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show all sequences of 1.1.1.B4

Purification and characterization of a novel carbonyl reductase involved in oxidoreduction of aromatic beta-amino ketones/alcohols

He, S.; Wang, Z.; Zou, Y.; Chen, S.; Xu, X.; Process Biochem. 49, 1107-1112 (2014)
No PubMed abstract available

Data extracted from this reference:

Application
Application
Commentary
Organism
synthesis
the enzyme might be useful in application as a replacement of chemical synthesis of aromatic chiral beta-amino alcohols
Kocuria rhizophila
Inhibitors
Inhibitors
Commentary
Organism
Structure
Ag+
complete inhibition
Kocuria rhizophila
Al3+
-
Kocuria rhizophila
Co2+
-
Kocuria rhizophila
Cu2+
complete inhibition
Kocuria rhizophila
EDTA
inhibitory at high concentration
Kocuria rhizophila
Fe2+
-
Kocuria rhizophila
Hg2+
complete inhibition
Kocuria rhizophila
Pb2+
-
Kocuria rhizophila
Zn2+
inhibits at 1 mM
Kocuria rhizophila
KM Value [mM]
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
additional information
-
additional information
Michaelis-Menten kinetics
Kocuria rhizophila
0.189
-
adrenalone
pH 7.0, 40°C
Kocuria rhizophila
0.204
-
NADH
pH 7.0, 40°C
Kocuria rhizophila
0.284
-
NADH
pH 7.0, 40°C
Kocuria rhizophila
0.455
-
(R)-adrenaline
pH 7.0, 40°C
Kocuria rhizophila
Metals/Ions
Metals/Ions
Commentary
Organism
Structure
Ca2+
activates
Kocuria rhizophila
Mg2+
activates
Kocuria rhizophila
Mn2+
activates
Kocuria rhizophila
additional information
(R)-epinephrine dehydrogenase is not a zinc metalloenzyme
Kocuria rhizophila
NH4+
activates
Kocuria rhizophila
Molecular Weight [Da]
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
67000
-
gel filtration
Kocuria rhizophila
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Kocuria rhizophila
-
-
-
Purification (Commentary)
Commentary
Organism
native enzyme 226fold to homogeneity by ammonium sulfate fractionation, anion exchange and hydrophobic interaction chromatography, followed by gel filtration
Kocuria rhizophila
Specific Activity [micromol/min/mg]
Specific Activity Minimum [µmol/min/mg]
Specific Activity Maximum [µmol/min/mg]
Commentary
Organism
190.2
-
purified native enzyme, pH 7.0, 40°C
Kocuria rhizophila
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
(R)-adrenaline + NAD+
-
743703
Kocuria rhizophila
? + NADH + H+
-
-
-
r
2-amino-3',4'-dihydroxyacetophenone + NADH + H+
-
743703
Kocuria rhizophila
? + NAD+
-
-
-
r
2-amino-4'-amino-acetophenone + NADH + H+
-
743703
Kocuria rhizophila
? + NAD+
-
-
-
r
2-amino-4'-hydroxyacetophenone + NADH + H+
-
743703
Kocuria rhizophila
? + NAD+
-
-
-
r
2-amino-acetophenone + NADH + H+
-
743703
Kocuria rhizophila
(R)-2-amino-1-phenylethanol + NAD+
-
-
-
r
2-amino-acetophenone + NADH + H+
-
743703
Kocuria rhizophila
? + NAD+
-
-
-
r
2-bromoacetophenone + NADH + H+
-
743703
Kocuria rhizophila
? + NAD+
-
-
-
r
acetaldehyde + NAD+
-
743703
Kocuria rhizophila
ethanol + NADH + H+
-
-
-
r
acetone + NADH + H+
-
743703
Kocuria rhizophila
propan-2-ol + NAD+
-
-
-
r
acetophenone + NADH + H+
-
743703
Kocuria rhizophila
1-phenylethanol + NAD+
-
-
-
r
adenosterone + NADH + H+
-
743703
Kocuria rhizophila
? + NAD+
-
-
-
r
adrenalone + NADH + H+
the NAD(H)-dependent dehydrogenase catalyzes the asymmetric reduction of adrenalone (corticosterone) to (R)-epinephrine, with an enantiomeric excess (e.e value) of more than 99%
743703
Kocuria rhizophila
(R)-epinephrine + NAD+
-
-
-
r
benzoylformic acid + NADH + H+
-
743703
