Ligand urea

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Basic Ligand Information

Molecular Structure
Picture of urea (click for magnification)
Molecular Formula
BRENDA Name
InChIKey
CH4N2O
urea
XSQUKJJJFZCRTK-UHFFFAOYSA-N
Synonyms:
CO(NH2)2


Show all pahtways known for Show all BRENDA pathways known for urea

Roles as Enzyme Ligand

In Vivo Substrate in Enzyme-catalyzed Reactions (7 results)

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

In Vivo Product in Enzyme-catalyzed Reactions (20 results)

EC NUMBER
PROVEN IN VIVO REACTION
REACTION DIAGRAM
LITERATURE
ENZYME 3D STRUCTURE
FMNH2 + O2 = 5,6-dimethylbenzimidazole + D-erythrose 4-phosphate + urea + ?
show the reaction diagram
-
-
biuret + H2O = urea + CO2 + NH3
show the reaction diagram
-
-
ureidomalonic acid + H2O = malonate + urea
show the reaction diagram
-
-
agmatine + H2O = putrescine + urea
show the reaction diagram
-
-
N-amidino-L-aspartic acid = L-aspartic acid + urea
show the reaction diagram
-
-
methylguanidine + H2O = methylamine + urea
show the reaction diagram
-
-
guanidinoacetate + H2O = glycine + urea
show the reaction diagram
-
-
1,4-diguanidinobutane + H2O = agmatine + urea
show the reaction diagram
-
guanidinoproclavaminic acid + H2O = proclavaminic acid + urea
show the reaction diagram
-
-
N1-aminopropylagmatine + H2O = spermidine + urea
show the reaction diagram
-
-
creatine + H2O = sarcosine + urea
show the reaction diagram
-
-
cyanamide + H2O = urea
show the reaction diagram
-
-

Substrate in Enzyme-catalyzed Reactions (20 results)

EC NUMBER
REACTION
REACTION DIAGRAM
LITERATURE
ENZYME 3D STRUCTURE
urea + H2O = ? + NH3
show the reaction diagram
-
urea + H2O = ?
show the reaction diagram
-
(-)-ureidoglycolate + urea = allantoate + H2O
show the reaction diagram
-

Product in Enzyme-catalyzed Reactions (82 results)

EC NUMBER
REACTION
REACTION DIAGRAM
LITERATURE
ENZYME 3D STRUCTURE
FMNH2 + O2 = 5,6-dimethylbenzimidazole + D-erythrose 4-phosphate + urea + ?
show the reaction diagram
-
-
biuret + H2O = urea + CO2 + NH3
show the reaction diagram
-
-
ureidomalonic acid + H2O = malonate + urea
show the reaction diagram
-
-
barbiturate + H2O = malonate + urea
show the reaction diagram
-
agmatine + H2O = putrescine + urea
show the reaction diagram
-
cyanamide + H2O = urea
show the reaction diagram
-
cyanamide + H2O = urea
show the reaction diagram
-

Activator in Enzyme-catalyzed Reactions (85 results)

EC NUMBER
COMMENTARY
LITERATURE
ENZYME 3D STRUCTURE
130% relative activity at 1 M
-
9% activation at 0.1%
-
slight activation
-
physiological concentration, 8% activation free protein
-
the enzyme is activated at low concentrations of urea
-
2.0-2.5 M, rapid and reversible activation at low concentrations and brief periods of exposure, inactivation at higher concentrations and longer periods of exposure; both activates and denatures the enzyme, rapid and reversible activation at 2.0-2.5 M urea
-
increase of activity by 250% in presence of 1 M urea with no apparent perturbation in enzyme structure. Presence of urea prohibits the closing of the active site thus allowing the substrate to bind
-
activity in 1, 2, and 3 M urea is about 1.75-, 2-, and 1.5-fold higher than in the absence of urea, respectively
-
recombinant enzyme relative activity is greatest in liquid assays in 1 M urea
-
activates
-
enhances activity of TCH4 protein
-
2 mM, activates
-
enhances activity together with dithiothreitol
-
stimulates at low concentration, inhibits at high concentration, 4 M
-
up to 1 M, 60% increase in activity
-
at concentrations lower than 0.8 M
-
2 M, stimulation
-
urea enhances the activity 47% more than the original activity at 5 mM
-
112% activity at 1 mM
-
5 mM, 119% of initial activity
-
1.0-5.0 mM, 1.1fold activation
-
118% activity at 10 mM
-
110.38% activity at 5 mM
-
122.7% activity at 5 mM
-
low concentrations stimulate
-
stimulates
-
23% activation at 1 M
-
addition of urea (1-4 M) greatly improves enterokinase cleavage specificity at the canonical site and reduces adventitious cleavage
-
slight activation at 1-4 M
-
enhances hydrolysis of azocasein
-
at 5 M and 8-9 M
-
activity decreases in the presence of 4 M urea and reaches the activity of the control again at 8 M when using casein as a substrate
-
3fold activation at 6 M, probably due to unfolding of the substrate azocasein, which enhances the enzymes sensitivity for proteolytic cleavage
-
3 M, enhances activity
-
stimulates
-
optimal concentration: 4-5 M, inclusion bodies from Escherichia coli as substrate
-
19% increase of activity at 1% (w/v)
-
8 M urea, 30 mM Phosphate buffer, pH 7.4, 100% activation
-
R97Q mutant, at low urea concentration, sharp activation with maximum, about 50% activation at 3 M urea, followed by rapid inactivation: 6 M: 80% inhibition, 8 M: 100% inhibition
-
0.2-0.5 M, increases activity
-
strong inducer of cyanase activity
-
up to 1 M of urea
-

