Ligand guanidinium chloride

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Basic Ligand Information

Molecular Structure
Picture of guanidinium chloride (click for magnification)
Molecular Formula
BRENDA Name
InChIKey
CH6ClN3
guanidinium chloride
PJJJBBJSCAKJQF-UHFFFAOYSA-N
Synonyms:
GdnHCl, Gu-HCl, Guanidine-HCl, guanidine/HCl, Guanidine chloride, Guanidine HCl, guanidine hydrochloride, guanidinium-HCl, guanidinium hydrochloride, GuHCl

Roles as Enzyme Ligand

Activator in Enzyme-catalyzed Reactions (18 results)

EC NUMBER
COMMENTARY
LITERATURE
ENZYME 3D STRUCTURE
activates at low concentrations, at higher concentrations concomitant loss of activity with a multi-state pathway of denaturation
-
activates
-
500 mM, activation at low concentrations and brief periods of exposure, inactivation at higher concentrations and longer periods of exposure
-
recombinant enzyme, 2.5fold activation at 0.5 M
-
4°C: activates the enzyme 2.5fold at 0.2 M
-
activation of recombinant wild-type 1.6fold at 0.5 M, inactivation at 1.6 M
-
enhances activity together with dithiothreitol, cysteine, 2-mercaptoethanol or sulfite
-
5 mM, 20% activation of guanosine 5'-tetraphosphate synthesis
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at low concentrations
-
1 M, 1156% increase in activity
-
0.1 mM, 1.1fold activation
-
90% activation at 4 M
-
at 2 mM
-
activates at low concentrations but inhibits above 2 M
-
stimulating, dual effector as cation activator and as a modulator of the active site conformation by alteration of the equilibrium distribution of pyridoxal 5'-phosphate intermediates formed in reaction with the beta-subunit, effects on reaction are highly dependent on the substrate, effects are altered by NaCl
-

Inhibitor in Enzyme-catalyzed Reactions (172 results)

