Information on EC 1.1.1.B3 - (S)-specific secondary alcohol dehydrogenase

Substrates: 100% (S)-enantiospecific product
Products: -

4'-acetylphenyl methanesulfonate + NADH + H+

(S)-4-(1-hydroxyethyl)phenyl methanesulfonate + NAD+

Substrates: 100% (S)-enantiospecific product
Products: -

4'-aminoacetophenone + NADH + H+

(S)-1-(4-aminophenyl)ethanol + NAD+

Substrates: 50% (S)-enantiospecific product
Products: -

4'-bromoacetophenone + NADH + H+

(1S)-1-(4-bromophenyl)ethanol + NAD+

Substrates: 82% of the activity with acetophenone
Products: -

4'-bromoacetophenone + NADH + H+

(S)-1-(4-bromophenyl)ethanol + NAD+

Substrates: 100% (S)-enantiospecific product
Products: -

4'-chloroacetophenone + NADH + H+

(1S)-1-(4-chlorophenyl)ethanol + NAD+

4'-chloroacetophenone + NADH + H+

(S)-1-(4-chlorophenyl)ethanol + NAD+

Substrates: 100% (S)-enantiospecific product
Products: -

4'-ethylacetophenone + NADH + H+

(S)-1-(4-ethylphenyl)ethanol + NAD+

Substrates: 100% (S)-enantiospecific product
Products: -

4'-fluoroacetophenone + NADH + H+

(1S)-1-(4-fluorophenyl)ethanol + NAD+

4'-fluoroacetophenone + NADH + H+

(S)-1-(4-fluorophenyl)ethanol + NAD+

Substrates: 100% (S)-enantiospecific product
Products: -

4'-hydroxyacetophenone + NADH + H+

(S)-4-(1-hydroxyethyl)phenol + NAD+

Substrates: 90% (S)-enantiospecific product
Products: -

4'-iodoacetophenone + NADH + H+

(1S)-1-(4-iodophenyl)ethanol + NAD+

Substrates: 31% of the activity with acetophenone
Products: -

4'-methoxyacetophenone + NADH + H+

(S)-1-(4-methoxyphenyl)ethanol + NAD+

Substrates: 100% (S)-enantiospecific product
Products: -

4'-nitroacetophenone + NADH + H+

(S)-1-(4-nitrophenyl)ethanol + NAD+

Substrates: 100% (S)-enantiospecific product
Products: -

4-acetylbenzonitrile + NADH + H+

(S)-4-(1-hydroxyethyl)benzonitrile + NAD+

Substrates: 100% (S)-enantiospecific product
Products: -

4-acetylpyridine + NADH + H+

(S)-1-(pyridin-4-yl)ethanol + NAD+

Substrates: 100% (S)-enantiospecific product
Products: -

4-chloro-3-oxobutanoate + NADH + H+

(S)-4-chloro-3-hydroxybutanoate + NAD+

Substrates: -
Products: 99% enantiomeric excess of (S)-enantiomer

4-methylpentan-2-ol + NADP+

4-methylpentan-2-one + NADPH + H+

Substrates: -
Products: -

4-phenylbutan-2-ol + NADP+

4-phenylbutan-2-one + NADPH + H+

Substrates: -
Products: -

6-hydroxy-1-indanone + NADH + H+

(S)-2,3-dihydro-1H-indene-1,6-diol + NAD+

Substrates: 100% (S)-enantiospecific product
Products: -

6-methyl-5-hepten-2-one + NADH + H+

(S)-6-methyl-5-hepten-2-ol + NAD+

Nocardia fusca AKU 2123

Substrates: -
Products: 188% of the activity with (RS)-2-hexanol

acetophenone + NADH + H+

(1S)-1-phenylethanol + NAD+

5 entries

acetophenone + NADH + H+

(S)-1-phenylethanol + NAD+

5 entries

acetophenone + NADH + H+

alpha-phenylethanol + NAD+

Substrates: 87% of the activity with phenylacetaldehyde
Products: -

acetophenone + NADPH + H+

(1S)-1-phenylethanol + NADP+

Substrates: -
Products: -

alpha-tetralone + NADH + H+

(S)-alpha-tetralol + NAD+

Substrates: completely enantioselective reaction
Products: 99% enantiomeric excess after 6 h at 50°C

