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Information on EC 1.5.1.18 - ephedrine dehydrogenase
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EC Tree
1.5.1.18 ephedrine dehydrogenaseIUBMB Comments
The product immediately hydrolyses to methylamine and 1-hydroxy-1-phenylpropan-2-one. Acts on a number of related compounds including (-)-sympatol, (+)-pseudoephedrine and (+)-norephedrine.
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The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
Synonyms
ephedrine dehydrogenase, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
(-)-ephedrine + NAD+ = (R)-2-methylimino-1-phenylpropan-1-ol + NADH + H+
-
-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dehydrogenation
-
-
-
-
oxidation
-
-
-
-
redox reaction
-
-
-
-
reduction
-
-
-
-
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PATHWAY SOURCE
PATHWAYS
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SYSTEMATIC NAME
IUBMB Comments
(-)-ephedrine:NAD+ 2-oxidoreductase
The product immediately hydrolyses to methylamine and 1-hydroxy-1-phenylpropan-2-one. Acts on a number of related compounds including (-)-sympatol, (+)-pseudoephedrine and (+)-norephedrine.
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CAS REGISTRY NUMBER
COMMENTARY
73508-06-2
-
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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
(-)-ephedrine + NAD+
(R)-2-methylimino-1-phenylpropan-1-ol + NADH + H+
-
-
-
?
1-phenylpropan-1,2-dione + NADH + H+
(R)-phenylacetylcarbinol + NAD+
high activity
-
-
r
ethyl 2-chlorobenzyolacetate + NADH + H+
?
low activity
-
-
r
(+)-norephedrine + NAD+
2-imino-1-hydroxy-1-phenylpropane + NADH
-
higher rate than (-)-ephedrine
-
-
?
(+)-norephedrine + NAD+
2-imino-1-hydroxy-1-phenylpropane + NADH
-
norephedrine is identical with threo-2-amino-1-hydroxy-1-phenylpropane
-
-
?
(+)-pseudoephedrine + NAD+
2-methylimino-1-phenylpropan-1-ol + NADH
-
higher rate than (-)-ephedrine
-
-
?
(+)-pseudoephedrine + NAD+
2-methylimino-1-phenylpropan-1-ol + NADH
-
pseudoephedrine is identical with DL-threo-2-(methylamino)-1-phenylpropan-1-ol
-
-
?
(-)-ephedrine + NAD+
(R)-2-methylimino-1-phenylpropan-1-ol + NADH
-
(-)-ephedrine is identical with 2-methylamino-1-phenyl-1-propanal
phenylacetylcarbinol is identical with 1-hydroxy-1-phenylpropan-2-one, three products: NADH, methylamine and phenylacetylcarbinol or its tautomeric form methylbenzoylcarbinol, ratio of NADH to methylamine is 1:1.1, enzyme attacks (-)-ephedrine at CH-NHCH3, yielding 2-methylimino-1-phenylpropanol, which is immediately hydrolyzed forming methylamine and phenylacetylcarbinol
?
(-)-ephedrine + NAD+
(R)-2-methylimino-1-phenylpropan-1-ol + NADH
-
first step in the catabolism of (-)-ephedrine
-
?
(-)-ephedrine + NAD+
(R)-2-methylimino-1-phenylpropan-1-ol + NADH
-
plays role in the metabolism of quite a number of different aromatic and aliphatic amino alcohols
-
?
(-)-sympatol + NAD+
4-[(1R,2E)-1-hydroxy-2-(methylimino)ethyl]phenol + NADH
-
higher rate than (-)-ephedrine
-
-
?
(-)-sympatol + NAD+
4-[(1R,2E)-1-hydroxy-2-(methylimino)ethyl]phenol + NADH
-
sympatol is identical with p-hydroxy-alpha-[(methylamino)methyl]benzyl tartrate
-
-
?
(R,R)-(-)-pseudoephedrine + NAD+
(R)-2-methylimino-1-phenylpropan-1-ol + NADH + H+
-
-
-
?
(R,R)-(-)-pseudoephedrine + NAD+
(R)-2-methylimino-1-phenylpropan-1-ol + NADH + H+
-
-
-
r
(R,S)-(-)-ephedrine + NAD+
(R)-2-methylimino-1-phenylpropan-1-ol + NADH + H+
-
-
-
?
