activation, used as nonfermentable carbon source in wild type and tpa1 mutant cell cultures, greater activity compared to activity in glucose-grown cells

285693

1.1.2.8

does not affect the adhS gene expression but induces PQQ-ADH activity

725154

1.1.3.5

100 mM, 1.5fold increase in activity

ethanol does not affect the adhS gene expression but induces PQQ-ADH activity

activation

stimulation

10% v/v, 2fold activation

15%, 1.7fold activation. Strong decrease in activity above 15%

7423

1.14.18.1

activity is enhanced in the presence of 10-50% (v/v)

presence of ethanol enhances the hydroxylation by resting non-induced cells

438299

1.17.1.9

increases maximal reaction rate

30% v/v, 5fold activation

287938, 287968

1.2.1.4

0.5-2% increases activity in crude extracts

655889

1.2.1.5

0.05 mM, 1.8fold stimulation

735898

1.2.4.2

a 3fold increase in the protein content of the E1o component 2-oxoglutarate dehydrogenase complex is observed in liver mitochondria of rats exposed to ethanol

1 M, increases activity by about 10%

12570

1.4.1.4

activates up to 40% v/v

391642

1.4.3.7

2fold activation in the presence of ethanol

activation, 12% v/v

enhances the inducing and protecting effects of betaine on the enzyme, alone has only a slightly activating effect on the enzyme activity, overview

activation, 1-10% v/v

increases activity

addition of 14% leads to 2fold increase of enzyme activity

486132

2.3.1.20

highest activity when diacylglycerol is in ethanol

486485

2.3.1.23

integral membrane enzyme, 2% (v/v), 30% increase in activity

5fold activation at 10% v/v

487764

2.3.2.13

enzyme activity is slightly elevated at a lower concentration of ethanol at 25°C. With increasing ethanol concentration, the enzyme activity decreases, and in the presence of 50% ethanol the enzyme activity is almost lost after incubation for 30 min at 25°C

686843

2.4.1.1

strong activation of enzyme in hepatocytes

659579

2.4.1.10

ethanol increases the fructooligosaccharide biosynthesis activity of levansucrase, fructooligosaccharide production at different temperatures in the presence of ethanol, inverse relationship between temperature and ratio synthetic activity/total activity of levansucrase, overview

736130

2.4.1.173

increase of activity at 7-20%

stress treatment induces higher levels of OGT protein expression

659361

2.6.1.1

binge ethanol treatment causes significant increase in blood plasma AST activity

activates

little activity unless activated either by a complex of 70S ribosomes, mRNA and uncharged tRNA or by a solvent like ethanol at approximately 20%

activates 1.5fold at 5% v/v

ethanol increases the enzyme activity to 136%

729689

3.1.1.59

activates even at higher concentrations

651510

3.1.1.75

10% (v/v): 100% activity compared to no addition

activation

80% ethanol, activation of both isoenzymes, conversion of isoenzyme H-1 to a 35500 Da form and isoenzyme H-2 to a 67000 Da form and a 35500 Da form

94685

3.1.3.5

livers from wild type mice treated with ethanol (2 g/kg of 20% ethanol) release 2-3fold higher levels of adenosine than livers from comparably treated CD73KO mice

15% increase of activity at 50% (v/v) ethanol, at 30°C

1% v/v ethanol: slight activation

135707

3.2.1.104

64% stimulation at a concentration of 20%, hydrolysis of cholesteryl beta-D-glucoside. 65% stimulation at a concentration of 20%, hydrolysis of p-nitrophenyl beta-D-glucoside

208428

3.2.1.133

enzyme activity increases to 113% in the presence of 10% (v/v) ethanol

707248

3.2.1.14

about 127% activity at 25% (v/v)

13% activation at 10% w/v

transglycosylation, activation

171731

3.2.1.B26

the liberation of aglycone from aryl beta-D-glucosides is stimulated by alcohols in a manner suggesting specific interaction between alcohol and enzyme

alcohol modifies the protein microenvironment, leading to a more flexible enzyme structure, which is probably responsible for the enhanced enzymatic activity

2.7 M, stimulates

116% activity in the presence of 1 mM

25% v/v, 6fold increase of the activity, methoxycarbonyl-D-Nle-Gly-Arg-p-nitroanilide as substrate, rFIXa, alcohols modify the conformation of FIXa rendering the active-site cleft more easily accessible to tripeptide substrates with a hydrophobic residue in the P3-position

activation e.g. between 2.5-12%, v/v, depending on substrate

209259

3.6.1.27

slight activation at concentration of 4 M

210607

3.6.5.3

stimulation by aliphatic alcohols in a decreasing order of effectiveness: ethylene glycol > 2-propanol > ethanol > glycerol > methanol > 1-propanol

activates

10% w/v, increases activity by 24%

all PLC1-6 are activated in salt/ethanol extractions

708374

5.4.99.17

1.6fold increase of activity when added to the enzyme test system at a concentration of 6%

stimulates

slight stimulation at low tRNA concentrations

114

6.3.2.2

feeding in vivo increases the enzyme expression, treatment of hepatocytes induces the expression of only the heavy enzyme subunit

Inhibitor in Enzyme-catalyzed Reactions (264 results)