capronaldehyde + NADH + H+

n-hexanol + NAD+

Substrates: 522% of the activity with phenylacetaldehyde
Products: -

ethyl (R)-4-chloro-3-hydroxybutanoate + NAD+

ethyl 4-chloro-3-oxobutanoate + NADH + H+

Nocardia fusca AKU 2123

Substrates: -
Products: 38.1% of the activity with (RS)-2-hexanol

ethyl 2-chloro-3-oxobutanoate + NADH + H+

ethyl 2-chloro-3-hydroxybutanoate + NAD+

Substrates: 49% of the activity with ethyl 4-chloro-3-oxobutanoate
Products: -

ethyl 3-oxobutanoate + NADH + H+

ethyl 3-hydroxybutanoate + NAD+

Substrates: 28% of the activity with ethyl 4-chloro-3-oxobutanoate
Products: -

ethyl 3-oxobutanoate + NADPH + H+

ethyl (S)-3-hydroxybutanoate + NADP+

Substrates: -
Products: -

ethyl 4-chloro-3-oxobutanoate + NADH + H+

ethyl (R)-4-chloro-3-hydroxybutanoate + NAD+

ethyl 4-chloro-3-oxobutanoate + NADH + H+

ethyl (S)-4-chloro-3-hydroxybutanoate + NAD+

Substrates: -
Products: product in more than 99% enantiomeric excess

ethyl 4-chloro-3-oxobutanoate + NADPH + H+

ethyl (S)-4-chloro-3-hydroxybutanoate + NADP+

heptan-1-ol + NADP+

heptanal + NADPH + H+

Substrates: -
Products: -

heptan-2-ol + NADP+

heptan-2-one + NADPH + H+

Substrates: -
Products: -

heptan-2-one + NADH + H+

heptan-2-ol + NAD+

Substrates: -
Products: -

heptan-3-one + NADH + H+

heptan-3-ol + NAD+

Substrates: -
Products: -

heptan-4-one + NADH + H+

heptan-4-ol + NAD+

Substrates: -
Products: -

hexan-1-ol + NADP+

hexanal + NADPH + H+

Substrates: -
Products: -

hexan-2-ol + NADP+

hexan-2-one + NADPH + H+

Substrates: -
Products: -

hexan-2-one + NADH + H+

hexan-2-ol + NAD+

Substrates: -
Products: -

hexan-3-one + NADH + H+

hexan-3-ol + NAD+

Substrates: -
Products: -

methyl (4-chlorobenzoyl)acetate + NADH + H+

(S)-methyl 3-(4-chlorophenyl)-3-hydroxypropanoate + NAD+

Substrates: 100% (S)-enantiospecific product
Products: -

methyl 3-(4-ethylphenyl)-3-oxopropanoate + NADH + H+

(S)-methyl 3-(4-ethylphenyl)-3-hydroxypropanoate + NAD+

Substrates: 100% (S)-enantiospecific product
Products: -

methyl 3-(4-methylphenyl)-3-oxopropanoate + NADH + H+

(S)-methyl 3-hydroxy-3-(4-methylphenyl)propanoate + NAD+

Substrates: 100% (S)-enantiospecific product
Products: -

methyl 3-oxo-3-phenylpropanoate + NADH + H+

(S)-methyl 3-hydroxy-3-phenylpropanoate + NAD+

Substrates: 100% (S)-enantiospecific product
Products: -

methyl 4-bromobenzoylacetate + NADH + H+

(S)-methyl 3-(4-bromophenyl)-3-hydroxypropanoate + NAD+

Substrates: 100% (S)-enantiospecific product
Products: -

methyl 4-chloro-3-oxobutanoate + NADPH + H+

methyl (S)-4-chloro-3-hydroxybutanoate + NADP+

Substrates: -
Products: -

methyl 4-fluorobenzoylacetate + NADH + H+

(S)-methyl 3-(4-fluorophenyl)-3-hydroxypropanoate + NAD+

Substrates: 100% (S)-enantiospecific product
Products: -

n-valeraldehyde + NADH + H+

? + NAD+

Nocardia fusca AKU 2123

Substrates: 84% of the activity with (RS)-2-hexanol
Products: -

nonan-2-one + NADH + H+

nonan-2-ol + NAD+

Substrates: -
Products: -

nonan-3-one + NADH + H+

nonan-3-ol + NAD+

Substrates: -
Products: -

nonan-4-one + NADH + H+

nonan-4-ol + NAD+

Substrates: -
Products: -

nonan-5-one + NADH + H+

nonan-5-ol + NAD+

Substrates: -
Products: -

octan-1-ol + NADP+

octanal + NADPH + H+

Substrates: -
Products: -

octan-2-ol + NADP+

octan-2-one + NADPH + H+

Substrates: -
Products: -

octan-2-one + NADH + H+

octan-2-ol + NAD+

Substrates: -
Products: -

octan-3-one + NADH + H+

octan-3-ol + NAD+

Substrates: -
Products: -

octan-4-one + NADH + H+

octan-4-ol + NAD+

Substrates: -
Products: -

p-chloro-acetophenone + NADH + H+

alpha-(p-chlorophenyl)ethanol + NAD+

Substrates: 288% of the activity with phenylacetaldehyde
Products: -

pentan-1-ol + NADP+

pentanal + NADPH + H+

Substrates: -
Products: -

pentan-2-ol + NADP+

pentan-2-one + NADPH + H+

Substrates: -
Products: -

pentan-2-one + NADH + H+

pentan-2-ol + NAD+

Substrates: -
Products: -

pentan-3-one + NADH + H+

pentan-3-ol + NAD+

Substrates: -
Products: -

phenylacetaldehyde + NADH + H+

2-phenylethanol + NAD+

Substrates: -
Products: -

propiophenone + NADH + H+

(S)-1-phenylpropan-1-ol + NAD+

pyruvic acid ethyl ester + NADH + H+

? + NAD+

Nocardia fusca AKU 2123

Substrates: 225% of the activity with (RS)-2-hexanol
Products: -

rac-1-indanol + NAD+

1-indanone + NADH + H+

Substrates: 3900% activity compared to (S)-1-phenylethanol
Products: -

rac-alpha-tetralol + NAD+

alpha-tetralone + NADH + H+

Substrates: 2700% activity compared to (S)-1-phenylethanol
Products: -

valeraldehyde + NADH + H+

n-pentanol + NAD+

Substrates: 433% of the activity with phenylacetaldehyde
Products: -

additional information

7 entries

(R)-1-phenylethanol + NAD+

1-phenylethanone + NADH + H+

Nocardia fusca AKU 2123

Substrates: 0.9% of the activity with (RS)-2-hexanol
Products: -

(R)-1-phenylethanol + NAD+

1-phenylethanone + NADH + H+

Nocardia fusca AKU 2123

Substrates: 21% of the activity with (RS)-2-hexanol
Products: -

(S)-1-phenylethanol + NAD+

acetophenone + NADH + H+

Substrates: -
Products: -

(S)-1-phenylethanol + NAD+

acetophenone + NADH + H+

Substrates: the enzyme catalyzes the stereospecific oxidation of (S)-1-phenylethanol to acetophenone during anaerobic ethylbenzene mineralization, but also the reverse reaction, i.e. NADH-dependent enantioselective reduction of acetophenone to (S)-1-phenylethanol, high enantioselectivity of the reaction
Products: -

(S)-1-phenylethanol + NAD+

acetophenone + NADH + H+

Substrates: -
Products: -

(S)-1-phenylethanol + NAD+

acetophenone + NADH + H+

(S)-1-phenylethanol + NAD+

acetophenone + NADH + H+

Substrates: -
Products: -

(S)-1-phenylethanol + NAD+

acetophenone + NADH + H+

Rhodotorula sp. AS2.2241

Substrates: -
Products: -

(S)-1-phenylethanol + NAD+

acetophenone + NADH + H+

Substrates: activity of the wild-type enzyme, the mutant I886A is (R)-specific forming (R)-1-phenylethanol
Products: -

(S)-1-phenylethanol + NAD+

acetophenone + NADH + H+

Substrates: -
Products: -

(S)-1-phenylethanol + NAD+

acetophenone + NADH + H+

Substrates: asymmetric reduction of acetophenone to produce (S)-1-phenylethanol, with an enantiomeric excess of more than 99%
Products: -

(S)-1-phenylethanol + NAD+

acetophenone + NADH + H+

Thermus thermophilus HB27 / ATCC BAA-163 / DSM 7039

Substrates: -
Products: -

(S)-1-phenylethanol + NAD+

acetophenone + NADH + H+

Thermus thermophilus HB27 / ATCC BAA-163 / DSM 7039

Substrates: asymmetric reduction of acetophenone to produce (S)-1-phenylethanol, with an enantiomeric excess of more than 99%
Products: -

