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Information on EC 1.1.1.311 - (S)-1-phenylethanol dehydrogenase
for references in articles please use BRENDA:EC1.1.1.311
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EC Tree 1 Oxidoreductases
1.1 Acting on the CH-OH group of donors
1.1.1 With NAD+ or NADP+ as acceptor
1.1.1.311 (S)-1-phenylethanol dehydrogenase
IUBMB Comments
The enzyme is involved in degradation of ethylbenzene.
The enzyme appears in viruses and cellular organisms
- 1.1.1.311
-
s-1-phenylethanol
- acetophenone
-
denitrifying
-
racemic
- 1-phenyl-1,2-ethanediol
- 2-hydroxyacetophenone
- ethylbenzene
-
enantioselective
-
enantiomeric
-
parapsilosis
- molybdenum
-
gibsonii
-
aromatoleum
- synthesis
-
s-enantiomer
-
kurthia
- isopropanol
- azoarcus
-
gluconobacter
-
cosubstrate
- aromaticum
-
cctcc
-
stereoinversion
-
oxydans
showSynonyms
(s)-ped, (s)-1-phenylethanol dehydrogenase, more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
(S)-PED
PED
PedH
prelog-specific NADH-dependent (S)-1-phenylethanol dehydrogenase
prelog-specific NADH-dependent (S)-1-phenylethanol dehydrogenase
-
prelog-specific NADH-dependent (S)-1-phenylethanol dehydrogenase
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
(S)-1-phenylethanol + NAD+ = acetophenone + NADH + H+
-
-
-
-
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PATHWAY SOURCE
PATHWAYS
MetaCyc
ethylbenzene degradation (anaerobic)
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SYSTEMATIC NAME
IUBMB Comments
(S)-1-phenylethanol:NAD+ oxidoreductase
The enzyme is involved in degradation of ethylbenzene.
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
2,2-dichloroacetophenone + NADH + H+
? + NAD+
Substrates: -
Products: -
Products: -
r
2-chloroacetophenone + NADH + H+
? + NAD+
Substrates: -
Products: -
Products: -
r
4'-bromoacetophenone + NADH + H+
(S)-4-(1-bromoethyl)phenol + NAD+
Substrates: -
Products: -
Products: -
r
4'-chloroacetophenone + NADH + H+
(S)-4-(1-chloroethyl)phenol + NAD+
Substrates: -
Products: -
Products: -
r
4'-ethylacetophenone + NADH + H+
? + NAD+
Substrates: -
Products: -
Products: -
r
4'-fluoroacetophenone + NADH + H+
(S)-4-(1-fluoroethyl)phenol + NAD+
Substrates: -
Products: -
Products: -
r
4'-methoxyacetophenone + NADH + H+
(S)-4-(1-methoxyethyl)phenol + NAD+
Substrates: -
Products: -
Products: -
r
4'-nitroacetophenone + NADH + H+
(S)-4-(1-nitroethyl)phenol + NAD+
Substrates: -
Products: -
Products: -
r
4-acetylpyridine + NADH + H+
? + NAD+
Substrates: -
Products: -
Products: -
r
methyl 4-(4-bromophenyl)-4-oxobutanoate + NADH + H+
(S)-methyl 4-(4-bromophenyl)-4-hydroxybutanoate + (S)-(-)-5-(4-bromophenyl)dihydrofuran-2(3H)-one + NAD+
methyl 4-(4-chlorophenyl)-4-oxobutanoate + NADH + H+
(S)-methyl 4-(4-chlorophenyl)-4-hydroxybutanoate + (S)-(-)-5-(4-chlorophenyl)dihydrofuran-2(3H)-one + NAD+
methyl 4-(4-fluorophenyl)-4-oxobutanoate + NADH + H+
(S)-methyl 4-(4-fluorophenyl)-4-hydroxybutanoate + (S)-(-)-5-(4-fluorophenyl)dihydrofuran-2(3H)-one + NAD+
Substrates: -
Products: -
Products: -
r
methyl 4-(4-methoxyphenyl)-4-oxobutanoate + NADH + H+
(S)-methyl 4-(4-methoxyphenyl)-4-hydroxybutanoate + (S)-(-)-5-(4-methoxyphenyl)dihydrofuran-2(3H)-one + NAD+
Substrates: -
Products: -
Products: -
r
methyl 4-(4-methylphenyl)-4-oxobutanoate + NADH + H+
(S)-methyl 4-(4-methylphenyl)-4-hydroxybutanoate + (S)-(-)-5-(4-methylphenyl)dihydrofuran-2(3H)-one + NAD+
Substrates: -
Products: -
Products: -
r
methyl 4-fluorobenzoylacetate + NADH + H+
(S)-methyl 3-(4-fluorophenyl)-3-hydroxypropanoate + NAD+
Substrates: -
Products: 100% enantiomertic excess
Products: 100% enantiomertic excess
?