Kocuria rhizophila
? + NAD+
-
-
-
r
ephedrine + NAD+
-
743703
Kocuria rhizophila
1-(3,4-dihydroxyphenyl)-2-(methylamino)-propan-1-one + NADH + H+
-
-
-
r
formaldehyde + NADH + H+
-
743703
Kocuria rhizophila
methanol + NAD+
-
-
-
r
isoproterenol + NAD+
-
743703
Kocuria rhizophila
1-(3,4-dihydroxyphenyl)-2-[(propan-2-yl)amino]ethane-1-one + NADH + H+
-
-
-
r
additional information
the enzyme catalyzes transformation of aromatic beta-amino ketones to the corresponding chiral alcohols. The purified enzyme yields pure (R)-enantiomer product with high activity and utilizes NADH as the cofactor. The enzyme shows selectivity for many aromatic beta-amino ketones/alcohols such as 2-amino-acetophenone, 2-amino-4'-hydroxyacetophenone, isoproterenol, and ephedrine. Substrate specificity, overview. No or poor activity with L-Tyr, L-Phe, Trp, ethanol, methanol, acetanilide, ethalacetoacetate, 2-phenethyl alcohol, and phenylmethanol
743703
Kocuria rhizophila
?
-
-
-
-
norepinephrine + NAD+
-
743703
Kocuria rhizophila
? + NADH + H+
-
-
-
r
phenylephrine + NAD+
-
743703
Kocuria rhizophila
1-(3-hydroxyphenyl)-2-(methylamino)ethane-1-one + NADH + H+
-
-
-
r
Subunits
Subunits
Commentary
Organism
homodimer
2 * 33000, SDS-PAGE
Kocuria rhizophila
Temperature Optimum [°C]
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
45
-
-
Kocuria rhizophila
Temperature Range [°C]
Temperature Minimum [°C]
Temperature Maximum [°C]
Commentary
Organism
20
70
activity range, profile overview. More than 80% of the maximum activity between 40°C and 55°C, above 60°C, the enzyme activity decreases sharply
Kocuria rhizophila
Temperature Stability [°C]
Temperature Stability Minimum [°C]
Temperature Stability Maximum [°C]
Commentary
Organism
20
40
purified enzyme, stable at
Kocuria rhizophila
55
-
purified enzyme, retains almost 40% of maximal activity for 60 min
Kocuria rhizophila
60
-
purified enzyme, 60 min, inactivation
Kocuria rhizophila
pH Optimum
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
6
-
-
Kocuria rhizophila
pH Range
pH Minimum
pH Maximum
Commentary
Organism
5.5
6.5
more than 80% of maximum activity is displayed in the pH range of pH 5.5-6.5. Below pH 4.5 or above pH 7.0 the activity decreases rapidly
Kocuria rhizophila
pH Stability
pH Stability
pH Stability Maximum
Commentary
Organism
4.5
7
the purifed enzyme retains 80% of its original activity over a broad range of pH 4.5-7.0 at 45°C for 24 h
Kocuria rhizophila
Cofactor
Cofactor
Commentary
Organism
Structure
additional information
the enzyme shows no activity for NADPH or NADP+
Kocuria rhizophila
NAD+
-
Kocuria rhizophila
NADH
-
Kocuria rhizophila
Application (protein specific)
Application
Commentary
Organism
synthesis
the enzyme might be useful in application as a replacement of chemical synthesis of aromatic chiral beta-amino alcohols
Kocuria rhizophila
Cofactor (protein specific)
Cofactor
Commentary
Organism
Structure
additional information
the enzyme shows no activity for NADPH or NADP+
Kocuria rhizophila
NAD+
-
Kocuria rhizophila
NADH
-
Kocuria rhizophila
Inhibitors (protein specific)
Inhibitors
Commentary
Organism
Structure
Ag+
complete inhibition
Kocuria rhizophila
Al3+
-
Kocuria rhizophila
Co2+
-
Kocuria rhizophila
Cu2+
complete inhibition
Kocuria rhizophila
EDTA
inhibitory at high concentration
Kocuria rhizophila
Fe2+
-
Kocuria rhizophila
Hg2+
complete inhibition
Kocuria rhizophila
Pb2+
-
Kocuria rhizophila
Zn2+
inhibits at 1 mM
Kocuria rhizophila
KM Value [mM] (protein specific)
