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Information on EC 1.1.1.422 - pseudoephedrine dehydrogenase
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1.1.1.422 pseudoephedrine dehydrogenaseIUBMB Comments
The enzyme, characterized from the bacterium Arthrobacter sp. TS-15, acts on a broad range of different aryl-alkyl ketones, such as haloketones, ketoamines, diketones, and ketoesters. It accepts various types of aryl groups including phenyl-, pyridyl-, thienyl-, and furyl-rings, but the presence of an aromatic ring is essential for the activity. In addition, the presence of a functional group on the alkyl chain, such as an amine, a halogen, or a ketone, is also crucial. The enzyme exhibits a strict anti-Prelog enantioselectivity. When acting on diketones, it catalyses the reduction of only the keto group closest to the ring, with no further reduction to the diol. cf. EC 1.1.1.423, ephedrine dehydrogenase.
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The expected taxonomic range for this enzyme is: unclassified Arthrobacter
Reaction Schemes
(+)-(1S,2S)-pseudoephedrine
+
=
(S)-2-methylamino-1-phenylpropan-1-one
+
+
Synonyms
pseudoephedrine dehydrogenase, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
PseDH
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
(+)-(1S,2S)-pseudoephedrine + NAD+ = (S)-2-methylamino-1-phenylpropan-1-one + NADH + H+
-
-
-
-
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SYSTEMATIC NAME
IUBMB Comments
(+)-(1S,2S)-pseudoephedrine:NAD+ 1-oxoreductase
The enzyme, characterized from the bacterium Arthrobacter sp. TS-15, acts on a broad range of different aryl-alkyl ketones, such as haloketones, ketoamines, diketones, and ketoesters. It accepts various types of aryl groups including phenyl-, pyridyl-, thienyl-, and furyl-rings, but the presence of an aromatic ring is essential for the activity. In addition, the presence of a functional group on the alkyl chain, such as an amine, a halogen, or a ketone, is also crucial. The enzyme exhibits a strict anti-Prelog enantioselectivity. When acting on diketones, it catalyses the reduction of only the keto group closest to the ring, with no further reduction to the diol. cf. EC 1.1.1.423, ephedrine dehydrogenase.
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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
(+)-(1S,2S)-pseudoephedrine + NAD+
(S)-2-methylamino-1-phenylpropan-1-one + NADH + H+
-
-
?
(4-chlorophenyl)-2-pyridinylmethanone + NAD+
(R)-(4-chlorophenyl)(pyridin-2-yl) methanol + NADH + H+
specifc activity: 0.2 U/mg. Product: 60% (R) enantiomeric excess
-
?
(S,R)-(+)-ephedrine + NAD+
? + NADH + H+
the enzyme is strictly stereospecific for the diastereomers (S,S)-(+)-pseudoephedrine and (S,R)-(+)-ephedrine
-
?
1,2-indandione + NAD+
? + NADH + H+
specifc activity: 9.52 U/mg
-
?
1,2-indanedione + NADH + H+
? + NAD+
5.9% of the activity as compared to methyl benzoylformate
-
?
1,2-naphthoquinone + NAD+
? + NADH + H+
specifc activity: 21.96 U/mg
-
?
1,2-naphthoquinone + NADH + H+
? + NAD+
13.7% of the activity as compared to methyl benzoylformate
-
?
1-phenyl-1,2-propanedione + NAD+
(S)-phenylacetylcarbinol + NADH + H+
specifc activity: 55.47 U/mg. Product: 99% (S) enantiomeric excess
-
?
1-phenyl-1,2-propanedione + NADH + H+
(S)-phenylacetylcarbinol + NAD+
34.6% of the activity as compared to methyl benzoylformate. (S)-Phenylacetylcarbinol is formed with more than 99% yield and more than 99% enantiomeric excess
-
?
2,2'-dichlorobenzil + NAD+
(2S)-1,2--bis(2-chlorophenyl)-2-hydroxyethan-1-one + NADH + H+
specifc activity: 10.08 U/mg. Product: 97% (S) enantiomeric excess
-
?
2,2'-dichlorobenzil + NADH + H+
? + NAD+
6.2% of the activity as compared to methyl benzoylformate
-
?
2,2'-furil + NAD+
(2S)-1,2-di(furan-2-yl)-2-hydroxyethan-1-one + NADH + H+
specifc activity: 0.66 U/mg. Product: 99% (S) enantiomeric excess
-
?
2,2'-thenil + NAD+
(2S)-2-hydroxy-1,2-di(thiophen-2-yl)ethan-1-one + NADH + H+
specifc activity: 0.58 U/mg. Product: 99% (S) enantiomeric excess
-
?
2-aminoacetophenone + NAD+
(1S)-2-amino-1-phenylethan-1-ol + NADH + H+
specifc activity: 9.49 U/mg. Product: 99% (S) enantiomeric excess
-
?
