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

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The expected taxonomic range for this enzyme is: Rhodocyclaceae

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EC NUMBER
COMMENTARY hide
1.1.1.311
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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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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
Ethylbenzene degradation
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ethylbenzene degradation (anaerobic)
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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.
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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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
?
-
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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
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
NAD+
-
no activity with NADP+
NADH
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-
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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, 30°C
0.001
acetophenone
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pH 8, 30°C
0.051
NAD+
-
pH 8, 30°C
0.0033
NADH
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pH 8, 30°C
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2
(S)-1-phenylethanol
Azoarcus sp.
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pH 8, 30°C
1.6
acetophenone
Azoarcus sp.
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pH 8, 30°C
2
NAD+
Azoarcus sp.
-
pH 8, 30°C
1.6
NADH
Azoarcus sp.
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pH 8, 30°C
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
3.8
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pH 8, 30°C
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4
-
reduction of acetophenone
7.8
assay at
8
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oxidation of (S)-1-phenylethanol
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
25
assay at
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pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.6
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two-dimensional gel electrophoresis
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PDB
SCOP
CATH
ORGANISM
UNIPROT
Aromatoleum aromaticum (strain EbN1)
Aromatoleum aromaticum (strain EbN1)
Aromatoleum aromaticum (strain EbN1)
Aromatoleum aromaticum (strain EbN1)
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
25500
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2 * 25500, SDS-PAGE
27000
4 * 27000
50000
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gel filtration
93000
gel filtration
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SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
tetramer
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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
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
overexpressed in Escherichia coli
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LINKS TO OTHER DATABASES (specific for EC-Number 1.1.1.311)
ExplorEnz
ExPASy
KEGG
MetaCyc
SABIO-RK
NCBI: PubMed, Protein, Nucleotide, Structure, Genome, OMIM
IUBMB Enzyme Nomenclature
PROSITE Database of protein families and domains
SYSTERS
Protein Mutant Database
InterPro (database of protein families, domains and functional sites)