(S)-1-phenylethanol + NAD+

acetophenone + NADH + H+

Substrates: -
Products: -

(S)-1-phenylethanol + NAD+

acetophenone + NADH + H+

Substrates: -
Products: -

(S)-2-butanol + NAD+

2-butanone + NADH + H+

Nocardia fusca AKU 2123

Substrates: 27% of the activity with (RS)-2-hexanol
Products: -

(S)-2-butanol + NAD+

2-butanone + NADH + H+

Substrates: -
Products: -

(S)-2-butanol + NAD+

2-butanone + NADH + H+

Saccharomyces pastorianus

Substrates: -
Products: -

(S)-2-butanol + NAD+

2-butanone + NADH + H+

Saccharomyces pastorianus Y379-50

Substrates: -
Products: -

(S)-2-butanol + NAD+

2-butanone + NADH + H+

Substrates: -
Products: -

(S)-2-hexanol + NAD+

2-hexanone + NADH + H+

Nocardia fusca AKU 2123

Substrates: reaction is stereoselective
Products: -

(S)-2-hexanol + NAD+

2-hexanone + NADH + H+

Nocardia fusca AKU 2123

Substrates: 121% of the activity with (RS)-2-hexanol
Products: -

(S)-2-pentanol + NAD+

2-pentanone + NADH + H+

Nocardia fusca AKU 2123

Substrates: 91% of the activity with (RS)-2-hexanol
Products: -

(S)-2-pentanol + NAD+

2-pentanone + NADH + H+

Substrates: -
Products: -

1-indanone + NADH + H+

(S)-1-indanol + NAD+

Substrates: 100% (S)-enantiospecific product
Products: -

1-indanone + NADH + H+

(S)-1-indanol + NAD+

Substrates: -
Products: 99% enantiomeric excess after 6 h at 50°C

1-phenylbutan-1-one + NADH + H+

1-phenylbutan-1-ol + NAD+

Substrates: -
Products: -

1-phenylbutan-1-one + NADH + H+

1-phenylbutan-1-ol + NAD+

Geotrichum candidum NBRC 4597

Substrates: -
Products: -

1-phenylpentan-1-one + NADH + H+

1-phenylpentan-1-ol + NAD+

Substrates: -
Products: -

1-phenylpentan-1-one + NADH + H+

1-phenylpentan-1-ol + NAD+

Geotrichum candidum NBRC 4597

Substrates: -
Products: -

1-phenylpropan-1-one + NADH + H+

1-phenylpropan-1-ol + NAD+

Substrates: -
Products: -

1-phenylpropan-1-one + NADH + H+

1-phenylpropan-1-ol + NAD+

Geotrichum candidum NBRC 4597

Substrates: -
Products: -

2'-fluoroacetophenone + NADH + H+

(1S)-1-(2-fluorophenyl)ethanol + NAD+

Substrates: 102% of the activity with acetophenone
Products: -

2'-fluoroacetophenone + NADH + H+

(1S)-1-(2-fluorophenyl)ethanol + NAD+

Substrates: 102% of the activity with acetophenone
Products: -

3'-fluoroacetophenone + NADH + H+

(1S)-1-(3-fluorophenyl)ethanol + NAD+

Substrates: 102% of the activity with acetophenone
Products: -

3'-fluoroacetophenone + NADH + H+

(1S)-1-(3-fluorophenyl)ethanol + NAD+

Substrates: 102% of the activity with acetophenone
Products: -

3-heptanone + NADH + H+

3-hexanol + NADH + H+

Substrates: -
Products: -

3-heptanone + NADH + H+

3-hexanol + NADH + H+

Geotrichum candidum NBRC 4597

Substrates: -
Products: -

4'-chloroacetophenone + NADH + H+

(1S)-1-(4-chlorophenyl)ethanol + NAD+

Substrates: 83% of the activity with acetophenone
Products: -

4'-chloroacetophenone + NADH + H+

(1S)-1-(4-chlorophenyl)ethanol + NAD+

Substrates: 83% of the activity with acetophenone
Products: -

4'-fluoroacetophenone + NADH + H+

(1S)-1-(4-fluorophenyl)ethanol + NAD+

Substrates: 117% of the activity with acetophenone
Products: -

4'-fluoroacetophenone + NADH + H+

(1S)-1-(4-fluorophenyl)ethanol + NAD+

Substrates: 117% of the activity with acetophenone
Products: -

acetophenone + NADH + H+

(1S)-1-phenylethanol + NAD+

Substrates: -
Products: enantiomeric excess of more than 99% for (S)-configuration of product

acetophenone + NADH + H+

(1S)-1-phenylethanol + NAD+

Substrates: -
Products: enantiomeric excess of more than 99% for (S)-configuration of product

acetophenone + NADH + H+

(1S)-1-phenylethanol + NAD+

Substrates: -
Products: -

acetophenone + NADH + H+

(1S)-1-phenylethanol + NAD+

Geotrichum candidum NBRC 4597

Substrates: -
Products: -

acetophenone + NADH + H+

(1S)-1-phenylethanol + NAD+

Rhodococcus ruber

760341

Substrates: -
Products: -

acetophenone + NADH + H+

(S)-1-phenylethanol + NAD+

Substrates: 100% (S)-enantiospecific product
Products: -

acetophenone + NADH + H+

(S)-1-phenylethanol + NAD+

Substrates: 100% (S)-enantiospecific product
Products: -

acetophenone + NADH + H+

(S)-1-phenylethanol + NAD+

Substrates: completely enantioselective reaction
Products: 99% enantiomeric excess after 6 h at 50°C

acetophenone + NADH + H+

(S)-1-phenylethanol + NAD+

Substrates: -
Products: -

acetophenone + NADH + H+

(S)-1-phenylethanol + NAD+

Substrates: -
Products: -

ethyl 4-chloro-3-oxobutanoate + NADH + H+

ethyl (R)-4-chloro-3-hydroxybutanoate + NAD+

685644

Substrates: -
Products: -

ethyl 4-chloro-3-oxobutanoate + NADH + H+

ethyl (R)-4-chloro-3-hydroxybutanoate + NAD+

Nocardia fusca AKU 2123

Substrates: -
Products: -

ethyl 4-chloro-3-oxobutanoate + NADPH + H+

ethyl (S)-4-chloro-3-hydroxybutanoate + NADP+

Candida albicans

Candida albicans ATCC MYA-2876

Substrates: -
Products: the enzyme catalyzes the asymmetric reduction of ethyl 4-chloro-3-oxobutanoate, 99% enantiomeric excess

ethyl 4-chloro-3-oxobutanoate + NADPH + H+

ethyl (S)-4-chloro-3-hydroxybutanoate + NADP+

Substrates: -
Products: the enzyme catalyzes the asymmetric reduction of ethyl 4-chloro-3-oxobutanoate, 99% enantiomeric excess

ethyl 4-chloro-3-oxobutanoate + NADPH + H+

ethyl (S)-4-chloro-3-hydroxybutanoate + NADP+

Substrates: -
Products: -

propiophenone + NADH + H+

(S)-1-phenylpropan-1-ol + NAD+

Substrates: 100% (S)-enantiospecific product
Products: -

propiophenone + NADH + H+

(S)-1-phenylpropan-1-ol + NAD+

Substrates: 100% (S)-enantiospecific product
Products: -

additional information

Substrates: application of PEDH for asymmetric reduction of 42 prochiral ketones and 11 beta-keto esters to enantiopure secondary alcohols, high enantioselectivity of the reaction, substrate binding mechanism analysis by molecular docking, modeling of enzyme-substrate complexes, overview
Products: -

additional information

additional information

Substrates: no substrates: cetophenone, 2-hydroxyacetophenone, acetone, butanone, 2-pentanone, 3-pentanone, 2-hexanone, 2-heptanone, 2-octanone, cyclohexanone, acetylacetone, 2,5-hexanedione and 5,5-dimethyl-l,3-cyclohexanedione
Products: -

additional information

Nocardia fusca AKU 2123

Substrates: primary alcohols are not accepted as substrate
Products: -

additional information

Substrates: the enzyme catalyzes stereoselective oxidation of (S)-secondary alcohols to corresponding ketones
Products: -

additional information

Rhodotorula sp. AS2.2241

Substrates: the enzyme catalyzes stereoselective oxidation of (S)-secondary alcohols to corresponding ketones
Products: -

additional information

Substrates: substrate specificity of ADHTt in the oxidation and the reduction reactions depends on the substrate, cf. (R)-specific secondary alcohol dehydrogenase, detailed overview. The enzyme shows a high reduction rate with halogenated aryl ketones, such as 2,2,2-trifluoroacetophenone, 2-chloroacetophenone, and 4-chlorobutyrophenone, and with aryl diketones, such as 1-phenyl-1,2-propanedione, although it is not active on benzil, i.e. diphenylethanedione. ADHTt proves to be very effective in reducing aryl alpha-keto esters, although it is not active on aliphatic alpha-keto esters and aryl beta-keto ester. Critical role of the D37 residue in discriminating NAD(H) from NADP(H)
Products: -

show all columns Go to Natural Substrate Search

Please wait a moment until the data is sorted. This message will disappear when the data is sorted.

NATURAL SUBSTRATE

NATURAL PRODUCT

REACTION DIAGRAM

ORGANISM

UNIPROT

LITERATURE

COMMENTARY

REVERSIBILITY
r=reversible
ir=irreversible
?=not specified

(S)-1-phenylethanol + NAD+

acetophenone + NADH + H+

7 entries

(S)-1-phenylethanol + NAD+

acetophenone + NADH + H+

Substrates: -
Products: -

(S)-1-phenylethanol + NAD+

acetophenone + NADH + H+

Substrates: -
Products: -

(S)-1-phenylethanol + NAD+

acetophenone + NADH + H+

Substrates: -
Products: -

(S)-1-phenylethanol + NAD+

acetophenone + NADH + H+

Rhodotorula sp. AS2.2241

Substrates: -
Products: -

(S)-1-phenylethanol + NAD+

acetophenone + NADH + H+

Substrates: activity of the wild-type enzyme, the mutant I886A is (R)-specific forming (R)-1-phenylethanol
Products: -

(S)-1-phenylethanol + NAD+

acetophenone + NADH + H+

Substrates: -
Products: -

(S)-1-phenylethanol + NAD+

acetophenone + NADH + H+

Thermus thermophilus HB27 / ATCC BAA-163 / DSM 7039

Substrates: -
Products: -

show all columns Go to Cofactor Search

Please wait a moment until the data is sorted. This message will disappear when the data is sorted.