methyl 4-oxo-4-(pyren-1-yl)butanoate + NADH + H+
(S)-methyl 4-hydroxy-4-(pyren-1-yl)butanoate + (S)-(-)-5-(pyren-1-yl)oxolan-2-one + NAD+
Substrates: -
Products: -
Products: -
r
methyl 4-oxo-4-phenylbutanoate + NADH + H+
(S)-methyl 4-hydroxy-4-phenylbutanoate + (S)-(-)-5-phenyldihydrofuran-2(3H)-one + NAD+
Substrates: -
Products: -
Products: -
r
(S)-1-phenylethanol + NAD+
acetophenone + NADH + H+
Substrates: -
Products: -
Products: -
r
(S)-1-phenylethanol + NAD+
acetophenone + NADH + H+
-
Substrates: -
Products: -
Products: -
r
(S)-1-phenylethanol + NAD+
acetophenone + NADH + H+
Substrates: -
Products: -
Products: -
r
(S)-1-phenylethanol + NAD+
acetophenone + NADH + H+
-
Substrates: -
Products: -
Products: -
r
(S)-1-phenylethanol + NAD+
acetophenone + NADH + H+
Substrates: -
Products: -
Products: -
r
(S)-1-phenylethanol + NAD+
acetophenone + NADH + H+
-
Substrates: no activity with NADP+. No activity with (R)-1-phenylethanol
Products: -
Products: -
r
(S)-1-phenylethanol + NAD+
acetophenone + NADH + H+
-
Substrates: -
Products: -
Products: -
r
(S)-1-phenylethanol + NAD+
acetophenone + NADH + H+
-
Substrates: no activity with NADP+. No activity with (R)-1-phenylethanol
Products: -
Products: -
r
(S)-1-phenylethanol + NAD+
acetophenone + NADH + H+
Substrates: -
Products: -
Products: -
r
2,2,2-trifluoroacetophenone + NADH + H+
(S)-1-phenyl-2,2,2-trifluoroethan-1-ol + NAD+
Substrates: -
Products: 100% enantiomertic excess
Products: 100% enantiomertic excess
?
2,2,2-trifluoroacetophenone + NADH + H+
(S)-1-phenyl-2,2,2-trifluoroethan-1-ol + NAD+
Substrates: -
Products: 100% enantiomertic excess
Products: 100% enantiomertic excess
?
2,4'-dichloroacetophenone + NADH + H+
(S)-2-chloro-1-(4-chloro-phenyl)-ethanol + NAD+
Substrates: -
Products: 100% enantiomeric excess
Products: 100% enantiomeric excess
?
2,4'-dichloroacetophenone + NADH + H+
(S)-2-chloro-1-(4-chloro-phenyl)-ethanol + NAD+
Substrates: -
Products: 100% enantiomeric excess
Products: 100% enantiomeric excess
?
2-acetylpyridine + NADH + H+
? + NAD+
Substrates: -
Products: -
Products: -
r
2-acetylpyridine + NADH + H+
? + NAD+
Substrates: -
Products: -
Products: -
r
4'-hydroxyacetophenone + NADH + H+
(S)-4-(1-hydroxyethyl)phenol + NAD+
Substrates: -
Products: -
Products: -
r
4'-hydroxyacetophenone + NADH + H+
(S)-4-(1-hydroxyethyl)phenol + NAD+
Substrates: -
Products: 90% enantiomeric excess
Products: 90% enantiomeric excess
?
4'-hydroxyacetophenone + NADH + H+
(S)-4-(1-hydroxyethyl)phenol + NAD+
Substrates: -
Products: -
Products: -
r
4-acetylbiphenyl + NADH + H+
(S)-1-(biphenyl-4-yl)ethanol + NAD+
Substrates: -
Products: 100% enantiomeric excess
Products: 100% enantiomeric excess
?