2-aminoacetophenone + NADH + H+
? + NAD+
5.9% of the activity as compared to methyl benzoylformate. The (S)-enantiomer is formed with 99% enantiomeric excess
-
?
2-bromo-1-(3-chlorophenyl)-1-propanone + NAD+
(R,S)-2-bromo-1-(3-chlorophenyl)propan-1-ol + NADH + H+
specifc activity: 12.58 U/mg
-
?
2-bromo-1-(3-chlorophenyl)-1-propanone + NADH + H+
? + NAD+
7.8% of the activity as compared to methyl benzoylformate
-
?
2-bromoacetophenone + NAD+
(1S)-2-bromo-1-phenylethan-1-ol + NADH + H+
specifc activity: 3.75 U/mg. Product: 37% (S) enantiomeric excess
-
?
2-bromoacetophenone + NADH + H+
? + NAD+
2.3% of the activity as compared to methyl benzoylformate. The (S)-enantiomer is formed with 37% enantiomeric excess
-
?
2-chloro-1-phenyl-1-propane + NAD+
(R,S)-2-chloro-1-phenylpropan-1-ol + NADH + H+
specifc activity: 5.41 U/mg
-
?
2-chloro-1-phenyl-1-propanone + NADH + H+
? + NAD+
3.3% of the activity as compared to methyl benzoylformate
-
?
4,4'-difluorobenzil + NAD+
(2S)-1,2-bis(4fluorophenyl)-2-hydroxyethan-1-one + NADH + H+
specifc activity: 1.5 U/mg. Product: 99% (S) enantiomeric excess
-
?
4,4'-dimethylbenzil + NAD+
(2S)-2-hydroxy-1,2-bis(4-methyphenyl)ethan-1-one + NADH + H+
specifc activity: 2.93 U/mg. Product: 99% (S) enantiomeric excess
-
?
4-chlorobenzil + NAD+
? + NADH + H+
specifc activity: 5.26 U/mg
-
?
4-chlorobenzil + NADH + H+
? + NAD+
3.2% of the activity as compared to methyl benzoylformate
-
?
benzil + NAD+
(2S)-2-hydroxy-1,2-diphenylethan-1-one + NADH + H+
specifc activity: 2.4 U/mg. Product: 99% (S) enantiomeric excess
-
?
benzil + NADH + H+
? + NAD+
1.4% of the activity as compared to methyl benzoylformate
-
?
ethyl 2-chlorobenzoylacetate + NAD+
ethyl (R,S)-2-chloro-3-hydroxy-3-phenylpropanoate + NADH + H+
specifc activity: 16.13 U/mg
-
?
ethyl 2-chlorobenzoylacetate + NADH + H+
? + NAD+
10% of the activity as compared to methyl benzoylformate
-
?
isatin + NAD+
? + NADH + H+
specifc activity: 66.99 U/mg. Product: 89% (S) enantiomeric excess
-
?
isatin + NADH + H+
? + NAD+
41.8% of the activity as compared to methyl benzoylformate. The (S)-enantiomer is formed with 89% enantiomeric excess
-
?
methyl benzoylformate + NAD+
methyl (2S)-hydroxy(phenyl)acetate + NADH + H+
specifc activity: 160.12 U/mg. Product: 99% (S) enantiomeric excess
-
?
methyl benzoylformate + NADH + H+
? + NAD+
substrate with highest activity. The (S)-enantiomer is formed with 99% enantiomeric excess
-
?
phenyl-2-pyridinylmethanone + NAD+
(S)-phenyl(pyridin-1-yl)methynol + NADH + H+
specifc activity: 0.04 U/mg. Product: 5% (S) enantiomeric excess
-
?
phenylglyoxal + NAD+
(R,S)-hydroxy(phenyl)acetaldehyde + NADH + H+
specifc activity: 5.51 U/mg
-
?
phenylglyoxal + NADH + H+
? + NAD+
3.4% of the activity as compared to methyl benzoylformate
-
?
(+)-(1S,2S)-pseudoephedrine + NAD+
(S)-2-(methylamino)-1-phenylpropan-1-one + NADH + H+
-
-
?
(+)-(1S,2S)-pseudoephedrine + NAD+
(S)-2-(methylamino)-1-phenylpropan-1-one + NADH + H+
the enzyme acts on a broad range of different aryl-alkyl ketones, such as haloketones, ketoamines, diketones, and ketoesters. It accepts various types of aryl groups including phenyl-, pyridyl-, thienyl-, and furyl-rings, but the presence of an aromatic ring is essential for the activity. In addition, the presence of a functional group on the alkyl chain, such as an amine, a halogen, or a ketone, is also crucial. The enzyme exhibits a strict anti-Prelog enantioselectivity. When acting on diketones, it catalyses the reduction of only the keto group closest to the ring, with no further reduction to the diol. (+)-(1S,2S)-pseudoephedrine i.e. (1S,2S)-2-(methylamino)-1-phenylpropan-1-ol. (S)-2-(methylamino)-1-phenylpropan-1-one i.e. (S)-methcathinone
-
?