COFACTOR

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

IMAGE

NAD+

12 entries

NADH

9 entries

NADP+

NADPH

additional information

NAD+

Nocardia fusca AKU 2123

NAD+

NAD+

NAD+

critical role of the D37 residue in discriminating NAD(H) from NADP(H)

NAD+

NAD+

Saccharomyces pastorianus

NAD+

NAD+

NAD+

NAD+

NAD+

NAD+

NADH

Nocardia fusca AKU 2123

NADH

NADH

NADH

critical role of the D37 residue in discriminating NAD(H) from NADP(H)

NADH

NADH

preferred over NADPH

NADH

NADH

NADH

Rhodococcus ruber

760341

NADPH

about 10% of the activity with NADH

NADPH

strong preference for NADPH as cofactor

additional information

Nocardia fusca AKU 2123

NADPH cannot substitute for NADH

additional information

the enzyme shows no activity with NADP(H)

show all columns Go to Metals and Ions Search

Please wait a moment until the data is sorted. This message will disappear when the data is sorted.

METALS and IONS

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

EDTA

activates to 127% activity compared to the control activity at 1 mM and to 163% at 10 mM

K+

activates to 167% activity compared to the control activity at 1 mM and to 193% at 100 mM

Li+

activates to 127% activity compared to the control activity at 1 mM and to 178% at 100 mM

Na+

activates to 179 at 100 mM

Zinc

sequence contains catalytic and structural zinc binding sites

Zn2+

additional information

Zn2+

contains zinc

Zn2+

activates to 114% activity compared to the control activity at 1 mM

additional information

the addition of Mg2+ does not affect the enzyme activity significantly

additional information

the addition of Mg2+ does not affect the enzyme activity significantly

show all columns Go to Inhibitor Search

Please wait a moment until the data is sorted. This message will disappear when the data is sorted.

INHIBITOR

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

IMAGE

(R)-1-phenylethanol

(S)-1-phenylethanol

strong substrate inhibition, 50% of maximum activity at 0.1 mM

1-butyl-3-methylimidazolium tetrafluoroborate

65% inhibition at 2 mM

4-hydroxy mercuribenzoate

2 mM, 5% residual activity

acetophenone

inhibitory above 0.02 mM, 75% of maximum activity at 1 mM

Ag+

1 mM, no residual activity

AgNO3

Ca2+

10% inhibition at 1 mM and 30% at 100 mM

CdCl2

Nocardia fusca AKU 2123

2 mM, 6.6% residual activity

citrate

2 mM, 28% residual activity

Co(NO3)2

2 mM, 59% residual activity

Cu2+

CuSO4

2 mM, complete inhibition

D-cysteine

2 mM, 8% residual activity

diethyldicarbonate

2 mM, 30% residual activity

EDTA

Fe2+

1 mM, 2.5% residual activity

Fe3+

1 mM, 44% residual activity

FeCl3

2 mM, 2% residual activity

glutathione

2 mM, 31% residual activity

guanidinium hydrochloride

1 M, 1.5% residual activity

Hg2+

67% inhibition at 1 mM

HgCl2

Nocardia fusca AKU 2123

2 mM, no residual activity

hydroxylamine

2 mM, 23% residual activity

Hydroxyquinoline

2 mM, 18% residual activity

iodoacetate

L-cysteine

2 mM, 12% residual activity

Mg2+

MgCl2

2 mM, 75% residual activity

MnSO4

2 mM, 53% residual activity

N-ethylmaleimide

2 mM, 5% residual activity

NiCl2

2 mM, 24% residual activity

o-phenanthroline

oxalate

2 mM, 26% residual activity

Pb(OAc)2

2 mM, 8% residual activity

phenyl methyl sulfonylfluoride

5 mM, 49% residual activity

potassium iodide

1 M, 1.4% residual activity

SDS

1%, no residual activity

Sodium azide

2 mM, 35% residual activity

sodium dodecylsulfate

tartarate

2 mM, 21% residual activity

Triton X-100

1% w/v, 67% residual activity

trypaflavine

Nocardia fusca AKU 2123

1 mM, 7.7% residual activity

Tween 80

1% w/v, 26.5% residual activity

Urea

1 M, 5.8% residual activity

Zn2+

1 mM, 79% residual activity

ZnSO4

2 mM, 2% residual activity

additional information

AgNO3

2 mM, complete inhibition

AgNO3

Nocardia fusca AKU 2123

2 mM, no% residual activity

Cu2+

1 mM, no residual activity

Cu2+

23% inhibition at 1 mM

EDTA

2 mM, 49% residual activity

EDTA

Nocardia fusca AKU 2123

2 mM, 56% residual activity

EDTA

5 mM, 50% residual activity

iodoacetate

Nocardia fusca AKU 2123

2 mM, 67% residual activity

iodoacetate

5% inhibition at 1 mM

Mg2+

1 mM, 77% residual activity

Mg2+

33% inhibition at 100 mM

o-phenanthroline

2 mM, 9% residual activity

o-phenanthroline

Nocardia fusca AKU 2123

2 mM, 0.4% residual activity

sodium dodecylsulfate

1% w/v, 6% residual activity

sodium dodecylsulfate

1%, 51% residual activity

additional information

not inhibitory or activating: EDTA, dithiothreitol

additional information

not inhibitory at 2 mM: BaCl2, CaCO3, NaCl

additional information

no effects by 5 mM 2-mercaptoethanol

show all columns Go to Activating Compound Search

Please wait a moment until the data is sorted. This message will disappear when the data is sorted.

ACTIVATING COMPOUND

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

IMAGE

2-mercaptoethanol

2 mM, 115% of initial activity

o-phenanthroline

activates to 108% activity compared to the control activity at 0.1 mM and to 109% at 1 mM

Triton X-100

1%, 112% of initial activity

Tween-20

1%, 111% of initial activity

Tween-80

1%, 115% of initial activity

additional information

not inhibitory or activating: EDTA, dithiothreitol

Go to Disease Search

Please wait a moment until the data is sorted. This message will disappear when the data is sorted.

DISEASE

TITLE OF PUBLICATION

LINK TO PUBMED

Neoplasms

Unusual charge stabilization of NADP+ in 17beta-hydroxysteroid dehydrogenase.

9525918

show all columns Go to KM Value Search

Please wait a moment until the data is sorted. This message will disappear when the data is sorted.

KM VALUE [mM]