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
additional information
-
additional information
Michaelis-Menten kinetics
Kocuria rhizophila
0.189
-
adrenalone
pH 7.0, 40°C
Kocuria rhizophila
0.204
-
NADH
pH 7.0, 40°C
Kocuria rhizophila
0.284
-
NADH
pH 7.0, 40°C
Kocuria rhizophila
0.455
-
(R)-adrenaline
pH 7.0, 40°C
Kocuria rhizophila
Metals/Ions (protein specific)
Metals/Ions
Commentary
Organism
Structure
Ca2+
activates
Kocuria rhizophila
Mg2+
activates
Kocuria rhizophila
Mn2+
activates
Kocuria rhizophila
additional information
(R)-epinephrine dehydrogenase is not a zinc metalloenzyme
Kocuria rhizophila
NH4+
activates
Kocuria rhizophila
Molecular Weight [Da] (protein specific)
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
67000
-
gel filtration
Kocuria rhizophila
Purification (Commentary) (protein specific)
Commentary
Organism
native enzyme 226fold to homogeneity by ammonium sulfate fractionation, anion exchange and hydrophobic interaction chromatography, followed by gel filtration
Kocuria rhizophila
Specific Activity [micromol/min/mg] (protein specific)
Specific Activity Minimum [µmol/min/mg]
Specific Activity Maximum [µmol/min/mg]
Commentary
Organism
190.2
-
purified native enzyme, pH 7.0, 40°C
Kocuria rhizophila
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
(R)-adrenaline + NAD+
-
743703
Kocuria rhizophila
? + NADH + H+
-
-
-
r
2-amino-3',4'-dihydroxyacetophenone + NADH + H+
-
743703
Kocuria rhizophila
? + NAD+
-
-
-
r
2-amino-4'-amino-acetophenone + NADH + H+
-
743703
Kocuria rhizophila
? + NAD+
-
-
-
r
2-amino-4'-hydroxyacetophenone + NADH + H+
-
743703
Kocuria rhizophila
? + NAD+
-
-
-
r
2-amino-acetophenone + NADH + H+
-
743703
Kocuria rhizophila
(R)-2-amino-1-phenylethanol + NAD+
-
-
-
r
2-amino-acetophenone + NADH + H+
-
743703
Kocuria rhizophila
? + NAD+
-
-
-
r
2-bromoacetophenone + NADH + H+
-
743703
Kocuria rhizophila
? + NAD+
-
-
-
r
acetaldehyde + NAD+
-
743703
Kocuria rhizophila
ethanol + NADH + H+
-
-
-
r
acetone + NADH + H+
-
743703
Kocuria rhizophila
propan-2-ol + NAD+
-
-
-
r
acetophenone + NADH + H+
-
743703
Kocuria rhizophila
1-phenylethanol + NAD+
-
-
-
r
adenosterone + NADH + H+
-
743703
Kocuria rhizophila
? + NAD+
-
-
-
r
adrenalone + NADH + H+
the NAD(H)-dependent dehydrogenase catalyzes the asymmetric reduction of adrenalone (corticosterone) to (R)-epinephrine, with an enantiomeric excess (e.e value) of more than 99%
743703
Kocuria rhizophila
(R)-epinephrine + NAD+
-
-
-
r
benzoylformic acid + NADH + H+
-
743703
Kocuria rhizophila
? + NAD+
-
-
-
r
ephedrine + NAD+
-
743703
Kocuria rhizophila
1-(3,4-dihydroxyphenyl)-2-(methylamino)-propan-1-one + NADH + H+
-
-
-
r
formaldehyde + NADH + H+
-
743703
Kocuria rhizophila
methanol + NAD+
-
-
-
r
isoproterenol + NAD+
-
743703
Kocuria rhizophila
1-(3,4-dihydroxyphenyl)-2-[(propan-2-yl)amino]ethane-1-one + NADH + H+
-
-
-
r
additional information
the enzyme catalyzes transformation of aromatic beta-amino ketones to the corresponding chiral alcohols. The purified enzyme yields pure (R)-enantiomer product with high activity and utilizes NADH as the cofactor. The enzyme shows selectivity for many aromatic beta-amino ketones/alcohols such as 2-amino-acetophenone, 2-amino-4'-hydroxyacetophenone, isoproterenol, and ephedrine. Substrate specificity, overview. No or poor activity with L-Tyr, L-Phe, Trp, ethanol, methanol, acetanilide, ethalacetoacetate, 2-phenethyl alcohol, and phenylmethanol
743703
Kocuria rhizophila
?
