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Information on EC 1.1.1.311 - (S)-1-phenylethanol dehydrogenase and Organism(s) Aromatoleum aromaticum and UniProt Accession Q5P5I4
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1.1.1.311 (S)-1-phenylethanol dehydrogenaseIUBMB Comments
The enzyme is involved in degradation of ethylbenzene.
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Word Map
- 1.1.1.311
-
s-1-phenylethanol
- acetophenone
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denitrifying
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racemic
- 1-phenyl-1,2-ethanediol
- 2-hydroxyacetophenone
- ethylbenzene
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enantioselective
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enantiomeric
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parapsilosis
- molybdenum
-
gibsonii
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aromatoleum
- synthesis
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s-enantiomer
-
kurthia
- isopropanol
- azoarcus
-
gluconobacter
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cosubstrate
- aromaticum
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cctcc
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stereoinversion
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oxydans
The taxonomic range for the selected organisms is: Aromatoleum aromaticum
The enzyme appears in selected viruses and cellular organisms
The enzyme appears in selected viruses and cellular organisms
Synonyms
(s)-ped, (s)-1-phenylethanol dehydrogenase, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
prelog-specific NADH-dependent (S)-1-phenylethanol dehydrogenase
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PATHWAY SOURCE
PATHWAYS
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-
SYSTEMATIC NAME
IUBMB Comments
(S)-1-phenylethanol:NAD+ oxidoreductase
The enzyme is involved in degradation of ethylbenzene.
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
2,2,2-trifluoroacetophenone + NADH + H+
(S)-1-phenyl-2,2,2-trifluoroethan-1-ol + NAD+
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100% enantiomertic excess
-
?
2,4'-dichloroacetophenone + NADH + H+
(S)-2-chloro-1-(4-chloro-phenyl)-ethanol + NAD+
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100% enantiomeric excess
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?
4'-bromoacetophenone + NADH + H+
(S)-4-(1-bromoethyl)phenol + NAD+
-
-
-
r
4'-chloroacetophenone + NADH + H+
(S)-4-(1-chloroethyl)phenol + NAD+
-
-
-
r
4'-fluoroacetophenone + NADH + H+
(S)-4-(1-fluoroethyl)phenol + NAD+
-
-
-
r
4'-methoxyacetophenone + NADH + H+
(S)-4-(1-methoxyethyl)phenol + NAD+
-
-
-
r
4'-nitroacetophenone + NADH + H+
(S)-4-(1-nitroethyl)phenol + NAD+
-
-
-
r
4-acetylbiphenyl + NADH + H+
(S)-1-(biphenyl-4-yl)ethanol + NAD+
-
100% enantiomeric excess
-
?
4-aminoacetophenone + NADH + H+
1-(4-aminophenyl)ethanol + NAD+
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racemic product
-
?
methyl 4-(4-bromophenyl)-4-oxobutanoate + NADH + H+
(S)-methyl 4-(4-bromophenyl)-4-hydroxybutanoate + (S)-(-)-5-(4-bromophenyl)dihydrofuran-2(3H)-one + NAD+
-
-
-
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+
-
-
-
r
methyl 4-(4-fluorophenyl)-4-oxobutanoate + NADH + H+
(S)-methyl 4-(4-fluorophenyl)-4-hydroxybutanoate + (S)-(-)-5-(4-fluorophenyl)dihydrofuran-2(3H)-one + NAD+
-
-
-
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+
-
-
-
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+
-
-
-
r
methyl 4-fluorobenzoylacetate + NADH + H+
(S)-methyl 3-(4-fluorophenyl)-3-hydroxypropanoate + NAD+
-
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+
-
-
-
r
methyl 4-oxo-4-phenylbutanoate + NADH + H+
(S)-methyl 4-hydroxy-4-phenylbutanoate + (S)-(-)-5-phenyldihydrofuran-2(3H)-one + NAD+
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-
-
r
(S)-1-phenylethanol + NAD+
acetophenone + NADH + H+
-
-
-
r
4'-hydroxyacetophenone + NADH + H+
(S)-4-(1-hydroxyethyl)phenol + NAD+
-
-
-
r
4'-hydroxyacetophenone + NADH + H+
(S)-4-(1-hydroxyethyl)phenol + NAD+
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90% enantiomeric excess
-
?
acetophenone + NADH + H+
(S)-1-phenylethanol + NAD+
-
-
-
r
acetophenone + NADH + H+
(S)-1-phenylethanol + NAD+
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100% enantiomeric excess
-
?
additional information
?
-
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
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-
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additional information
?
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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
-
-
-
additional information
?
-
-
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
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
(S)-1-phenylethanol + NAD+
acetophenone + NADH + H+
-
-
-
r
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
kinetic and thermodynamic analysis, isothermal titration calorimetry, molecular modelling, overview
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additional information
additional information
-
kinetic and thermodynamic analysis, isothermal titration calorimetry, molecular modelling, overview
-
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
30
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
PEDH belongs to the short-chain dehydrogenase/reductase superfamily
additional information
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
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
docking simulation for prochiral ketone and beta-keto ester substrates
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
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
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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)
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)
-
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)
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