Ligand methanol

reaction with meta-chloroperbenzoic acid in the presence of methanol (3% or ca. 1 M after mixing) at pH 7.4 and 25°C results in the accumulation of a considerable fraction of the P450cam as the putative Cpd II species

704713

1.14.18.1

2 entries

reaction rate 111%

increases maximal reaction rate

slightly stimulating

activity is increased about 6fold in the presence of 5% methanol (v/v)

used in the assay as activating compound in concentration of 0.5% for 96 h

684628

1.3.99.4

activates at up to 25% v/v, inhibits slightly at 50% v/v

763180

1.4.1.20

the catalytic efficiency in 30% (v/v) methanol is 1.15fold than that of in the aqueous phase

activates

MtaB plus methanol positively affect the catalytic efficiency of MtaA. activation of MtaA by MtaB is methanol-dependent. Methylation of cob(I)inamide with methanol is dependent on imidazole but not on the demethylation of methylcob(III)inamide with coenzyme M. The demethylation reaction is even inhibited by imidazole

717561

2.3.1.23

activation, arachidonoyl-CoA as substrate

20% v/v, 17% activation

675468

2.5.1.6

53.26% increased yield of S-adenosyl-L-methionine at 1.0% methanol

activates

30%, 2.3fold stimulation

641996

2.7.6.5

maximal stimulation of GPSI by 20% v/v

at 1% v/v

methanol increases the enzyme activity to 111%

729689

3.1.1.75

10% (v/v): 137% activity compared to no addition

activates enzyme form A and B

134717

3.2.1.133

enzyme activity increases to 104.4% in the presence of 10% (v/v) methanol

707248

3.2.1.14

about 125% activity at 25% (v/v)

750770

4z2i, 3D-view

3.2.1.192

activates 14% at 5%, inhibits 20% at 30%

1%, 1.4fold activation

linear increase in enzyme-catalyzed cleavage of p-nitrophenyl alpha-L-fucoside and fucosyl fluoride

aqueous methanol system, up to 40% methanol, increases transglycosylation

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

a methanol based deblocking solution preserves enzymatic activity, provides conditions compatible with sequencing and enhances deblocking of electroblotted samples

678405

3.4.21.22

25% v/v, 4fold 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

95341

3.4.23.5

exposure of the enzyme to 5-15% (v/v) methanol produces 50% increase in enzyme activity

753835

3.5.1.3

uncompetitive activation

288888

3.5.1.9

optimal activation e.g. between 5-15%, 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

strong stimulation

active at 15-30% v/v methanol with an optimal concentration of 25%

5944

Inhibitor in Enzyme-catalyzed Reactions (186 results)

top print hide

1.1.1.1

50% (v/v), 30% loss of activity

684620

1.1.1.359

40% (v/v), 50% activity

639106

1.1.1.360

20% (v/v), 30% loss of activity

668544

1.1.1.4

14% residual activity at 10% (v/v)

739127

1.1.1.6

10% v/v: 25-75% loss of activity, 5% v/v, 50-95% loss of activity, depending on substrate, enzyme regains activity after removal of alcohol

636296

1.1.1.71

75% inhibition in buffer without NaCl, 81% inhibition in buffer with 600 mM NaCl

substrate inhibition

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

742261

1.11.1.19

about 40% residual activity at 40% (v/v)

in vitro inhibitor

85.0% residual activity at 70% (v/v)

complete inhibition at 50% v/v

inhibits at 20% v/v

40% inhibition at 30% concentration as co-solvent

675467

1.14.14.1

partially affects (10-20%) activity of the active recombinant enzyme; partially affects (10-20%) activity of the active recombinant enzyme; partially affects (10-20%) activity of the active recombinant enzyme; partially affects (10-20%) activity of the active recombinant enzyme; partially affects (10-20%) activity of the active recombinant enzyme; partially affects (10-20%) activity of the active recombinant enzymes

706823

1.14.14.3

bacterial luciferase luminescence intensity decreases to the steady state depending on the methanol concentration

702496

1.14.15.4

10%, v/v, complete inhibition of hydroxylation

complete inhibition at 40% (v/v)

complete inhibition at 2% (v/v)

1 M, 62% inhibition

78.29% residual activity at 50% (v/v)

activates at up to 25% v/v, inhibits slightly at 50% v/v

763180

1.4.3.19

54% residual activity after 30 min incubation at 30% (v/v)

84.55% residual activity at 20% (v/v)

at nonsaturating concentrations of phenylethanolamine, methanol inhibits in a competitive fashion. With respect to S-adenosyl-L-methionine inhibition by methanol is noncompetitive

639437

2.3.1.23

oleoyl-CoA as substrate

10% (v/v), 30% inhibition; 70% inhibition

727099

2.4.1.18

about 45.2% decreased enzyme activity, 10%

5 mM, 36% loss of activity

747674

2.4.2.5

45% inhibition at 20% v/v

2.4% methanol depresses methionine adenosyltransferase specific activity, this effect is not observed with 0.8% methanol

10% v/v, weak

65% inhibition at 20%, 85% inhibition at 30%

758848

2.6.1.B21

65% inhibition at 20%, 85% inhibition at 30%; moderate inhibition at 20-30%

about 50% residual activity at 30% (v/v)

753524

3.1.1.2

48% residual activity in the presence of 90% (v/v) methanol, after 60 min at 70°C

above 20% v/v

inhibitory above 0.14 mM

91% inhibition at 10% (vol/vol)

80-90% inhibition

48% residual activity in the presence of 90% (v/v) methanol, after 60 min at 70°C

20% (v/v), 2 h, 20°C, 44% loss of activity

749724

3.2.1.123

excess amounts inhibit

646694

3.2.1.176

68% residual activity at 1 mM

moderate inhibition at 5 mM

10% v/v, about 5% loss of activity

91.6% residual activity at 10% (v/v)

681359

3.2.1.38

inhibition above 50 mM

99% inhibition at 10%

732324

3.2.1.55

inhibits 15% and 50% at 5% and 10% v/v, respectively

5%, 26.5% inhibition of activity with carboxymethyl cellulose, 13.5% inhibition of xylanase activity, fusion enzyme (EG-M-Xyn) of endoglucanase (cellulase) from Teleogryllus emma and xylanase from Thermomyces lanuginosus

750783

3.2.1.98

20%, 22.4% loss of activity

10% (v/v), about% inhibition

725181

3.2.1.B31

methanol-H2O at 1:2 (v/v) leads to a loss of activity of about only 20%. The enzyme is completely inactivated by methanol-H2O at above 1:1 (v/v)

723359

3.3.2.10

hydration of trans-stilbene oxide

208916

3.3.2.11

reduces the activity by 86% at 3.75% v/v

Ki: 860 mM

inactivation only above 30%

incubation in 20% (v/v) methanol (10-20 h, 4°C) results in partial decomposition of the high molecular weight PSP-GroEL complex with precipitation of denatured chaperonin and a small (no more than 10%) loss of PSP activity

707457