4-acetylbiphenyl + NADH + H+
(S)-1-(biphenyl-4-yl)ethanol + NAD+
Substrates: -
Products: 100% enantiomeric excess
Products: 100% enantiomeric excess
?
4-aminoacetophenone + NADH + H+
1-(4-aminophenyl)ethanol + NAD+
Substrates: -
Products: racemic product
Products: racemic product
?
4-aminoacetophenone + NADH + H+
1-(4-aminophenyl)ethanol + NAD+
Substrates: -
Products: racemic product
Products: racemic product
?
acetophenone + NADH + H+
(S)-1-phenylethanol + NAD+
Substrates: -
Products: -
Products: -
r
acetophenone + NADH + H+
(S)-1-phenylethanol + NAD+
-
Substrates: -
Products: -
Products: -
r
acetophenone + NADH + H+
(S)-1-phenylethanol + NAD+
Substrates: -
Products: 100% enantiomeric excess
Products: 100% enantiomeric excess
?
acetophenone + NADH + H+
(S)-1-phenylethanol + NAD+
Substrates: -
Products: 100% enantiomeric excess
Products: 100% enantiomeric excess
?
acetophenone + NADH + H+
(S)-1-phenylethanol + NAD+
Substrates: -
Products: -
Products: -
r
methyl 4-(4-bromophenyl)-4-oxobutanoate + NADH + H+
(S)-methyl 4-(4-bromophenyl)-4-hydroxybutanoate + (S)-(-)-5-(4-bromophenyl)dihydrofuran-2(3H)-one + NAD+
Substrates: -
Products: -
Products: -
r
methyl 4-(4-bromophenyl)-4-oxobutanoate + NADH + H+
(S)-methyl 4-(4-bromophenyl)-4-hydroxybutanoate + (S)-(-)-5-(4-bromophenyl)dihydrofuran-2(3H)-one + NAD+
Substrates: -
Products: -
Products: -
r
methyl 4-(4-chlorophenyl)-4-oxobutanoate + NADH + H+
(S)-methyl 4-(4-chlorophenyl)-4-hydroxybutanoate + (S)-(-)-5-(4-chlorophenyl)dihydrofuran-2(3H)-one + NAD+
Substrates: -
Products: -
Products: -
r
methyl 4-(4-chlorophenyl)-4-oxobutanoate + NADH + H+
(S)-methyl 4-(4-chlorophenyl)-4-hydroxybutanoate + (S)-(-)-5-(4-chlorophenyl)dihydrofuran-2(3H)-one + NAD+
Substrates: -
Products: -
Products: -
r
additional information
?
-
Substrates: the enzyme is used for chemoenzymatic synthesis of enantiomerically enriched (S)- and (R)-gamma-aryl-gamma-butyrolactones, whereby the key step is an enzyme-catalyzed stereoselective reduction of methyl 4-oxo-4-arylbutanoates, (S)-PED-catalyzed bioreduction
Products: -
Products: -
-
additional information
?
-
Substrates: the low pH cluster model is used to investigate kinetics and thermodynamics of the PEDH catalysed reductions of ketones to alcohols. The optimization of enzyme-ketone complexes (ES), transitions states (TS) as well as the enzyme-alcohol complexes (EP) are obtained for acetophenone and its structural analogues: 2,2-di-chloroacetophenone, 2-chloroacetophenone, 4'-nitroacetophenone, 4'-hydroxyacetophenone, 4'-methoxyacetophenone, 4'-ethylacetophenone, 4'-fluoroacetophenone, 4'-chloroacetophenone, 4'-bromoacetophenone, and 2-acetyl- and 4-acetylpyridine. Analysis of transition states for acetophenone derivatives, kinetic and thermodynamic analysis, overview
Products: -
Products: -
-
additional information
?
-
-
Substrates: the low pH cluster model is used to investigate kinetics and thermodynamics of the PEDH catalysed reductions of ketones to alcohols. The optimization of enzyme-ketone complexes (ES), transitions states (TS) as well as the enzyme-alcohol complexes (EP) are obtained for acetophenone and its structural analogues: 2,2-di-chloroacetophenone, 2-chloroacetophenone, 4'-nitroacetophenone, 4'-hydroxyacetophenone, 4'-methoxyacetophenone, 4'-ethylacetophenone, 4'-fluoroacetophenone, 4'-chloroacetophenone, 4'-bromoacetophenone, and 2-acetyl- and 4-acetylpyridine. Analysis of transition states for acetophenone derivatives, kinetic and thermodynamic analysis, overview
Products: -
Products: -
-
additional information
?