SUBSTRATE

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

IMAGE

4.2

(S)-1-indanol

pH 6.0, 65°C, recombinant enzyme, reduction reaction

0.0055

(S)-1-phenylethanol

pH 7.8, 25°C

0.012 - 29.8

(S)-2-butanol

0.33

(S)-2-hexanol

Nocardia fusca AKU 2123

30°C, pH 7.5

0.07 - 8.8

(S)-2-pentanol

1.6

(S)-3-pentyn-2-ol

Nocardia fusca AKU 2123

30°C, pH 7.5

0.4 - 2.25

1-chloroacetophenone

27.6

1-Indanone

pH 6.0, 65°C, recombinant enzyme, reduction reaction

2.5

2-Hexanone

Nocardia fusca AKU 2123

30°C, pH 7.5

6.4

4-chloro-3-oxobutanoate

pH 6.0, 45°C

0.0113 - 0.153

acetophenone

5.8

alpha-tetralone

pH 6.0, 65°C, recombinant enzyme, reduction reaction

3.3

ethyl 4-chloro-3-oxobutanoate

pH 6.0, 30°C

0.157

NADH

pH 7.0, 25°C

5.1

rac-1-indanol

pH 6.0, 65°C, recombinant enzyme, reduction reaction

5.3

rac-alpha-tetralol

pH 6.0, 65°C, recombinant enzyme, reduction reaction

additional information

0.012

(S)-2-butanol

wild type enzyme, in 0.1 M glycine-NaOH buffer (pH 10.5), at 65°C

29.8

(S)-2-butanol

mutant enzyme W95L/N249Y, in 0.1 M glycine-NaOH buffer (pH 10.5), at 65°C

0.07

(S)-2-pentanol

wild type enzyme, in 0.1 M glycine-NaOH buffer (pH 10.5), at 65°C

8.8

(S)-2-pentanol

mutant enzyme W95L/N249Y, in 0.1 M glycine-NaOH buffer (pH 10.5), at 65°C

0.4

1-chloroacetophenone

mutant N179S, pH 6.5, 30°C

1.31

1-chloroacetophenone

mutant S174G, pH 6.5, 30°C

1.45

1-chloroacetophenone

mutant N179S/I214F/S215G, pH 6.5, 30°C

2.25

1-chloroacetophenone

wild-type, pH 6.5, 30°C

0.0113

acetophenone

pH 7.8, 25°C

0.153

acetophenone

pH 7.0, 25°C

additional information

enzyme exhibits positive cooperativity in both forward and reverse direction

additional information

kinetics and substrate specificity, overview

additional information

kinetics

show all columns Go to Turnover Number Search

Please wait a moment until the data is sorted. This message will disappear when the data is sorted.

TURNOVER NUMBER [1/s]

SUBSTRATE

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

IMAGE

61.4

(S)-1-indanol

pH 6.0, 65°C, recombinant enzyme, reduction reaction

1.2 - 4.8

(S)-2-butanol

2.6 - 6.7

(S)-2-pentanol

3.95 - 204

1-chloroacetophenone

8.3

1-Indanone

pH 6.0, 65°C, recombinant enzyme, reduction reaction

7.7

alpha-tetralone

pH 6.0, 65°C, recombinant enzyme, reduction reaction

45.7

rac-1-indanol

pH 6.0, 65°C, recombinant enzyme, reduction reaction

48.1

rac-alpha-tetralol

pH 6.0, 65°C, recombinant enzyme, reduction reaction

1.2

(S)-2-butanol

wild type enzyme, in 0.1 M glycine-NaOH buffer (pH 10.5), at 65°C

4.8

(S)-2-butanol

mutant enzyme W95L/N249Y, in 0.1 M glycine-NaOH buffer (pH 10.5), at 65°C

2.6

(S)-2-pentanol

wild type enzyme, in 0.1 M glycine-NaOH buffer (pH 10.5), at 65°C

6.7

(S)-2-pentanol

mutant enzyme W95L/N249Y, in 0.1 M glycine-NaOH buffer (pH 10.5), at 65°C

3.95

1-chloroacetophenone

wild-type, pH 6.5, 30°C

21.8

1-chloroacetophenone

mutant S174G, pH 6.5, 30°C

119

1-chloroacetophenone

mutant N179S, pH 6.5, 30°C

204

1-chloroacetophenone

mutant N179S/I214F/S215G, pH 6.5, 30°C

show all columns Go to kcat/KM Value Search

Please wait a moment until the data is sorted. This message will disappear when the data is sorted.

kcat/KM VALUE [1/mMs^-1]

SUBSTRATE

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

IMAGE

1.75 - 295

1-chloroacetophenone

1.75

1-chloroacetophenone

wild-type, pH 6.5, 30°C

14.2

1-chloroacetophenone

mutant S174G, pH 6.5, 30°C

140

1-chloroacetophenone

mutant N179S/I214F/S215G, pH 6.5, 30°C

295

1-chloroacetophenone

mutant N179S, pH 6.5, 30°C

show all columns Go to Specific Activity Search

Please wait a moment until the data is sorted. This message will disappear when the data is sorted.

SPECIFIC ACTIVITY [µmol/min/mg]

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

1.5

immobilized recombinant enzyme

151.1

substrate: (S)-1-phenylethanol

224

pH 6.0, 30°C

358.6

pH 7.0, 25°C

41.5

Nocardia fusca AKU 2123

30°C, pH 7.5

846

30°C, pH 6.0

show all columns Go to pH Optimum Search

Please wait a moment until the data is sorted. This message will disappear when the data is sorted.

pH OPTIMUM

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

oxidation reaction

5.5

ketone reduction

5.8

alcohol oxidation

show all columns Go to pH Range Search

reduction reaction

Please wait a moment until the data is sorted. This message will disappear when the data is sorted.

pH RANGE

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

5.5 - 6.5

Nocardia fusca AKU 2123

reduction reaction

5.5 - 7

more than 80% of maximum activity within

6 - 7.7

reduction reaction, high activity

6.5 - 7

more than 80% of maximum activity

8.5 - 9.5

Nocardia fusca AKU 2123

oxidation reaction

9 - 10

oxidation reaction, high activity

show all columns Go to Temperature Optimum Search

Please wait a moment until the data is sorted. This message will disappear when the data is sorted.

TEMPERATURE OPTIMUM

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

Nocardia fusca AKU 2123

oxidation reaction

oxidation reaction

show all columns Go to Temperature Range Search

Nocardia fusca AKU 2123

reduction reaction

reduction reaction

Please wait a moment until the data is sorted. This message will disappear when the data is sorted.

TEMPERATURE RANGE

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

54% of maximum activity

25 - 35

more than 80% of maximum activity within

25 - 73

the enzyme displays activity at temperatures up to 73°C

no residual activity

61% of maximum activity

show all columns Go to Organism Search

only manually annotated data include textmining data from AMENDAenzyme occurrence in organism, localization and source tissue with reliability ranks include all textmining data from AMENDAenzyme occurrence in organism, localization and source tissue with reliability ranks + FRENDAco-occurrence of enzyme names and organism names (less precise)

Please wait a moment until the data is sorted. This message will disappear when the data is sorted.

ORGANISM

COMMENTARY

LITERATURE

UNIPROT

SEQUENCE DB

SOURCE

brenda

brenda

cultivar Jinxuan

UniProt

brenda

Candida albicans

cf. EC 1.1.1.289

Candida albicans ATCC MYA-2876

UniProt

brenda

cf. EC 1.1.1.289

UniProt

brenda

brenda

brenda

brenda

UniProt

brenda

Geotrichum candidum NBRC 4597

UniProt

brenda

Nocardia fusca AKU 2123

brenda

strain DSM 43297

UniProt

brenda

brenda

brenda

Rhodotorula sp. AS2.2241

brenda

brenda

Saccharomyces pastorianus

brenda

Saccharomyces pastorianus Y379-50

brenda

brenda

UniProt

brenda

684583, 701031

brenda

Thermus thermophilus HB27 / ATCC BAA-163 / DSM 7039

brenda

brenda

brenda

brenda

UniProt

brenda

brenda

gene adhB

UniProt

brenda

show all columns Go to Source Tissue Search

only manually annotated data include textmining data from AMENDAenzyme occurrence in organism, localization and source tissue with reliability ranks

Please wait a moment until the data is sorted. This message will disappear when the data is sorted.

SOURCE TISSUE

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

SOURCE

brenda

brenda

show all columns Go to Localization Search

only manually annotated data include textmining data from AMENDAenzyme occurrence in organism, localization and source tissue with reliability ranks

Please wait a moment until the data is sorted. This message will disappear when the data is sorted.

LOCALIZATION

ORGANISM

UNIPROT

COMMENTARY

GeneOntology No.

LITERATURE

SOURCE

brenda

5737

brenda

top hide

Highest Expressing Human Cell Lines

Filter by:

Cell Line Links

Gene Links

show all columns Go to General Information Search

Please wait a moment until the data is sorted. This message will disappear when the data is sorted.