-
-
-
-
norepinephrine + NAD+
-
743703
Kocuria rhizophila
? + NADH + H+
-
-
-
r
phenylephrine + NAD+
-
743703
Kocuria rhizophila
1-(3-hydroxyphenyl)-2-(methylamino)ethane-1-one + NADH + H+
-
-
-
r
Subunits (protein specific)
Subunits
Commentary
Organism
homodimer
2 * 33000, SDS-PAGE
Kocuria rhizophila
Temperature Optimum [°C] (protein specific)
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
45
-
-
Kocuria rhizophila
Temperature Range [°C] (protein specific)
Temperature Minimum [°C]
Temperature Maximum [°C]
Commentary
Organism
20
70
activity range, profile overview. More than 80% of the maximum activity between 40°C and 55°C, above 60°C, the enzyme activity decreases sharply
Kocuria rhizophila
Temperature Stability [°C] (protein specific)
Temperature Stability Minimum [°C]
Temperature Stability Maximum [°C]
Commentary
Organism
20
40
purified enzyme, stable at
Kocuria rhizophila
55
-
purified enzyme, retains almost 40% of maximal activity for 60 min
Kocuria rhizophila
60
-
purified enzyme, 60 min, inactivation
Kocuria rhizophila
pH Optimum (protein specific)
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
6
-
-
Kocuria rhizophila
pH Range (protein specific)
pH Minimum
pH Maximum
Commentary
Organism
5.5
6.5
more than 80% of maximum activity is displayed in the pH range of pH 5.5-6.5. Below pH 4.5 or above pH 7.0 the activity decreases rapidly
Kocuria rhizophila
pH Stability (protein specific)
pH Stability
pH Stability Maximum
Commentary
Organism
4.5
7
the purifed enzyme retains 80% of its original activity over a broad range of pH 4.5-7.0 at 45°C for 24 h
Kocuria rhizophila
Other publictions for EC 1.1.1.B4
No.
1st author
Pub Med
title
organims
journal
volume
pages
year
Activating Compound
Application
Cloned(Commentary)
Crystallization (Commentary)
Engineering
General Stability
Inhibitors
KM Value [mM]
Localization
Metals/Ions
Molecular Weight [Da]
Natural Substrates/ Products (Substrates)
Organic Solvent Stability
Organism
Oxidation Stability
Posttranslational Modification
Purification (Commentary)
Reaction
Renatured (Commentary)
Source Tissue
Specific Activity [micromol/min/mg]
Storage Stability
Substrates and Products (Substrate)
Subunits
Temperature Optimum [°C]
Temperature Range [°C]
Temperature Stability [°C]
Turnover Number [1/s]
pH Optimum
pH Range
pH Stability
Cofactor
Ki Value [mM]
pI Value
IC50 Value
Activating Compound (protein specific)
Application (protein specific)
Cloned(Commentary) (protein specific)
Cofactor (protein specific)
Crystallization (Commentary) (protein specific)
Engineering (protein specific)
General Stability (protein specific)
IC50 Value (protein specific)
Inhibitors (protein specific)
Ki Value [mM] (protein specific)
KM Value [mM] (protein specific)
Localization (protein specific)
Metals/Ions (protein specific)
Molecular Weight [Da] (protein specific)
Natural Substrates/ Products (Substrates) (protein specific)
Organic Solvent Stability (protein specific)
Oxidation Stability (protein specific)
Posttranslational Modification (protein specific)
Purification (Commentary) (protein specific)
Renatured (Commentary) (protein specific)
Source Tissue (protein specific)
Specific Activity [micromol/min/mg] (protein specific)
Storage Stability (protein specific)
Substrates and Products (Substrate) (protein specific)
Subunits (protein specific)
Temperature Optimum [°C] (protein specific)
Temperature Range [°C] (protein specific)
Temperature Stability [°C] (protein specific)
Turnover Number [1/s] (protein specific)
pH Optimum (protein specific)
pH Range (protein specific)
pH Stability (protein specific)
pI Value (protein specific)
Expression
General Information
General Information (protein specific)
Expression (protein specific)
KCat/KM [mM/s]
KCat/KM [mM/s] (protein specific)
741784
Nealon
I86A/C295A mutant secondary a ...