-
Substrates: the enzyme is used for chemoenzymatic synthesis of enantiomerically enriched (S)- and (R)-gamma-aryl-gamma-butyrolactones, whereby the key step is an enzyme-catalyzed stereoselective reduction of methyl 4-oxo-4-arylbutanoates, (S)-PED-catalyzed bioreduction
Products: -
Products: -
-
additional information
?
-
Substrates: the low pH cluster model is used to investigate kinetics and thermodynamics of the PEDH catalysed reductions of ketones to alcohols. The optimization of enzyme-ketone complexes (ES), transitions states (TS) as well as the enzyme-alcohol complexes (EP) are obtained for acetophenone and its structural analogues: 2,2-di-chloroacetophenone, 2-chloroacetophenone, 4'-nitroacetophenone, 4'-hydroxyacetophenone, 4'-methoxyacetophenone, 4'-ethylacetophenone, 4'-fluoroacetophenone, 4'-chloroacetophenone, 4'-bromoacetophenone, and 2-acetyl- and 4-acetylpyridine. Analysis of transition states for acetophenone derivatives, kinetic and thermodynamic analysis, overview
Products: -
Products: -
-
additional information
?
-
-
Substrates: no activity with ethanol, 1-propanol, 1-butanol, 2-phenylethanol or benzyl alcohol
Products: -
Products: -
?
additional information
?
-
-
Substrates: no activity with ethanol, 1-propanol, 1-butanol, 2-phenylethanol or benzyl alcohol
Products: -
Products: -
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
(S)-1-phenylethanol + NAD+
acetophenone + NADH + H+
Substrates: -
Products: -
Products: -
r
(S)-1-phenylethanol + NAD+
acetophenone + NADH + H+
-
Substrates: -
Products: -
Products: -
r
(S)-1-phenylethanol + NAD+
acetophenone + NADH + H+
Substrates: -
Products: -
Products: -
r
(S)-1-phenylethanol + NAD+
acetophenone + NADH + H+
-
Substrates: -
Products: -
Products: -
r
(S)-1-phenylethanol + NAD+
acetophenone + NADH + H+
-
Substrates: -
Products: -
Products: -
r
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
-
the presence of 10 mM EDTA (10 mM), 1 mM pyrazole or 1 mM 1,10-phenanthroline in enzyme assays does not affect the activity, indicating that the enzyme does not contain easily accessible bivalent metal ions. (S)-1-phenylethanol oxidation is not inhibited by 0.1 mM 5,5'-dithiobis-(2-nitrobenzoic acid), 1 mM 4-hydroxymercuribenzoic acid or 1 mM N-ethylmaleimide, indicating that no accessible cysteine residues are required for catalysis
-
(R)-1-phenylethanol
0.05 mM, 50% inhibition of acetophenone reduction activity
(R)-1-phenylethanol
-
oxidation of (S)-1-phenylethanol is completely inhibited in the presence of tenfold higher concentrations of (R)-1-phenylethanol
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
kinetic and thermodynamic analysis, isothermal titration calorimetry, molecular modelling, overview
-
additional information
additional information
-
kinetic and thermodynamic analysis, isothermal titration calorimetry, molecular modelling, overview
-
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
30
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pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
Highest Expressing Human Cell Lines
Cell Line LinksPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
additional information
evolution
PEDH belongs to the short-chain dehydrogenase/reductase superfamily
evolution
-
PEDH belongs to the short-chain dehydrogenase/reductase superfamily
-
additional information
the reaction mechanism of ketone reduction by short chain dehydrogenase/reductase, (S)-1-phenylethanol dehydrogenase from Aromatoleum aromaticum, is studied with DFT methods using cluster model approach
additional information
-
the reaction mechanism of ketone reduction by short chain dehydrogenase/reductase, (S)-1-phenylethanol dehydrogenase from Aromatoleum aromaticum, is studied with DFT methods using cluster model approach
additional information
-
the reaction mechanism of ketone reduction by short chain dehydrogenase/reductase, (S)-1-phenylethanol dehydrogenase from Aromatoleum aromaticum, is studied with DFT methods using cluster model approach
-
Show AA Sequence and Transmembrane Helices (235 entries)
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Please use the AA Sequence and Transmembrane Helices Search for a specific query.