GENERAL INFORMATION

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

evolution

metabolism

evolution

the enzyme belongs to the short-chain dehydrogenase/reductase family

evolution

the enzyme belongs to the short-chain dehydrogenase/reductase family

metabolism

strain EbN1 produces (S)-1-phenylethanol via a direct anaerobic oxidation of ethylbenzene by the molybdenum enzyme ethylbenzene dehydrogenase. In the second step of the pathway, PEDH catalyzes the stereospecific conversion of (S)-1-phenylethanol to acetophenone and is also capable to catalyze the industrially important reverse reaction, namely, NADH-dependent enantioselective reduction of acetophenone to (S)-1-phenylethanol

metabolism

Go to AA Sequence and Transmembrane Helices SearchGo to Localization Prediction

Please wait a moment until the data is sorted. This message will disappear when the data is sorted.

UNIPROT

ENTRY NAME

ORGANISM

NO. OF AA

NO. OF TRANSM. HELICES

MOLECULAR WEIGHT[Da]

SOURCE

SEQUENCE

LOCALIZATION PREDICTION

The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).

A0A494WD27 pBLAST

A0A494WD27_CAMSI

268

29041

TrEMBL

Mitochondrion (Reliability: 5)

A3GF05 pBLAST

A3GF05_PICST

Scheffersomyces stipitis (strain ATCC 58785 / CBS 6054 / NBRC 10063 / NRRL Y-11545)

285

30779

TrEMBL

D5G304 pBLAST

D5G304_CANPA

279

29994

TrEMBL

M5A8V4 pBLAST

M5A8V4_GEOCN

342

36731

TrEMBL

P77990 pBLAST

P77990_THEET

352

37590

TrEMBL

Secretory Pathway (Reliability: 3)

P87219 pBLAST

SOU1_CANAL

Candida albicans (strain SC5314 / ATCC MYA-2876)

281

30038

Swiss-Prot

Q6YBW1 pBLAST

Q6YBW1_RHOER

348

36206

TrEMBL

show all columns Go to Molecular Weight Search

Please wait a moment until the data is sorted. This message will disappear when the data is sorted.

MOLECULAR WEIGHT

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

105000

about, recombinant enzyme, gel filtration in presence of 0.15 M NaCl

120000

gel filtration

140000

recombinant enzyme, gel filtration

150000

Nocardia fusca AKU 2123

gel filtration

26000

4 * 26961, recombinant enzyme, mass spectrometry, 4 * 26000, recombinant enzyme, SDS-PAGE

26961

4 * 26961, recombinant enzyme, mass spectrometry, 4 * 26000, recombinant enzyme, SDS-PAGE

27000

4 * 27000, SDS-PAGE and crystallization data, enzyme is a tetramer with two types of hydrophobic interfaces

29000

4 * 29000, SDS-PAGE

36026

x * 36026, calculated, x * 39000, SDS-PAGE

39000

59000

gel filtration

71000

about, recombinant enzyme, gel filtration in absence of NaCl

93000

PAGE

39000

Nocardia fusca AKU 2123

4 * 39000, SDS-PAGE

39000

x * 36026, calculated, x * 39000, SDS-PAGE

show all columns Go to Subunit Search

Please wait a moment until the data is sorted. This message will disappear when the data is sorted.

SUBUNIT

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

tetramer

x * 29040, calculated from amino acid sequence

x * 36026, calculated, x * 39000, SDS-PAGE

tetramer

4 * 29000, SDS-PAGE

tetramer

4 * 29000, SDS-PAGE

tetramer

Nocardia fusca AKU 2123

4 * 39000, SDS-PAGE

tetramer

4 * 26961, recombinant enzyme, mass spectrometry, 4 * 26000, recombinant enzyme, SDS-PAGE

tetramer

tetramer

Thermus thermophilus HB27 / ATCC BAA-163 / DSM 7039

tetramer

Thermus thermophilus HB27 / ATCC BAA-163 / DSM 7039

4 * 26961, recombinant enzyme, mass spectrometry, 4 * 26000, recombinant enzyme, SDS-PAGE

tetramer

4 * 27000, SDS-PAGE and crystallization data, enzyme is a tetramer with two types of hydrophobic interfaces

tetramer

4 * 27000, SDS-PAGE and crystallization data, enzyme is a tetramer with two types of hydrophobic interfaces

Go to Crystallization (commentary) Search

Please wait a moment until the data is sorted. This message will disappear when the data is sorted.

CRYSTALLIZATION (Commentary)

ORGANISM

UNIPROT

LITERATURE

homology modeling of structure. The substrate binding pocket consists of residues P122, W123, E125, S174, N179, V180, S214, P215, G217, Y218, I223, S224, D225, F226 and V227, with all of the residues lying in the flexible loop regions

apo-enzyme and bound to NAD+, at a resolution of 2.1 and 2.4 A, respectively. Enzyme is a tetamer with two types of hydrophobic interfaces. NAD+-binding is associated with a conformational shift of the substrate binding loop from a crystallographically unordered open to a more ordered closed form

show all columns Go to Protein Variants Search

Please wait a moment until the data is sorted. This message will disappear when the data is sorted.

PROTEIN VARIANTS

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

N179S

about 40fold increase in specific activity

N179S/I214F/S215G

about 50fold increase in specific activity

S174G

about 7fold increase in specific activity

W288A

(R)-selective mutant

W288I

(R)-selective mutant

W288L

the enantiopreference oft he mutant is intermediate between wild type (S)-selectivity and (R)-selectivity

W288M

the enantiopreference of the mutant enzyme is similar to wild type ((S)-selectivity)

W288V

(R)-selective mutant

W288A

Geotrichum candidum NBRC 4597

(R)-selective mutant

W288I

Geotrichum candidum NBRC 4597

(R)-selective mutant

W288L

Geotrichum candidum NBRC 4597

the enantiopreference oft he mutant is intermediate between wild type (S)-selectivity and (R)-selectivity

W288M

Geotrichum candidum NBRC 4597

the enantiopreference of the mutant enzyme is similar to wild type ((S)-selectivity)

W288V

Geotrichum candidum NBRC 4597

(R)-selective mutant

W95L/N249Y

the mutant exhibits higher activity but decreased affinity toward aliphatic alcohols, aldehydes as well as NAD+ and NADH compared to the wild type enzyme, optimum pH is at about pH 8.6

I86A

W110A

the mutant shows imperfect wild type stereoselectivity (S)

W110A/I86A

the mutant enzyme is completely non-stereoselective for the reduction of 2-hexanone.Additionally, an extremely low level of stereoselectivity (i.e. from 10% to 24%) is observed for the reduction of aryl-aliphatic ketones and aliphatic ketones

additional information

I86A

site-directed mutagensis, the secondary alcohol dehydrogenase I86A mutant is stereospecific for (R)-alcohols instead of (S)-alcohols, in contrast to the wild-type enzyme, the mutation I86A allows large substituents to fit into the large pocket of I86ATeSADH, which corresponds to the small pocket in wild-type TeSADH, modeling of the stereopreference of TeSADH I86A

I86A

the mutant shows reversed stereoselectivity (R) compared to the wild type enzyme

additional information

covalent immobilization of the purified recombinant enzyme on different supports, i.e. on glyoxyl agarose, amino epoxy agarose, CNBr-activated sepharose, monoaminoethyl-N-ethylagarose-glutaraldehyde, monoaminoethyl-N-ethyl agarose, or polyethyleneimine agarose, immobilized enzyme activities, overview

additional information

Thermus thermophilus HB27 / ATCC BAA-163 / DSM 7039

show all columns Go to pH Stability Search

Please wait a moment until the data is sorted. This message will disappear when the data is sorted.

pH STABILITY

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

5.5 - 9.5

Nocardia fusca AKU 2123

30 min, 30°C, more than 90% residual activity

5.6

between pH 5.6-7.0, 4°C, stable for 48 h

between pH 5.6-7.0, 4°C, stable for 48 h

after a thermal treatment at pH 7.0 and 70°C for 1 h, the remaining TtADH activity is over 90%, while the soluble protein concentration decreases by a 85%

show all columns Go to Temperature Stability Search

Please wait a moment until the data is sorted. This message will disappear when the data is sorted.