Thermoanaerobacter ethanolicus
Arch. Biochem. Biophys.
606
151-156
2016
-
-
-
-
3
-
1
1
-
1
-
-
-
2
-
-
1
-
-
-
-
-
17
1
1
-
-
24
1
-
-
2
-
-
-
-
-
-
2
-
3
-
-
1
-
1
-
1
-
-
-
-
-
1
-
-
-
-
17
1
1
-
-
24
1
-
-
-
-
-
-
-
26
26
742305
Peng
-
Continuous preparation of (R) ...
Morganella morganii, Morganella morganii CMCC(B)49208
Chin. J. Proc. Engin.
16
286-291
2016
-
1
-
-
-
-
-
-
-
-
-
2
-
2
-
-
-
-
-
-
-
-
4
-
1
-
-
-
1
-
-
1
-
-
-
-
1
-
1
-
-
-
-
-
-
-
-
-
-
2
-
-
-
-
-
-
-
-
4
-
1
-
-
-
1
-
-
-
-
-
-
-
-
-
740394
Chen
Cloning, expression, and chara ...
Gluconobacter oxydans, Gluconobacter oxydans DSM 2343
Enzyme Microb. Technol.
70
18-27
2015
-
-
-
-
-
-
2
3
-
3
-
-
-
2
-
-
-
-
-
-
-
-
13
-
1
-
-
2
1
-
-
2
-
-
-
-
-
-
2
-
-
-
-
2
-
3
-
3
-
-
-
-
-
-
-
-
-
-
13
-
1
-
-
2
1
-
-
-
-
-
-
-
2
2
739942
Wang
Cloning, expression, and direc ...
Leifsonia xyli, Leifsonia xyli HS0904
Appl. Microbiol. Biotechnol.
98
8591-8601
2014
-
1
-
-
2
-
-
6
-
-
-
-
-
2
-
-
-
-
-
-
-
-
2
-
-
-
-
6
-
-
-
-
-
-
-
-
1
-
-
-
2
-
-
-
-
6
-
-
-
-
-
-
-
-
-
-
-
-
2
-
-
-
-
6
-
-
-
-
-
-
-
-
6
6
743703
He
-
Purification and characteriza ...
Kocuria rhizophila
Process Biochem.
49
1107-1112
2014
-
1
-
-
-
-
9
5
-
5
1
-
-
1
-
-
1
-
-
-
1
-
19
1
1
1
3
-
1
1
1
3
-
-
-
-
1
-
3
-
-
-
-
9
-
5
-
5
1
-
-
-
-
1
-
-
1
-
19
1
1
1
3
-
1
1
1
-
-
-
-
-
-
-
721911
Zhou
Biocatalytic characterization ...
Carboxydothermus hydrogenoformans, Carboxydothermus hydrogenoformans DSM 6008
Biotechnol. Lett.
35
359-365
2013
-
1
1
-
-
-
-
1
-
-
1
-
4
2
-
-
-
-
-
-
-
-
15
1
1
-
-
1
1
-
-
2
-
-
-
-
1
1
2
-
-
-
-
-
-
1
-
-
1
-
4
-
-
-
-
-
-
-
15
1
1
-
-
1
1
-
-
-
-
-
-
-
-
-
739805
Aggarwal
Expression, purification, crys ...
Candida parapsilosis, Candida parapsilosis ATCC 7330
Acta Crystallogr. Sect. F
69
313-315
2013
-
-
1
1
-
-
-
-
-
-
-
-
-
2
-
-
-
-
-
-
-
-
2
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
2
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
723841
Protsko
Crystallization and preliminar ...
Thermoanaerobacter ethanolicus
Acta Crystallogr. Sect. F
66
831-833
2010
-
-
1
1
1
-
-
-
-
-
1
1
-
3
-
-
1
-
-
-
-
-
1
1
-
-
-
-
-
-
-
2
-
-
-
-
-
1
2
1
1
-
-
-
-
-
-
-
1
1
-
-
-
1
-
-
-
-
1
1
-
-
-
-
-
-
-
-
-
1
1
-
-
-
725726
Li
-
Deracemization of aryl seconda ...
Microbacterium oxydans, Microbacterium oxydans ECU2010
J. Mol. Catal. B
64
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