(R,S)-(-)-ephedrine + NAD+
(R)-2-methylimino-1-phenylpropan-1-ol + NADH + H+
-
-
-
r
1-phenylpropan-1,2-dione + NAD+
phenylacetylcarbinol + NADH + H+
-
-
-
?
1-phenylpropan-1,2-dione + NAD+
phenylacetylcarbinol + NADH + H+
EDH overcomes the stability of the conjugated molecule PPD by reducing it to alpha-hydroxyketone (R)- and (S)-PAC, respectively. Phenylacetylcarbinol (PAC) cannot be oxidized by these dehydrogenases and possibly undergoes a cleavage reaction to yield benzaldehyde and acetaldehyde
-
-
?
suprifene + NAD+
p-hydroxy-alpha-[(1-methylimino)ethyl]benzyl alcohol + NADH
-
higher rate than (-)-ephedrine
-
-
?
suprifene + NAD+
p-hydroxy-alpha-[(1-methylimino)ethyl]benzyl alcohol + NADH
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suprifene is identical with p-hydroxyephedrine
-
-
?
additional information
?
-
-
wide range of ethanolamines as substrates, overview
-
-
?
additional information
?
-
ephedrine dehydrogenase (EDH) exhibits strict selectivity for the oxidation of the diastereomers (R,S)-(-)-ephedrine and (R,R)-(-)-pseudoephedrine. Conversion of all ephedrine isomers required the addition of NAD+ as an oxidant. Without a surplus oxidant or in the presence of NADP+, cell lysates do not significantly convert ephedrine
-
-
-
additional information
?
-
enzyme EDH exhibits a strict enantioselectivity for the oxidation of (R,S)-(-)-ephedrine and (R,R)-(-)-pseudoephedrine
-
-
-
additional information
?
-
enzyme EDH is specific for the enantioselective oxidation of (-)-(R) N-(pseudo)ephedrine. Prelog-specific EDH catalyzes the regio- and enantiospecific reduction of 1-phenyl-1,2-propanedione to (R)-phenylacetylcarbinol with full conversion and enantiomeric excess of over 99%. In addition, the enzyme performs the reduction of a wide range of aryl-aliphatic carbonyl compounds, including ketoamines, ketoesters, and haloketones, to the corresponding enantiopure alcohols. The enzyme performs the reduction of aromatic ketones with a strict regioselectivity for the first carbonyl function on the alpha-position close to the aromatic ring. Substrate specificity and stereochemistry, overview. No activity with acetophenone, poor activity with 4,4-dimethylbenzil, 2-thenoylacetonitrile, 4-(chlorophenyl)-2-pyridinylmethanone, phenyl-2-pyridinylmethanone, 2-chloroacetophenone, 3-chloropropiophenone, 1-phenyl-1-propanone, 4-chlorobenzil, 2-chloro-1-phenyl-1-propanone, 2-bromo-1-(3-chlorophenyl)-1-propanone, and isatin
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-
-
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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
(-)-ephedrine + NAD+
(R)-2-methylimino-1-phenylpropan-1-ol + NADH + H+
-
-
-
?
(R,S)-(-)-ephedrine + NAD+
(R)-2-methylimino-1-phenylpropan-1-ol + NADH + H+
-
-
-
r
additional information
?
-
ephedrine dehydrogenase (EDH) exhibits strict selectivity for the oxidation of the diastereomers (R,S)-(-)-ephedrine and (R,R)-(-)-pseudoephedrine. Conversion of all ephedrine isomers required the addition of NAD+ as an oxidant. Without a surplus oxidant or in the presence of NADP+, cell lysates do not significantly convert ephedrine
-
-
-
(-)-ephedrine + NAD+
(R)-2-methylimino-1-phenylpropan-1-ol + NADH
-
first step in the catabolism of (-)-ephedrine
-
?
(-)-ephedrine + NAD+
(R)-2-methylimino-1-phenylpropan-1-ol + NADH
-
plays role in the metabolism of quite a number of different aromatic and aliphatic amino alcohols
-
?
(R,R)-(-)-pseudoephedrine + NAD+
(R)-2-methylimino-1-phenylpropan-1-ol + NADH + H+
-
-
-
?
