Information on EC 1.1.1.311 - (S)-1-phenylethanol dehydrogenase

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The expected taxonomic range for this enzyme is: Rhodocyclaceae

EC NUMBER
COMMENTARY hide
1.1.1.311
-
RECOMMENDED NAME
GeneOntology No.
(S)-1-phenylethanol dehydrogenase
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
(S)-1-phenylethanol + NAD+ = acetophenone + NADH + H+
show the reaction diagram
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-
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
ethylbenzene degradation (anaerobic)
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Ethylbenzene degradation
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Microbial metabolism in diverse environments
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SYSTEMATIC NAME
IUBMB Comments
(S)-1-phenylethanol:NAD+ oxidoreductase
The enzyme is involved in degradation of ethylbenzene.
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
(S)-1-phenylethanol + NAD+
acetophenone + NADH + H+
show the reaction diagram
additional information
?
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
(S)-1-phenylethanol + NAD+
acetophenone + NADH + H+
show the reaction diagram
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
NAD+
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no activity with NADP+
NADH
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INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
(R)-1-phenylethanol
additional information
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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
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0016
(S)-1-phenylethanol
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pH 8, 30C
0.001
acetophenone
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pH 8, 30C
0.051
NAD+
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pH 8, 30C
0.0033
NADH
-
pH 8, 30C
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2
(S)-1-phenylethanol
Azoarcus sp.
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pH 8, 30C
1.6
acetophenone
Azoarcus sp.
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pH 8, 30C
2
NAD+
Azoarcus sp.
-
pH 8, 30C
1.6
NADH
Azoarcus sp.
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pH 8, 30C
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
3.8
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pH 8, 30C
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4
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reduction of acetophenone
7.8
assay at
8
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oxidation of (S)-1-phenylethanol
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
25
assay at
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.6
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two-dimensional gel electrophoresis
PDB
SCOP
CATH
ORGANISM
UNIPROT
Aromatoleum aromaticum (strain EbN1)
Aromatoleum aromaticum (strain EbN1)
Aromatoleum aromaticum (strain EbN1)
Aromatoleum aromaticum (strain EbN1)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
50000
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gel filtration
93000
gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
tetramer
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
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
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
overexpressed in Escherichia coli