(+)-(1S,2S)-pseudoephedrine + NAD+
(S)-2-(methylamino)-1-phenylpropan-1-one + NADH + H+
the enzyme is strictly stereospecific for the diastereomers (S,S)-(+)-pseudoephedrine and (S,R)-(+)-ephedrine
-
?
additional information
?
-
no activity with: acetophenone,2-thenoylacetonitrile, 2-chloroacetophenone, 3-chloropropiophenone, 1-phensyl-1,3-butanedione, 1-phenyl-1-propanone
-
?
additional information
?
-
no activity on (S,N)-(+)-(pseudo)ephedrine or (R,N)-(-)-(pseudo)ephedrine
-
-
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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
(+)-(1S,2S)-pseudoephedrine + NAD+
(S)-2-(methylamino)-1-phenylpropan-1-one + NADH + H+
-
-
-
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
NAD+
the enzyme displays no apparent activity with NADP(H) and full catalytic activity with NAD(H). A model of the active site in complex with NAD+ and 1-phenyl-1,2-propanedione suggests key roles for S143 and W152 in recognition of the substrate and positioning for the reduction reaction
NAD+
no apparent activity with NADP(H)+ and full catalytic activity with NAD(H). The preference for NADH makes the utilization of the enzyme an attractive for industrial applications, since NADH is more stable and less expensive than NADPH under operational reaction conditions
NADH
the enzyme displays no apparent activity with NADP(H) and full catalytic activity with NAD(H)
NADH
no apparent activity with NADP(H)+ and full catalytic activity with NAD(H). The preference for NADH makes the utilization of the enzyme an attractive for industrial applications, since NADH is more stable and less expensive than NADPH under operational reaction conditions
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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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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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.2
substrate: (4-chlorophenyl)-2-pyridinylmethanone, pH 7.5, 25°C
12.58
substrate: 2-bromo-1-(3-chlorophenyl)-1-propanone, pH 7.5, 25°C
16.13
substrate: ethyl 2-chlorobenzoylacetate, pH 7.5, 25°C
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6.5
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
35
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
15 - 40
15°C: about 40% of maximal activity, 40°C: about 65% of maximal activity
20 - 40
20°C: about 50% of maximal activity, 40°C: about 70% of maximal activity, substrate: 1-phenyl-1,2-propanedione
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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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.
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
28170
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
octamer
8 * 33000, SDS-PAGE, the smallest oligomeric state seemed to be a dimer, the predominant oligomeric states are the tetramer and octamer
tetramer
4 * 33000, SDS-PAGE, the smallest oligomeric state seemed to be a dimer, the predominant oligomeric states are the tetramer and octamer
dimer
2 * 33000, SDS-PAGE, the smallest oligomeric state seemed to be a dimer, the predominant oligomeric states are the tetramer and octamer
dimer
2 * 33000, smallest active oligomer is a dimer, the largest oligomeric state is a dodecamer, SDS-PAGE
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
hanging-drop vapor diffusion method, the crystal structure of the enzyme-NAD+ complex, refined to a resolution of 1.83 A, reveales a tetrameric structure, which is confirmed by solution studies
the crystal structure of the enzyme-NAD+ complex, refined to a resolution of 1.83 A, reveales a tetrameric structure, which is confirmed by solution studies
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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6 - 8
6 - 8
highest stability, t1/2: 113-193 h. Outside this pH range, the stability of the enzyme dropps rapidly to under 10 h
752351
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
15
25
40
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
overexpressed in Escherichia coli T7 Shuffle (DE3) after insertion into plasmid pET19b
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
industry
the wide substrate spectrum of these dehydrogenases, combined with their regio- and enantioselectivity, suggests a high potential for the industrial production of valuable chiral compounds
synthesis
synthesis
the wide substrate spectrum of these dehydrogenases, combined with their regio- and enantioselectivity, suggests a high potential for the industrial production of valuable chiral compounds
synthesis
the enzyme catalyzes the oxidation of an isomers of ephedrine and the regio- and enantioselective reduction of sterically demanding substrate 1-phenyl-1,2-propanedione to give (S)-phenylacetylcarbinol. (S)-phenylacetylcarbinol can serve as a precursor in the synthesis of many pharmaceuticals, such as (+)-(S,S)-pseudoephedrine
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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. (A0A545BBS8), Arthrobacter sp. TS-15 (A0A545BBS8)
-
brenda
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 (A0A545BBS8)
brenda
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