10 mM, more than 90% inhibition

40% (v/v), 30% activity

639106

1.1.1.360

20% (v/v), 20% loss of activity

668544

1.1.1.4

3.7% residual activity at 10% (v/v)

739127

1.1.1.47

19% residual activity at 50% (v/v)

10% v/v: 25-75% loss of activity, depending on substrate, enzyme regains activity after removal of alcohol

3.6% residual activity at 80% (v/v)

741032

1.1.99.28

16% inhibition at 2 M, 48% inhibition at 4.7 M

substrate inhibition

the native enzyme shows less than 5% residual activity in the presence of ethanol

5% v/v, 50% inhibition, complete loss of activity at 20% v/v

5%, 10% inhibition

45% inhibition at 10% concentration as co-solvent

675467

1.14.15.4

10%, v/v, complete inhibition of hydroxylation

285390

1.14.18.1

50% ethanol, 56% inhibition

depression

complete inhibition at 40% (v/v)

IC50 of 4.8 vol%

competitive inhibition

substrate n-butanol

43% inhibition when 0.04 ml are added to reaction mixture

486495

2.3.1.23

integral membrane enzyme, 10%, 20% inhibition

irreversible at 2% v/v

487085

2.3.1.58

precipitation with ethanol completely inhibits enzyme activity

at 4% inhibits

substrate inhibition above 0.5 M

735557

2.4.1.10

complete inhibition at 1.6 M

488314

2.4.1.11

traces inactivate the enzyme

488424

2.4.1.15

10% (v/v), 28% inhibition; 72% inhibition

727099

2.4.1.17

50% inhibition of isozyme UGT2B17 at 1%

658524

2.4.1.18

about 57.2% decreased enzyme activity, 10%

15%, about 3 M, about 50% inhibition of product formation

20% v/v, 4% inhibition

675468

2.4.1.245

5 mM, 47% loss of activity

20% v/v, 42% inhibition

675468

2.5.1.18

inhibits the mu- and pi-class GST activities in vivo by 53% and 13%, respectively, in hepatocytes and the culture medium, the enzyme activity is increased in the cell medium, overview, the inhibitory effect is completely oe partially reversible by vitamin E or 4-methylpyrazole, respectively

673913

2.5.1.6

25 mM ethanol substantially decreases the enzymatic activity of MAT II

0.5%, 20% inhibition

dose-dependent inhibition of insulin receptor substrate-1-associated PI3K activity in skeletal muscle, but not in adipose tissue, ethanol-induced diabetic rats

707910

2.7.1.165

10% v/v, less than 65% inhibition; less than 65% activity in the presence of 10% (v/v)

0.03%, inhibition of PKCgamma oscillation at 0.1 mM

662219

2.7.11.20

decreases phosphorylation of eEF2K, whereas elongation factor 2 phosphorylation increases, but this response is not mediated by eEF2K

concentrations above 0.005 ml/0.2 ml assay

10 mM, 20% inhibition

6%, 85% inhibition

inhibits the enzyme, LPL activity is reduced by 23-25% 2-4 hours after the administration of alcohol, respectively, with respect to controls, in vivo or in post-heparin plasma. The concentrations of inhibitors ANGPTL3 and ANGPTL4 drops to 67% and 86% of baseline values, respectively, at 280 min after alcohol consumption. The acute effects of alcohol consumption, especially on postprandial lipemia, seem to be accentuated in hypertriglyceridemic subjects

product inhibition

97% inhibition at 75% v/v

80-90% inhibition

reversible noncompetitive

inhibition of PAP-1

23% and 28% inhibition at 0.5% and 1% (v/v) ethanol, respectively

at a concentration above 2%

astrocyte treatment with ethanol inhibits the activity of arylsulfatase B, and triggers the degradation of chondroitin-4-sulfate, increases total sulfated glycosaminoglycans, chondroitin-4-sulfate and neurocan core-protein content and inhibits neurite outgrowth in neurons cocultured with ethanol-treated astrocytes in vitro. Ethanol also inhibits arylsulfatase B activity and increases sulfated glycosaminoglycans and neurocan levels in the developing hippocampus after in vivo ethanol exposure

729806

3.1.6.8

decreases ASA activity levels in the liver, but not in the cerebral cortex and kidney

10% ethanol: inactivation

135707

3.2.1.104

39% inhibition at a concentration of 50%, hydrolysis of p-nitrophenyl beta-D-glucoside

208428

3.2.1.116

20% (v/v), 2 h, 20°C, 39% loss of activity

749724

3.2.1.123

excess amounts inhibit

20%, 91% inhibition

41% residual activity at 1 mM

744885

3.2.1.20

moderate inhibition at 5 mM

10% v/v, about 40% loss of activity

727250

3.2.1.25

5 mM, no residual activity

695304

3.2.1.33

83.3% residual activity at 10% (v/v)

inhibition above 50 mM

complete inhibition at 10%

inhibition reversible when up to 80% ethanol concentration used

5%, 16% inhibition of activity with carboxymethyl cellulose, 24% inhibition of xylanase activity, fusion enzyme (EG-M-Xyn) of endoglucanase (cellulase) from Teleogryllus emma and xylanase from Thermomyces lanuginosus

20%, 29.5% loss of activity

749651