(R,R)-(-)-pseudoephedrine + NAD+
(R)-2-methylimino-1-phenylpropan-1-ol + NADH + H+
-
-
-
r
1-phenylpropan-1,2-dione + NAD+
phenylacetylcarbinol + NADH + H+
-
-
-
?
1-phenylpropan-1,2-dione + NAD+
phenylacetylcarbinol + NADH + H+
EDH overcomes the stability of the conjugated molecule PPD by reducing it to alpha-hydroxyketone (R)- and (S)-PAC, respectively. Phenylacetylcarbinol (PAC) cannot be oxidized by these dehydrogenases and possibly undergoes a cleavage reaction to yield benzaldehyde and acetaldehyde
-
-
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
NAD+
-
required for enzyme activity, NAD+ can not be replaced by NADP+, FAD or FMN
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
-
EDTA causes no remarkable loss of activity
-
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
4.7
purified native enzyme, substrate (-)-ephedrine, pH 7.8, 25°C
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
9.5 - 12.2
-
pH 9.5: 60% of maximum activity, pH 12.2: 60% of maximum activity
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
25
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TEMPERATURE RANGE
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
additional information
the Gram-positive soil bacterium Arthrobacter sp. strain TS-15 (DSM 32400) is capable of metabolizing all isomers of ephedrine as a sole source of carbon and energy. No growth on ephedrine as the sole source of nitrogen occurs because Arthrobacter sp. TS-15 cannot metabolize the nitrogen in ephedrine
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
metabolism
the enzyme is involved in the ephedrine metabolism, overview
physiological function
Arthrobacter sp. TS-15 is capable of metabolizing all isomers of ephedrine as a sole source of carbon and energy. Enantioselective oxidation of (-)-(R,N)-(pseudo)ephedrine and (+)-(S,N)-(pseudo)ephedrine catalyzed by PseDH and EDH, respectively, overview
evolution
ephedrine dehydrogenase (EDH) from Arthrobacter sp. TS-15 is an NADH-dependent member of the oxidoreductase superfamily of short-chain dehydrogenases/reductases (SDRs)
evolution
the enzyme belongs to the superfamily of short-chain dehydrogenases
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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).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.5 - 8.5
7.5 - 8.5
-
at 4°C maximum stability, after 24 h 20% loss of activity
392100
7.5 - 8.5
half-life is about 38 h at pH 8.0, and about 10 h at pH 7.0 and pH 9.0, profile overview
752351
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant His-tagged enzyme from Escherichia coli strain T7 SHuffle(DE3) by nickel affinity chromatography
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant expression of His-tagged enzyme in Escherichia coli strain T7 SHuffle(DE3)
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
synthesis
the wide substrate spectrum of the dehydrogenase, combined with its regio- and enantioselectivity, suggests a high potential for the industrial production of valuable chiral compounds
additional information
both (R,S)-(-)-ephedrine and (S,S)-(+)-pseudoephedrine are constituents of various over-the-counter (OTC) drugs and are also used as decongestants and stimulants. Arthrobacter sp. TS-15 and its isolated ephedrine-oxidizing enzymes have potential for use in decontamination and synthetic applications
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Klamann, E.; Lingens, F.
Degradation of (-)-ephedrine by Pseudomonas putida detection of (-)-ephedrine:NAD+-oxidoreductase from Arthrobacter globiformis
Z. Naturforsch. C
35
80-87
1980
Arthrobacter globiformis
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Shanati, T.; Lockie, C.; Beloti, L.; Grogan, G.; Ansorge-Schumacher, M.B.
Two enantiocomplementary ephedrine dehydrogenases from Arthrobacter sp. TS-15 with broad substrate specificity
ACS Catal.
9
6202-6211
2019
Arthrobacter sp. TS-15 (A0A545BBR2)
-
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Shanati, T.; Ansorge-Schumacher, M.B.
Biodegradation of ephedrine isomers by Arthrobacter sp. strain TS-15 discovery of novel ephedrine and pseudoephedrine dehydrogenases
Appl. Environ. Microbiol.
86
e02487-19
2020
Arthrobacter sp. TS-15 (A0A545BBR2)
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Release 2023.1 (January 2023)
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