Ligand dimethyl sulfoxide

cosolvent DMF improves the transglycosylation yields in concentrations of 2%-10% v/v, whereas at higher concentrations (>30% v/v DMSO), it turns out to be deleterious for the process

753044

3.2.1.21

5 entries

3.2.1.3

717115

3.2.1.31

1%, 1.3fold activation

746874

3.2.1.33

catalytic activity is promoted in the presence of DMSO. DMSO affects the oligomerization state, causing the enzyme dimers to associate into tetramers

11% activation at 10% w/v

707248

3.2.1.73

activation to 111.5% at 5 mM

the activity progressively increases with increase in dimethyl sulfoxide concentration up to 5% (v/v)

699225

3.4.19.6

activity using substrates containing 2% v/v DMSO is 5% higher than that using substrate containing no DSMO

activation

12% activation at 5%

increases enzyme activity up to 2fold with increasing concentration

about 140% activity at 2 mM

752343

3.4.24.B17

induces conformational changes, stimulates with SecY s substrate, at concentration up to 20% v/v, slightly inhibitory with casein as a substrate

650082

3.5.2.3

increases the catalytic efficiency on the ring cyclization reaction, but not on the ring hydrolysis

246644

3.6.1.54

112% activity at 10% (v/v) DMSO

757216

6wii, 3D-view

3.6.5.6

cosolvent stabilizes tubulin

644203

4.1.2.38

highest activity between 20% and 30% dimethyl sulfoxide (v/v) with a peak at 25%. Records of pH-activity profiles at different dimethyl sulfoxide concentrations and constant ionic strength (100 mM) reveals a strong influence of the cosolvent on the activity of BAL, and indicates a cross effect on the optimal pH with a shift of profiles to the alkaline milieu. Correlation between the dependency on pH and dimethyl sulfoxide concentration is due to interaction of dimethyl sulfoxide with the amino acid side chain Glu50 in the catalytic site of the biocatalyst

10% v/v

24% activation at 0.5%

activates

enhances activity

water-miscible, enhances phosphotransferase activity

650390

5.4.4.6

activates the whole enzyme activity

742730

6.2.1.55

levels of samp3ylated proteins and samp3 transcripts are increased by the addition of dimethyl sulfoxide to aerobically growing cells

745772

6.3.4.16

activates in absence of the activator acetylglutamate

1462

5ojo, 3D-view

Inhibitor in Enzyme-catalyzed Reactions (511 results)

32.6% residual activity at 5% (v/v)

8.4% residual activity at 40% (v/v)

inactivation

complete inhibition in buffer without NaCl, 60% inhibition in buffer with 600 mM NaCl

complete inhibition by 50% DMSO

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

742261

1.11.1.14

50% inhibition at 20%, 90% inhibition at 30%, pH 5.0, 25Â°C

763987

1.11.1.16

50% inhibition at 20%, 90% inhibition at 30%, pH 5.0, 25Â°C

763987

1.11.1.19

less than 10% residual activity at 40% (v/v)

764606

3vxj, 3D-view

1.11.1.7

76.0% residual activity at 30% (v/v)

competitive inhibition at 16.6-66 mM, binding structure analysis by circular dichroism and fluorescence spectroscopy. Seven DMSO molecules interact with amino acids onthe surface of Renilla luciferase. Two of them interact with two catalytic residues (Glu144, His285), the rest of the DMSO molecules have specific interactions with the residues in the substrate binding site including Pro220, Phe180, and Phe261

745096

7omd, 3D-view

1.14.13.163

inhibits slightly by 10% at 20% v/v

744640

1.14.13.8

about 50% inhibition at 0.5 % (v/v)

conversion of 5-epiaristolochene to capsidiol activity is inhibited at concentrations above 10% (v/v) dimethyl sulfoxide

1-33% residual activity at 40% (v/v)

739949

1.2.1.5

10% (v/v), 32% inhibition

722210

1.3.3.5

68.04% residual activity at 50% (v/v)

slightly inhibitory

in the presence of 4% (v/v) DMSO, Mycobacterium tubercolosis reductase activity is reduced by only 10%. It is recommended that the DMSO content in sets of inhibition assays should be kept at a constant with 4% (v/v) DMSO as the upper limit

competitive, about 82% inhibition at 1% v/v

756932

2.1.1.100

more than 4% cause inhibition

485043

2.3.1.17

20% inhibition at 40% v/v

about 22.9% decreased enzyme activity, 10%

705085

2.4.1.19

98% residual activity at 5 mM

757110

2.4.1.22

20% v/v, 43% inhibition

675468

2.4.1.245

5 mM, 89% loss of activity

747674

2.4.1.90

20% v/v, 62% inhibition

80% inhibition at 20% v/v

40% inhibition at 20%, 70% inhibition at 30%; slight to moderate inhibition at 20-30%

50% inhibition at 10% v/v, no inhibition at 2.86% v/v

about 60% residual activity at 30% (v/v)

753524

3.1.1.117

10 mM, 14% loss of activity; 16% inhibition at 10 mM

751237

3.1.1.2

71% residual activity in the presence of 90% (v/v) dimethyl sulfoxide, after 60 min at 70Â°C

BTID-A, 54% inhibition at 1% w/v

70% inihibition at 5%

49% inhibition at 75% v/v

730129

3.1.1.75

85% inhibition at 10% (vol/vol)

730744

3.1.1.79

increase in enzyme activity (130%) is observed at 25% v/v DMSO although at a higher concentration (50%), DMSO decreases enzyme activity to 72%

5% inhibition

addition to the reaction mixture results in a dose-dependent inhibition of PAP1 activity, 25% loss of PAP1 activity at a 1% concentration

inhibits enzyme activity at concentrations higher than 30% (v/v)

4% inhibition at 10% and 13% at 25%

754214

3.2.1.192

inhibits 26% at 15% and 42% at 30%

754332

3.2.1.20

weak inhibition at 5%

5 mM, no residual activity

695304

3.2.1.33

80.8% residual activity at 10% (v/v)

61%inhibition at 10%

the enzyme is inhibited by 30-50% (v/v) DMSO

732073

3.2.1.98

10%, 18.3% loss of activity

10% (v/v), about% inhibition

reduces the activity by 42% at 6.25% v/v

inhibitory effect with more than 5% (v/v) dimethyl sulfoxide

10% DMSO decreases the activity to 85%. 30% DMSO reduces the activity to about 70%, and 50% DMSO reduces the activity to about 45%

754581

3.4.21.117

catalytic activity of the protease decreases with increasing DMSO concentration

above 5%

50% inhibition at 4%

competitive

the number of active sites of papain decreases with increasing concentration of dimethyl sulfoxide whereas the incubation time, in a buffer containing 3% dimethyl sulfoxide does not affect the number of active sites. A rapid decrease of the initial reaction rate, by up to 30%, is observed between 1 and 2% dimethyl sulfoxide

activity gradually decreased above 1.0% DMSO

763467

3.4.23.1

1%, complete loss of activity

667408

1yx9, 3D-view

3.4.23.12

about 65% residual activity at 0.1 mM