Inhibitor in Enzyme-catalyzed Reactions (398 results)

EC NUMBER
COMMENTARY
LITERATURE
ENZYME 3D STRUCTURE
FabG is fully unfolded at 6 M, approximately 90% of the enzyme activity can be recovered on dialyzing the denaturant. Two states in the reversible unfolding process of FabG in presence of NADPH, one is an activity-enhanced state and the other, an inactive state in case of equilibrium unfolding with urea
-
at pH 9.9
-
inactive at 3 M but regains activity after dialysis
-
strong inhibition
-
2.2 mM, 50% inhibition, reversible
-
enzyme activity and electrophoretic pattern of LDH-A4 and malate dehydrogenase, EC 1.1.1.37, compared in relation to heat and urea inactivation, LDH is more sensitive than MDH, overview
-
40% (v/v), 85% activity
-
enzyme activity and electrophoretic pattern of MDH and lactate dehydrogenase, EC 1.1.1.27, compared in relation to heat and urea inactivation, LDH is more sensitive than MDH, overview
-
denaturation, in 3-5 M urea, the enzyme undergoes a reversible tetramer-dimer-monomer quaternary structural change in an acidic pH environment, which resulted in a molten globule state that is prone to aggregate, Mn2+ protects, overview
-
inactivation at 3-5 M urea, the pigeon cytosolic NADP+-dependent malic enzyme unfolds and aggregates into various forms with dimers as the basic unit, under the same denaturing conditions but in the presence of 4 mM Mn2+, the enzyme exists exclusively as a molten globule dimer in solution, overview
-
low molecular weight form
-
inhibition in vitro and in vivo at sublethal concentration of 0.02-0.05 mM, IC50: 0.0238 mM
-
oxidized truncated enzyme
-
1 M, 5.8% residual activity
-
6 M, at 30°C for 1-2 h: partial inactivation, urea + KBr: complete inactivation
-
urea causes a dose-dependent but reversible inhibition by dissoziation of the hetero-oligomeric enzyme comparable with the effect of heat-treatment, 3.5 M urea reduces GDH activity by 20%, 5 M urea by 80% and 8 M urea by ca. 90%
-
effect on various molecular forms
-
1% w/v, 85% residual activity
-
50% inhibition at 4 M in 3.5 min
-
at 10 mM inhibitory, hydrogen production
-
1 M, 3% inhibition. 3 M, 42% inhibition. 5 M, 56% inhibition
-
causes isothermal unfolding of mutant C69S in a three-state mechanism, thermodynamic analysis, overview; nonlinear decrease of activity, activity lost at about 5 M, three-state unfolding of mutant enzyme
-
1-4 M
-
86% inhibition at 4 M
-
at 5.0 M urea, the half-time of the enzyme is 45 min, at 6.0 M urea 8 min, and at 7.5 M urea, the enzyme is inactivated within 1 min. r´Reversible, non-competitive inhibition of the luciferase activity occurs at concentrations up to 1.5 M
-
70% loss of activity at 1 M
-
70-80% inhibition at 2 M
-
denaturation curve, thermodynamics, wild-type and mutants, overview
-
2.0 mM, complete inhibition
-
1 M urea reduces activity by 20%, 2 M urea by 40%, and 3 M urea by 80%, concentrations over 5 M urea eliminate activity
-
immediate inhibition, repression of induction
-
500 mM, 44% inhibition
-
no activity at 2.5 M
-
no modification with 8 M urea
-
3.5 M, complete and irreversible inactivation
-
30% inhibition at 50 mM
-
about 50% inhibition of isoform LAAOII and about 20% inhibition of isoform LAAOI at 5 mM
-
both activates and denatures the enzyme, reversible inactivation above 2.5 M, half-time of inactivation is 46 min at 2 M and 37°C
-
at 4 M, 38% inhibition and at 7.2 M, 93% inhibition
-
4 M, 60% inhibition
-
50% inhibition at 6 mM
-
1 mM urea has no significant effect on activity whereas 50% enzyme inhibition is observed at 750 mM, enzyme after treatment with urea below 500 mM regains about 95% activity
-
activation: 0.4-0.6 M, inactivation at higher concentration
-
1 mM, 80% residual activity
-
1 mM, 80% residual activity
-
2.5 M, almost complete inhibition
-
denaturation of holo-transketolase by urea displays at least three transitions, where only the final equilibrium denaturation transition is the same for both apo-transketolase and holo-transketolase. Enzyme is deactivated initially by changes in structure associated with the cofactors, but this event does not release the cofactor from the enzyme. Holo-transketolase does not denature to apo-transketolase at 2 M urea. Complete dissociation of cofactors from holo-transketolase at 3.8 M urea without formation of the compact form of apo-transketolase (intermediate form). Holo-transketolase and apo-transketolase at 7.2 M urea both show a common denatured form
-
about 50% inhibition at 1 M, complete inactivation at 4 M
-
inactivation at 8 mM
-
complete inactivation of wild-type and mutant at 6 M, low activity at 4 M
-
irreversible inactivation of recombinant wild-type at 9.3 M and of recombinant mutant G196V at 5 M, at up to 8 M activation of the wild-type
-
10 mM, 15% inhibition; 85% inhibition
-
50% inhibition at 0.4 M, complete inhibition at 2 M. Up to 2 M, reversible inhibition
-
inhibition at high concentration, 4 M, stimulation at low concentration
-
0.9 M, 50% inhibition
-
loss of 81% activity at 2 M, 50% at 1 M
-
8 M, 20% inhibition
-
6 M, complete inactivation
-
plus dithiothreitol and IAA
-
urea-induced unfolding of thymidylate kinase is noncooperative and influences the functional properties of the enzyme much less than their Cm values. Complete inhibition at 1.0 M
-
0.9 M, 50% inhibition
-