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
homotetramer
tetramer
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
docking simulation for prochiral ketone and beta-keto ester substrates
sitting drop method in a buffer containing 12-18% PEG 8000, 0.05 M potassium phosphate, pH 7.5 and 3% 2-methyl-2,4-pentanediol. The structure of the apo-form of the enzyme is solved with a resolution at 2.1 A. The enzyme soaked with NAD+ and the inhibitor (R)-1-phenylethanol forms a different crystal form containing two subunits in the asymmetric unit
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
synthesis
synthesis
application of (S)-1-phenylethanol dehydrogenase for asymmetric reduction of 42 prochiral ketones and 11 beta-keto esters to enantiopure secondary alcohols. The conversions are carried out in a batch reactor using recombinant Escherichia coli as whole-cell catalysts and isopropanol as reaction solvent and cosubstrate for NADH recovery. Ketones are converted to the respective secondary alcohols with excellent enantiomeric excesses and high productivities
synthesis
the enzyme recombinantly expressed in Escherichia coli is used for chemoenzymatic synthesis of enantiomerically enriched (S)- and (R)-gamma-aryl-gamma-butyrolactones, whereby the key step is an enzyme-catalyzed stereoselective reduction of methyl 4-oxo-4-arylbutanoates, (S)-PED-catalyzed bioreduction in preparative scale
synthesis
-
application of (S)-1-phenylethanol dehydrogenase for asymmetric reduction of 42 prochiral ketones and 11 beta-keto esters to enantiopure secondary alcohols. The conversions are carried out in a batch reactor using recombinant Escherichia coli as whole-cell catalysts and isopropanol as reaction solvent and cosubstrate for NADH recovery. Ketones are converted to the respective secondary alcohols with excellent enantiomeric excesses and high productivities
-
synthesis
-
the enzyme recombinantly expressed in Escherichia coli is used for chemoenzymatic synthesis of enantiomerically enriched (S)- and (R)-gamma-aryl-gamma-butyrolactones, whereby the key step is an enzyme-catalyzed stereoselective reduction of methyl 4-oxo-4-arylbutanoates, (S)-PED-catalyzed bioreduction in preparative scale
-
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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
45
82-93
2006
Azoarcus sp. (Q5P5I4), Azoarcus sp. EbN1 (Q5P5I4)
brenda
Kniemeyer, O.; Heider, J.
(S)-1-Phenylethanol dehydrogenase of Azoarcus sp. strain EbN1, an enzyme of anaerobic ethylbenzene catabolism
Arch. Microbiol.
176
129-135
2001
Azoarcus sp., Azoarcus sp. EbN1
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.
99
5055-5069
2015
Aromatoleum aromaticum (Q5P5I4), Aromatoleum aromaticum, Aromatoleum aromaticum EbN1 (Q5P5I4)
brenda
Borowiecki, P.; Telatycka, N.; Tataruch, M.; Zadlo-Dobrowolska, A.; Reiter, T.; Schuehle, K.; Heider, J.; Szaleniec, M.; Kroutil, W.
Biocatalytic asymmetric reduction of gamma-keto esters to access optically active gamma-aryl-gamma-butyrolactones
Adv. Synth. Catal.
362
2012-2029
2020
Aromatoleum aromaticum (Q5P5I4), Aromatoleum aromaticum EbN1 (Q5P5I4)
-
brenda
Stawoska, I.; Dudzik, A.; Wasylewski, M.; Jemiola-Rzeminska, M.; Skoczowski, A.; Strzalka, K.; Szaleniec, M.
DFT-based prediction of reactivity of short-chain alcohol dehydrogenase
J. Comput. Aided Mol. Des.
31
587-602
2017
Aromatoleum aromaticum (Q5P5I4), Aromatoleum aromaticum, Aromatoleum aromaticum EbN1 (Q5P5I4)
brenda
EXTERNAL LINKS (specific for EC-Number 1.1.1.311)
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Release 2023.1 (January 2023)
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