increases conversion, giving the conversion of 90% compared to 9% in control at a substrate concentration of 70 mM in 1 h. Operational stability increases at higher temperatures with the addition of 2-propanol in the reaction mixture with good conversion (90%) and enantiomeric excess (more than 99%) at 45°C and 50°C. It may be used as a co-substrate for the bioreduction reaction, which may help in widening its applicability in terms of substrate tolerance, reduced time of conversion, increased conversion rate and thermostability

696788

1cyd, 3D-view

1.1.1.2

highly efficient reduction of ketones by coupling with excess isopropanol to regenerate NADPH

about 140% activity at 5% (v/v)

764983

1.14.18.1

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

increases maximal reaction rate

activates

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

stimulation

increases the yield of beta-cyclodextrin

488855, 488861

2.4.1.21

above 70%, activation

10% v/v, 460% of initial activity, 30% v/v, 110% of initial activity

isopropanol increases the enzyme activity to 133%

729689

3.1.1.59

activates even at higher concentrations

651510

3.1.1.76

2fold activation at 5% (v/v)

the presence of 15% (v/v) isopropanol generates a significant increase of 80% on enzyme activity

753835

3.4.24.72

about 140% activity at 2 mM

752343

3.5.1.11

5% (v/v), 30 min at room temperature, 1.95fold activation

1% (v/v), 1.2fold activation

756271

3.6.5.3

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

724475

4.6.1.1

isoform AC6 shows about 20% stimulation of activity with 100 mM 2-propanol, isoform AC7 shows about 35% stimulation of activity with 100 mM 2-propanol, isoform AC9 shows about 40% stimulation of activity with 100 mM 2-propanol

713708

4.6.1.13

3 entries

Inhibitor in Enzyme-catalyzed Reactions (179 results)

41.1% residual activity at 5% (v/v)

at 10% propan-2-ol kcat reaches 65% of that at 1.25% propan-2-ol

substrate inhibition

10%, inactivation

compatitive inhibition at 19.3-76 mM, binding structure analysis by circular dichroism and fluorescence spectroscopy. Four isopropanol molecules interact with amino acids. Most of these molecules move around the amino acidin the binding sites, and only one isopropanol molecule interacts with His285

745096

1.14.13.92

52% inhibition at 30% concentration as co-solvent

675467

1.17.1.10

33-66% residual activity at 20 and 40% (v/v)

IC50 of 4.7 vol%

inhibits about 60% at 15%

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

763180

1.4.1.20

in the presence of isopropanol at 10% (v/v), the enzyme retains about 30% of the original activity. However, the enzyme exhibits nearly no activity in the presence of isopropanol at 30% (v/v)

10% (v/v), 14% inhibition; 86% inhibition

20% inhibition at 20% v/v

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

about 30% residual activity at 10% (v/v)

753524

3.1.1.2

55% residual activity in the presence of 90% (v/v) 2-propanol, after 60 min at 70°C

complete inhibition at 75% v/v

80-90% inhibition

65-95% inhibition at 5-10%, respetively

749608

3.1.8.1

55% residual activity in the presence of 90% (v/v) 2-propanol, after 60 min at 70°C

692889

3.2.1.2

40%, relative activity is decreased to 80%

746791

5wqs, 3D-view

3.2.1.20

strong inhibition at 5%

1% (v/v), about 25% loss of activity, 5% (v/v), about 55% loss of activity

749441

3.2.1.78

about 60% residual activity at 20% (v/v)

749688

3.2.1.8

5%, 21.6% inhibition of activity with carboxymethyl cellulose, 53% inhibition of xylanase activity, fusion enzyme (EG-M-Xyn) of endoglucanase (cellulase) from Teleogryllus emma and xylanase from Thermomyces lanuginosus

750783

3.2.1.B1

about 40% residual activity at 10% (v/v)

731420, 750000