50% inhibition of wild-type enzyme at 0.75 M, 50% inhibition of H92N mutant enzyme at 0.35 M, 50% inhibition of H92Q mutant enzyme at 0.2 M
-
the enzymatic activity of isoform FADS2 decreases dramatically at increasing urea concentration, with a mid-point for activity loss at 2.1 m urea
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5 mM, 16% loss of activity (recombinant enzyme expressed in Sulfolobus solfataricus). 5 mM, 17% loss of activity (recombinant enzyme expressed in Escherichia coli as thioredoxin-free form (EcSisEstA I)). 5 mM, 10% loss of activity (recombinant enzyme expressed in Escherichia coli as a thioredoxin-EstA fusion protein (EcSisEstA II))
-
strong inhibition
-
the stability of the immobilized recombinant enzyme is 2.7fold increased compared to the soluble recombinant enzyme
-
7.0 M, inactivation
-
10 mM, 15% loss of activity
-
20% inhibition at 4 M
-
40% of maximal activity with single-stranded DNA with 6.6 M
-
slight inhibition
-
in vivo: activity decreases in vivo (mIMCD-3 cell), measuring choline by chemiluminescence, substrate sn-glycero-3-phosphocholine. in vitro: no directl inhibition of GDPD5 activity, GPC-PDE in vitro activity is reduced by over 60% in immuno-precipitates from HEK293 cells exposed to high urea concentration.
-
88% residual activity in the presence of 8 M urea, after 60 min at 70°C
-
1 M, 74% inhibition
-
2 mM, 57% of initial activtiy
-
90.4% residual activity at 10 mM
-
0.1 M, 55% inhibition
-
20% loss of activity at 8 M
-
isoform Ag-II shows 92% residual activity at 5 mM urea
-
10 mM, 6% inhibition
-
1%, 38% inhibition
-
100% inhibition at 3 M
-
relative activity in presence of 2 M 32%
-
84.86% residual activity at 1 M
-
10 mM, 85% residual activity
-
14.5% residual activity at 7 mM
-
about 70% residual activity at 100 mM
-
85.86% residual activity at 10 mM
-
competitive
-
completely inactive in presence of 6 M urea
-
2.0 M
-
sensitive to very low concentrations of urea
-
weak
-
12% residual activity in the presence of 4 mM urea
-
high concentrations (6 M) of urea significantly decrease the enzyme activity by over 60%, most likely due to disrupting the enzyme structural integrity
-
slight inhibition
-
5 mM, 50% loss of activity in absence of CaCl2
-
inactivated at 3 M
-
the reversible unfolding/refolding process of the PLpro in the presence of urea is investigated. The zinc-binding domain of the enzyme starts to unfold at urea concentration below 0.35 M and reaches a first plateau at 1-3.5 M. At this stage, the palm and thumb core domains remain well folded but totally inactive
-
at 2.4 M urea the activity decreases continuously to 50% when using N-alpha-benzoyl-DL-arginine-2-naphthylamide as a substrate
-
70% inhibition at 5 M
-
2 M reduces cleavage to 95%, 3 M reduces cleavage to 5%
-
isoform NepI shows about 85% residual activity at 4 M and is completely inhibited at 6 M urea
-
95.5% residual activity at 5 mM
-
50 mM, 72% residual activity
-
5 M, not at 2 M
-
complete inhibition at 8 M
-
inhibits 95.7% at 8 M, no inhibition at 4 M
-
0.5 M
-
6 M, irreversible inactivation
-
95% loss of activity in 2.25 M
-
moderate inhibition
-
inhibition kinetics and effects on enzyme structure, overview
-
competitive
80% inhibition at 2 M
-
slight inhibition, 10 mM: 10% inhibition
-
competitive inhibition
-
5% and 20% activity loss with 2 M and 5 M urea pre-treatment for 10 min at 30°C
-
0.2-1 M
-
8 M, both isoenzymes
-
above 2 M, reversible inactivation
-
weak
-
deactivation by denaturation of the protein
-
79% inhibitin at 4 M, 93% at 8 M
-
8 M, denaturates
-
about 100% inhibition at concentration of 4 mM
-
4 mM: inactivation
-
partial inactivation
-
20% activity remains at 3 M urea, and no activity is detected in 6 M urea
-
the beta-elimination activity of the enzyme complex decrease less sharply than the beta-replacement activity with increasing concentration in absence of NaCl, 0.1 M NaCl alters the effect of urea concentration
-
13.9% inhibition at 1 mM
-
1 mM, 22% inhibition
-
1 mM, 86% of initial activity
-
complete inhibition at a concentration of 1 M in triethanolamine hdrochloride buffer, folate and pteroylpolyglutamates protect
-
above 1 mM
-
competitive
-
addition of 1 M urea reduces activity to 58%
-
98% loss of activity at 10 mM
-
mechanism of inhibition, urea inhibits ribonuclease A competitively over a concentration range from 100 mM to 4.0 M, urea with its high dipolar moment is a competitive inhibitor and a very high concentration (more than 4.0 M) of it could denature the enzyme, beginning the interaction with the protein at the active center
-
50% inhibition at 2 M, 10% at 1 M
-
8 M, completely and irreversibly inactivates
-
4 M
-
90% inhibition at 2 M, 1% inhibition of aggregated enzyme
-
inhibitory effect to W203A/W205A/W206A mutant
-
denaturation at 3.3 M, the Zn2+-depleted enzyme is much more sensitive to denaturation by urea than the native enzyme
-
the Thermus aquaticus enzyme loses activity at 4-5.5 M urea, but it regains activity with increasing concentrations of urea, reaching 70% of its original activity in 8.5 M urea
-
physiological concentrations of urea inhibit, at least when ATP and/or glutamate are nonsaturating. Inhibition is partially reversed by trimethylamine-N-oxide
-
competitive to nicotinate mononucleotide
-
20% inhibition with 100 mM, 50% inhibition with 250 mM, 90% inhibition with 800 mM
-