TEMPERATURE STABILITY

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

phosphate buffer, pH 7.0, 7 h, 80% residual activity

half-life 16.5 h

24 h, purified recombinant enzyme, 134% inactivation

additional information

the thermal stability of the enzyme adsorbed by ionic exchange is very similar to the stability of the covalently immobilized enzymes in the pH range 5-9, thermal inactivation kinetics, overview

half-life 2.2 h

Nocardia fusca AKU 2123

30 min, pH 7.0, 85% residual activity

half-life 0.05 h

Nocardia fusca AKU 2123

30 min, pH 7.0, 50% residual activity

24 h, purified recombinant enzyme, 142% inactivation

24 h, purified recombinant enzyme, 107% inactivation

after a thermal treatment at pH 7.0 and 70°C for 1 h, the remaining TtADH activity is over 90%, while the soluble protein concentration decreases by a 85%

show all columns Go to Organic Solvent Search

30 min, purified recombinant enzyme, 50% inactivation

half-life is 30 min

Please wait a moment until the data is sorted. This message will disappear when the data is sorted.

ORGANIC SOLVENT

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

benzene

85% residual activity

cyclohexane

88% residual activity

dimethyl formamide

dimethyl phthallate

131% residual activity

dimethyl sulfoxide

dioxane

34% v/V, 16% residual activity

Ethanol

heptane

101% residual activity

hexane

74% residual activity

isooctane

106% residual activity

isopropanol

Pyridine

15% v/v, 0.4% residual activity

tetrahydrofuran

additional information

dimethyl formamide

5%, 82% residual activity

dimethyl formamide

15% v/v, 16% residual activity

dimethyl formamide

15% v/v, 16% residual activity

dimethyl formamide

1%, 56% residual activity

dimethyl sulfoxide

5%, 89% residual activity

dimethyl sulfoxide

15% v/v, 16% residual activity

dimethyl sulfoxide

15% v/v, 16% residual activity

dimethyl sulfoxide

1%, 67% residual activity

Ethanol

15% v/v, 48% residual activity

Ethanol

15% v/v, 48% residual activity

isopropanol

15% v/v, 2.5% residual activity

isopropanol

15% v/v, 2.5% residual activity

tetrahydrofuran

15% v/v, 11% residual activity

tetrahydrofuran

15% v/v, 11% residual activity

tetrahydrofuran

1%, 77% residual activity

additional information

the enzyme shows a good tolerance to common organic solvents

additional information

Thermus thermophilus HB27 / ATCC BAA-163 / DSM 7039

the enzyme shows a good tolerance to common organic solvents

Go to Storage Stability Search

Please wait a moment until the data is sorted. This message will disappear when the data is sorted.

STORAGE STABILITY

ORGANISM

UNIPROT

LITERATURE

-20°C, phosphate buffer, pH 7.0, presence of 2-mercaptoethanol and phenylmethyl sulfonylfluoride, stable for at least 3 months

Go to Purification (commentary) Search

Please wait a moment until the data is sorted. This message will disappear when the data is sorted.

PURIFICATION (Commentary)

ORGANISM

UNIPROT

LITERATURE

by heat treatment at 70°C and/or adsorption chromatography on an IDA-Cu2+ support, both methods combined result in 8.8fold purification

Ni Sepharose column chromatography

recombinant enzyme

recombinant enzyme 11fold to homogeneity from Escherichia coli strain BL21(DE3) by heat denaturation of host proteins, anion exchange chromatography and gel filtration

recombinant protein

Strep-Tactin column chromatography

Nocardia fusca AKU 2123

recombinant enzyme

recombinant enzyme

Go to Cloned (commentary) Search

Please wait a moment until the data is sorted. This message will disappear when the data is sorted.

CLONED (Commentary)

ORGANISM

UNIPROT

LITERATURE

expressed in Escherichia coli C43 cells

expressed in Escherichia coli RB791 cells

expressed in Escherichia coli Rosetta (DE3) cells and Arabidopsis thaliana protoplast

expressed in Escherichia coli Rosetta(DE3) cells

expression in Escherichia coli

expression in Escherichia coli strain BL21(DE3)

684583, 701031

expression in Escherichia coli

685644, 685641

expression in Escherichia coli

expression in Escherichia coli

expression in Escherichia coli

show all columns Go to Application Search

Please wait a moment until the data is sorted. This message will disappear when the data is sorted.

APPLICATION

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

synthesis

12 entries

synthesis

production of ethyl (R)-4-chloro-3-hydroxybutanoate using whole recombinant cells of Escherichia coli and 2-propanol as an energy source to regenerate NADH. Yield reaches 36.6 g/l with purity of more than 99% enantiomeric excess and 95.2% conversion

685644

synthesis

synthesis of (R)-1,3-butanediol from its racemate by stereoselective oxidation of the (S)-isomer using (S)-specific secondary alcohol dehydrogenase in whole recombinant Escherichia coli cells. Yield of the (R)-product reaches 72.6 g/l, with a molar recovery yield of 48.4% and an optical purity of 95% enantiomeric excess

685641

synthesis

the enzyme is useful in production of chiral compounds for organic synthesis

synthesis

the immobilized enzyme is utilized in the asymmetric reduction of acetophenone to produce (S)-1-phenylethanol, with an enantiomeric excess of more than 99%

synthesis

synthesis of ethyl (S)-4-chloro-3-hydroxybutanoate in Escherichia coli. Coexpression of carbonyl reductase CRII and a glucose dehydrogenase gives an activity of 15 U/mg protein using ethyl 4-chloro-3-oxobutanoate as a substrate in a water/butyl acetate system. The transformants give a molar yield of 91%, and an optical purity of the (S)-isomer of more than 99% enantiomeric excess

synthesis

the enzyme can be used for stereospecific interconversion of (R)-1-phenylethanol and (S)-1-phenylethanol via the oxoform together with the (R)-specific secondary alcohol dehydrogenase using whole cells as biocatalysts that include the required cofactor regenration system, method, overview. Optically pure secondary alcohols are widely used in pharmaceuticals, flavors, agricultural chemicals and specialty materials

synthesis

Candida albicans

the enzyme catalyzes the asymmetric reduction of ethyl 4-chloro-3-oxobutanoate, the activity is 6.2 U/mg. Using two coexisting recombinant Escherichia coli strains, in which a strain expressing glucose dehydrogenase is used as an NADPH regenerator. An optical purity of 99% (e.e.) and a maximum yield of 1240 mM (S)-4-chloro-3-hydroxybutanoate are obtained, and highest turnover number of 53900 can be achieved without adding extra NADP+/NADPH

synthesis

using recombinant Scr2 in an aqueous-organic solvent system with a substrate fed-batch strategy and a final substrate concentration of 1 M, a yield of 95.3% and e.e. of 99% is obtained after 6-h reaction

Candida albicans ATCC MYA-2876

synthesis

Thermus thermophilus HB27 / ATCC BAA-163 / DSM 7039

the immobilized enzyme is utilized in the asymmetric reduction of acetophenone to produce (S)-1-phenylethanol, with an enantiomeric excess of more than 99%

synthesis

Thermus thermophilus HB27 / ATCC BAA-163 / DSM 7039

the enzyme is useful in production of chiral compounds for organic synthesis

synthesis

Rhodotorula sp. AS2.2241

synthesis

top print hide References Search

Please wait a moment until the data is sorted. This message will disappear when the data is sorted.

REF.

AUTHORS

TITLE

JOURNAL

VOL.

PAGES

YEAR

ORGANISM (UNIPROT)

PUBMED ID

SOURCE

Pennacchio, A.; Pucci, B.; Secundo, F.; La Cara, F.; Rossi, M.; Raia, C.A.

