2 mM, enzyme retains 25% of its activity
-
454.6% activity at 5 mM
inhibitor
-
activates at 1 mM, complete inhibition at 5-10 mM
-
about 150% activity at 2 mM
-
106.59% activity at 1 mM
-
at 2 mM 0% relative enzyme activity
-
chelating loosely bound Mn2+ and replacing it with a variety of bivalent metal ions including Mg2+, Zn2+, Ni2+, Hg2+, Cu2+, Co2+, Ca2+ and Cd2+ retains its enzymatic activity
-
complete inhibition at 1 mM
-
5 mM, 5.2fold activation
-
activates
-
1 mM, no activity is retained
-
moderate activity
-
1 mM, can replace Ca2+ in activation
isoform Bo4416 shows 143% activity at 5 mM Hg2+
-
0.01 mM, stimulates
-
10 microM 100% inhibition, 1 microM 67% activity left
-
ion inhibits DNA hydrolyzing activity
-
human ferrochelatase is capable of catalyzing the insertion of the inhibitory metal ion Hg2+ into a porphyrin macrocycle
-
1 mM Hg2+ abolishes enzyme function entirely
-
1 mM Hg2+ abolishes enzyme function entirely
-
inhibitory
-
inhibition
-

3D Structure of Enzyme-Ligand-Complex (PDB) (1367 results)

EC NUMBER
ENZYME 3D STRUCTURE

Enzyme Kinetic Parameters

kcat Value (Turnover Number) (16 results)

EC NUMBER
TURNOVER NUMBER [1/S]
TURNOVER NUMBER MAXIMUM [1/S]
COMMENTARY
LITERATURE

KM Value (22 results)

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

Ki Value (23 results)

EC NUMBER
KI VALUE [MM]
KI VALUE MAXIMUM [MM]
COMMENTARY
LITERATURE
0.542
-
pH 6.0, 25°C
0.15
-
immobilized enzyme, at pH 6.8 and 25°C
0.0002
-
noncompetitive inhibition
0.00033
-
-
0.0005
-
pH 7.4, 37°C
0.00038
-
pH 6.8, 25°C
0.57
-
40°C
0.007
-
-
0.11
-
-
0.0446
-
pH 6, 50°C
0.05
-
-
0.55
-
-
0.0005
-
-
20
-
-
0.1
-
-
0.15
-
-

IC50 Value (42 results)

EC NUMBER
IC50 VALUE
IC50 VALUE MAXIMUM
COMMENTARY
LITERATURE
0.00009
-
IC50 0.00009 mM
0.87
-
pH 6.0, 25°C
0.03256
-
immobilized enzyme, at pH 6.8 and 25°C
0.27
-
pH 7.4, 37°C
6.2
-
at 25°C
0.17
-
IC50: 0.17 mM
0.509
-
pH 8.0, 25°C
0.0025
-
noncompetitive with respect to choline, IC50: 0.0004 mM, mixed type inhibition with respect to acetyl-CoA, IC50: 0.0025 mM, activity can be recovered using 2,3-dimercapto-propanol
0.5
-
strongly inhibits the sterol glucosyltransferase activity, IC50 (mM): 0.5
0.000000873
0.00000585
-
0.017
-
IC50: 0.017 mM
0.0348
-
pH 6, 50°C
0.5
-
at pH 6.5 and 25°C
10
-
at pH 5.0 and 40°C
1
-
at pH 4.0 and 37°C
0.67
-
1 mM, complete inhibition, IC50: 0.67 mM
0.000049
-
inhibits ATPase activity, IC50: 49 nM, targets the cysteine residue in the DECH box, competitive, cysteine or DTT protect at large concentrations

References & Links