Metals and Ions (5 results)

EC NUMBER
COMMENTARY
LITERATURE
ENZYME 3D STRUCTURE
activates both isozymes TAH I and TAH II
-
132% relative activity at 8 mM urea for salivary gland alpha-amylase
-
the enzyme activity is significantly promoted at 1 mM urea
-
stimulates hydrolysis of serum albumin in a dose-dependent manner, caused primarily by denaturation of the protein substrate
-
activates
-

3D Structure of Enzyme-Ligand-Complex (PDB) (34 results)

Enzyme Kinetic Parameters

kcat Value (Turnover Number) (26 results)

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

KM Value (112 results)

EC NUMBER
KM VALUE [MM]
KM VALUE MAXIMUM [MM]
COMMENTARY
LITERATURE
1.88
-
pH 7.5, 30°C; pH 8.0, 40°C

Ki Value (16 results)

EC NUMBER
KI VALUE [MM]
KI VALUE MAXIMUM [MM]
COMMENTARY
LITERATURE
TABLE ID
0.00186
-
-
533
2
-
-
19423
2000
-
-
20781
5
-
pH 9.0, 30°C, wild-type enzyme
21640
4.6
-
pH 8.0, 25°C
22145
4.6
-
pH 8.0, 25°C
22334
500
-
-
30954
1050
-
at pH 7.4 and 25°C
32363
2700
-
-
34403

IC50 Value (13 results)

EC NUMBER
IC50 VALUE
IC50 VALUE MAXIMUM
COMMENTARY
LITERATURE
0.0238
-
inhibition in vitro and in vivo at sublethal concentration of 0.02-0.05 mM, IC50: 0.0238 mM
2250
-
pH 4.0, 65°C
600
-
pH 7.4, 37°C

References & Links