EC NUMBER
COMMENTARY
LITERATURE
ENZYME 3D STRUCTURE
FabG is fully unfolded at 4 M, approximately 90% of the enzyme activity can be recovered on dialyzing the denaturant. In presence of NADPH, there is no stabilization of FabG in case of equilibrium unfolding with guanidinium chloride
-
rapid inactivation at 4 M
-
in the presence of 4 M guanidine hydrochloride enzyme structure is unfolded with complete loss of enzyme activity
-
1 M, 1.5% residual activity
-
84.2% residual activity at 3 mM
-
at 10 mM inhibitory, hydrogen production
-
almost linear decrease of activity up to 1 M where activity vanishes, three-state unfolding of mutant enzyme; causes isothermal unfolding of mutant C69S in a three-state mechanism, thermodynamic analysis, overview
-
70-80% inhibition at 0.1 M
-
no activity at guanidine hydrochloride concentrations exceeding 0.6 M
-
2.0 mM, 95% inhibition
-
recombinant wild-type rCtFtn and mutant A19Y are stable at up to 2 M GdnHCl. At 2.5 M GdnHCl both proteins start to loose structural stability
-
87.3% residual activity at 0.1 mM
-
0.1 M guanidine hydrochloride reduces activity by 30%, 0.2 M guanidine hydrochloride by 60%, and 0.4 M guanidine hydrochloride by 85%, concentrations over 0.7 M guanidine hydrochloride eliminate activity
-
unfolding of both wild type and mutant dN-GAPDS proteins is described by a single [GdnHCl]50 value. For the truncated mutant dN-GAPDS, it constitutes 1.83 M. Different mutations of dN-GAPDS alter this parameter to various extents. The most pronounced effect is observed in the case of mutants P111A, P157A, and D311N. The mutation P111A increases the value of [GdnHCl]50 by 0.43 M, the mutations P157A and D311N decrease the GdnHCl50 value by 0.36 and 0.48 M, respectively. In other mutants, the [GdnHCl]50 value is less affected or does not change, overview; unfolding of muscle isoenzyme GAPD is a two step process
-
10% (v/v), 42% inhibition
-
an exponential decrease in enzymatic activity from 100% to 20% is observed between 0 and 0.05 M, no activity is observed above 0.5 M
-
reversible inactivation at 1 M, pH 7.0, kinetics, overview
-
72°C, almost complete loss of activity by addition of more than 3 M
-
complete loss of activity
-
enzyme unfolding at 1 M, 0.5 M is not enough for proper unfolding. The fusion protein forms visible aggregates due to unfolding of MBP
-
25% inhibition at 2 mM, 30% inhibition at 3 mM
-
4°C: 50% inactivation at 1.0 M, complete inactivation at 1.6 M, reversible
-
destroys zinc finger thiols of DnaJ protein
-
86% loss of activity at 0.25 M
-
Co2+ protects
-
800 mM, almost complete inhibition
-
50% inhibition at 0.3 M, complete inhibition at 0.7-1 M
-
irreversible inactivation of recombinant wild-type at 1.6 M and of recombinant mutant G196V at 0.2 M, at 0.5 M activation of the wild-type
-
study on kinetics of inactivation and aggregation at 0.7 M guanidine hydrochloride. Osmolytes trimethylamine-N-oxide and betaine exhibit the highest protective efficacy against phosphorylase b inactivation
-
10 mM, 63% inhibition; 37% inhibition
-
only recombinant enzyme
-
50% loss of activity at 1.04 M, only little residual activity between 2 and 6 M
-
0.25 M, 50% inhibition
-
loss of 86% activity at 0.3M GdmCl, 50% at 0.2 M
-
85% residual activity at 1 M guanidine hydrochloride
-
0.5 M, 30% loss of activity for the mutant P204H, 5% loss of activity for the wild-type, both are unfolded at 1 M
-
5 mM, 50% inhibition of polyphosphate synthesis
-
guanidine hydrochloride-induced unfolding of thymidylate kinase is noncooperative and influences the functional properties of the enzyme much less than their Cm values. Complete inhibition at 0.4 M
-
0.25 M, 50% inhibitioin
-
inhibitory at 0.2 M, 40% inhibition at 0.4 M, 65% inhibition at 0.5 M
-
3.5-4.0 M, inactivation
-
full-length enzyme retains most of its activity at guanidine hydrochloride concentrations below 0.5 M, whereas an abrupt decrease of the activity of p54 and p46 is found when guanidine hydrochloride concentration is increased
-
below 1 M, inactivation occurs without loss of the secondary structure
-
over 80% inhibition at 0.5 M
-
inactivation of the enzyme by GuHCl (guanidine hydrochloride) is a slow, reversible reaction with fractional remaining activity. The microscopic rate constants are determined. The enzyme is protected by the substrate to a certain extent during guanidine denaturation. The changes of conformation of the enzyme in different concentrations of GuHCl are studied. The inactivation occurs before the noticeable conformational changes of the enzyme molecule as a whole can be detected, which suggests that the active site of the enzyme has more flexibility than the whole enzyme molecule
-
denaturation
-
1 mM, 69.5% of initial activity, mutant H260L
-
0.05 to 0.6 mM, as the concentraion is increased, the loss of of the whole conformational structure occurs and the relative activity decreases from 80% at 0.05 mM to 29% at 0.6 mM compared to the control, pH 8.0, 100°C
-
the enzyme loses 54% and 70% of the original activity in 0.5 M and 1.0 M guanidinium hydrochloride, respectively. Irreversible denaturation at higher concentration of 6 M of guanidinium hydrochloride, kinetics, overview. The protein almost completely unfolds in 4.0 M guanidinium hydrochloride
-
2 M, 32% residual activity
-
inhibition of both enzyme variants at 1 M, 30°C, 1 h
-
0.6 M, 30% inhibition
-
50% inhibition at 3 M
-
3 M, activity completely lost
-
20.5% residual activity at 1 mM
-
84% inhibition at 2 M
-
hexameric LAP is almost completely inactivated, showing 0.6% residual activity, by incubation with 2.5 M GuHCl and 40 mM DTT for 3 h at room temperature
-
reversible, significantly decreases the Km-value of substrate hydrolysis, without changing the maximal velocity
-
1% residual activity in the presence of 4 mM guanidine hydrochloride
-
competitive
-
0.1 M, 20 min, 72% loss of activity
-
6 M guanidinium hydrochloride gives a 40% reduction of activity after 1 h of incubation at 40°C
-
5 mM, 65% loss of activity in absence of CaCl2, activation in presence of 1 mM CaCl2
-
complete loss of activity at 6 M guanidine-HCl
-
activates at low concentrations but inhibits above 2 M
-
500 mM reduces cleavage to 60%, 1 M reduces cleavage to 0%
-
50 mM, 40% residual activity
-
2 M and above, not at 1 M
-
competitive inhibitor
-
enhanced by EDTA
-
22% inhibition at 1 mM
-
0.5 M
-
3.4 M, complete inhibition
-
0.5 M: 50% inhibition, 1 M: 100% inhibition
-
kinetics of GuHCl-induced denaturation of the two dUTPase isozymes at pH 7.5, 4 °C and 1.5-4 M
-
85% inhibition at 4.2 M, complete recovery of activity after dialysis
-
approx. 50% uncompetitive inhibition above 0.5 mM
-
deactivation by denaturation of the protein
-
6 M, denaturates
-
strong inhibition, unfolding within 1 h
-
at concentrations lower than 1 M, activity is gradually decreased suggesting the existence of the native tetrameric form with denaturation intermediates such as dimeric and monomeric forms of the enzyme. At higher concentrations above 1 M, the enzyme completely lost the activity, suggesting that the enzyme structure is completely denatured
-
complete inhibition at 1 M
-
complete inhibition at 1 M, 51% inhibition of aggregated enzyme
-
20% inhibition with 150 mM guanidinium chloride in the presence of 100 mM KCl, 80% inhibition with 1 mM KCl
-
at 0.8 M guanidine hydrochloride, the enzyme forms a molten globule like intermediate, which is enzymatically inactive
-
inactivation at 0.5 M
-
5 min at 100°C, 8000 mM, significant reduction in the activity
-

Metals and Ions (1 result)

EC NUMBER
COMMENTARY
LITERATURE
ENZYME 3D STRUCTURE
the single mutant R308A changes to a trimeric and kinetically cooperative form, whereas the other enzyme variants are not altered
-

Enzyme Kinetic Parameters

Ki Value (5 results)

EC NUMBER
KI VALUE [MM]
KI VALUE MAXIMUM [MM]
COMMENTARY
LITERATURE
0.0075
-
-
1000
-
pH 7.5, 25°C

IC50 Value (14 results)

EC NUMBER
IC50 VALUE
IC50 VALUE MAXIMUM
COMMENTARY
LITERATURE
155
-
pH 7.4, 37°C
440
-
-

References & Links

Links to other databases for guanidinium chloride

ChEBI
PubChem
ChEBI
PubChem