Purification and characterization of a novel recombinant highly enantioselective short-chain NAD(H)-dependent alcohol dehydrogenase from Thermus thermophilus

Appl. Environ. Microbiol.

3949-3958

2008

Thermus thermophilus

18456852

brenda

Abokitse, k.; Hummel, w.

Cloning, sequence analysis, and heterologous expression of the gene encoding a (S)-specific alcohol dehydrogenase from Rhodococcus erythropolis DSM 43297

Appl. Microbiol. Biotechnol.

380-386

2003

Rhodococcus erythropolis (Q6YBW1)

12719937

brenda

Hoeffken, H.W.; Duong, M.; Friedrich, T.; Breuer, M.; Hauer, B.; Reinhardt, R.; Rabus, R.; Heider, J.

Crystal structure and enzyme kinetics of the (S)-specific 1-phenylethanol dehydrogenase of the denitrifying bacterium strain EbN1

Biochemistry

82-93

2006

uncultured bacterium, uncultured bacterium EbN1

16388583

brenda

685641

Yamamoto, H.; Matsuyama, A.; Kobayashi, Y.

Synthesis of (R)-1,3-butanediol by enantioselective oxidation using whole recombinant Escherichia coli cells expressing (S)-specific secondary alcohol dehydrogenase

Biosci. Biotechnol. Biochem.

925-927

2002

Candida parapsilosis

brenda

Xie, S.-X.; Ogawa, J.; Shimizu, S.

NAD+-Dependent (S)-specific secondary alcohol dehydrogenase involved in stereoinversion of 3-pentyn-2ol catalyzed by Nocardia fusca AKU 2123

Biosci. Biotechnol. Biochem.

1721-1729

1999

Nocardia fusca AKU 2123

10586501

brenda

685644

Yamamoto, H.; Matsuyama, A.; Kobayashi, Y.

Synthesis of ethyl (R)-4-chloro-3-hydroxybutanoate with recombinant Escherichia coli cells expressing (S)-specific secondary alcohol dehydrogenase

Biosci. Biotechnol. Biochem.

481-483

2002

Candida parapsilosis

11999433

brenda

Soni, P.; Kansal, H.; Banerjee, U.C.

Purification and characterization of an enantioselective carbonyl reductase from Candida viswanathii MTCC 5158

Process Biochem.

1632-1640

2007

Candida viswanathii, Candida viswanathii MTCC 5158

brenda

Pal, S.; Park, D.H.; Plapp, B.V.

Activity of yeast alcohol dehydrogenases on benzyl alcohols and benzaldehydes: characterization of ADH1 from Saccharomyces carlsbergensis and transition state analysis

Chem. Biol. Interact.

178

16-23

2009

Saccharomyces cerevisiae, Saccharomyces pastorianus, Saccharomyces pastorianus Y379-50

19022233

brenda

Pennacchio, A.; Esposito, L.; Zagari, A.; Rossi, M.; Raia, C.A.

Role of Tryptophan 95 in substrate specificity and structural stability of Sulfolobus solfataricus alcohol dehydrogenase

Extremophiles

751-761

2009

Saccharolobus solfataricus

19588068

brenda

Rocha-Martin, J.; Vega, D.; Cabrera, Z.; Bolivar, J.; Fernandez-Lafuente, R.; Berenguer, J.; Guisan, J.

Purification, immobilization and stabilization of a highly enantioselective alcohol dehydrogenase from Thermus thermophilus HB27 cloned in E. coli

Process Biochem.

1004-1012

2009

Thermus thermophilus, Thermus thermophilus HB27 / ATCC BAA-163 / DSM 7039

brenda

Protsko, C.; Vieille, C.; Laivenieks, M.; Prasad, L.; Sanders, D.A.; Delbaere, L.T.

Crystallization and preliminary X-ray diffraction analysis of the Thermoanaerobacter ethanolicus secondary alcohol dehydrogenase I86A mutant

Acta Crystallogr. Sect. F

831-833

2010

Thermoanaerobacter ethanolicus (P77990)

20606285

brenda

Cao, H.; Mi, L.; Ye, Q.; Zang, G.; Yan, M.; Wang, Y.; Zhang, Y.; Li, X.; Xu, L.; Xiong, J.; Ouyang, P.; Ying, H.

Purification and characterization of a novel NADH-dependent carbonyl reductase from Pichia stipitis involved in biosynthesis of optically pure ethyl (S)-4-chloro-3-hydroxybutanoate

Biores. Technol.

102

1733-1739

2011

Scheffersomyces stipitis (A3GF05)

20933386

brenda

Li, Y.; Xu, J.; Xu, Y.

Deracemization of aryl secondary alcohols via enantioselective oxidation and stereoselective reduction with tandem whole-cell biocatalysts

J. Mol. Catal. B

48-52

2010

Rhodotorula sp., Rhodotorula sp. AS2.2241

brenda

You, Z.Y.; Liu, Z.Q.; Zheng, Y.G.

Characterization of a newly synthesized carbonyl reductase and construction of a biocatalytic process for the synthesis of ethyl (S)-4-chloro-3-hydroxybutanoate with high space-time yield

Appl. Microbiol. Biotechnol.

1671-1680

2014

Candida parapsilosis (D5G304)

23793261

brenda

Dudzik, A.; Snoch, W.; Borowiecki, P.; Opalinska-Piskorz, J.; Witko, M.; Heider, J.; Szaleniec, M.

Asymmetric reduction of ketones and beta-keto esters by (S)-1-phenylethanol dehydrogenase from denitrifying bacterium Aromatoleum aromaticum

Appl. Microbiol. Biotechnol.

5055-5069

2015

Aromatoleum aromaticum, Aromatoleum aromaticum EbN1

25549618

brenda

Cai, P.; An, M.; Xu, S.; Yan, M.; Hao, N.; Li, Y.; Xu, L.

Asymmetric synthesis of (S)-4-chloro-3-hydroxybutanoate by sorbose reductase from Candida albicans with two co-existing recombinant Escherichia coli strains

Biosci. Biotechnol. Biochem.

1090-1093

2015

Candida albicans (P87219), Candida albicans ATCC MYA-2876 (P87219)

25765951

brenda

Xu, G.C.; Shang, Y.P.; Yu, H.L.; Xu, J.H.

Identification of key residues in Debaryomyces hansenii carbonyl reductase for highly productive preparation of (S)-aryl halohydrins

Chem. Commun. (Camb.)

15728-15731

2015

Debaryomyces hansenii

26364768

brenda

760341

Schmermund, L.; Reischauer, S.; Bierbaumer, S.; Winkler, C.K.; Diaz-Rodriguez, A.; Edwards, L.J.; Kara, S.; Mielke, T.; Cartwright, J.; Grogan, G.; Pieber, B.; Kroutil, W.

Chromoselective photocatalysis enables stereocomplementary biocatalytic pathways

Angew. Chem. Int. Ed. Engl.

6965-6969

2021

Rhodococcus ruber

33529432

brenda

Koesoema, A.A.; Sugiyama, Y.; Sriwong, K.T.; Xu, Z.; Verina, S.; Standley, D.M.; Senda, M.; Senda, T.; Matsuda, T.

Reversible control of enantioselectivity by the length of ketone substituent in biocatalytic reduction

Appl. Microbiol. Biotechnol.

103

9529-9541

2019

Geotrichum candidum (M5A8V4), Geotrichum candidum, Geotrichum candidum NBRC 4597 (M5A8V4)

31720775

brenda

Zhou, Y.; Peng, Q.; Zhang, L.; Cheng, S.; Zeng, L.; Dong, F.; Yang, Z.

Characterization of enzymes specifically producing chiral flavor compounds (R)- and (S)-1-phenylethanol from tea (Camellia sinensis) flowers

Food Chem.

280

27-33

2019

Camellia sinensis (A0A494WD27), Camellia sinensis

30642496

brenda