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Literature summary for 1.1.1.B4 extracted from

  • He, S.; Wang, Z.; Zou, Y.; Chen, S.; Xu, X.
    Purification and characterization of a novel carbonyl reductase involved in oxidoreduction of aromatic beta-amino ketones/alcohols (2014), Process Biochem., 49, 1107-1112 .
No PubMed abstract available
Search for more literature for 1.1.1.B4

Application

Application Comment 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 Comment 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 Comment 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 Comment 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] Comment Organism
67000
-
 gel filtration Kocuria rhizophila

Organism

Organism UniProt Comment Textmining
Kocuria rhizophila
-
-
-

Purification (Commentary)

Purification (Comment) 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] Comment Organism
190.2
-
 purified native enzyme, pH 7.0, 40°C Kocuria rhizophila

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
(R)-adrenaline + NAD+
-
 Kocuria rhizophila ? + NADH + H+
-
 r
2-amino-3',4'-dihydroxyacetophenone + NADH + H+
-
 Kocuria rhizophila ? + NAD+
-
 r
2-amino-4'-amino-acetophenone + NADH + H+
-
 Kocuria rhizophila ? + NAD+
-
 r
2-amino-4'-hydroxyacetophenone + NADH + H+
-
 Kocuria rhizophila ? + NAD+
-
 r
2-amino-acetophenone + NADH + H+
-
 Kocuria rhizophila (R)-2-amino-1-phenylethanol + NAD+
-
 r
2-amino-acetophenone + NADH + H+
-
 Kocuria rhizophila ? + NAD+
-
 r
2-bromoacetophenone + NADH + H+
-
 Kocuria rhizophila ? + NAD+
-
 r
acetaldehyde + NAD+
-
 Kocuria rhizophila ethanol + NADH + H+
-
 r
acetone + NADH + H+
-
 Kocuria rhizophila propan-2-ol + NAD+
-
 r
acetophenone + NADH + H+
-
 Kocuria rhizophila 1-phenylethanol + 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% Kocuria rhizophila (R)-epinephrine + NAD+
-
 r
adrenosterone + NADH + H+
-
 Kocuria rhizophila ? + NAD+
-
 r
benzoylformic acid + NADH + H+
-
 Kocuria rhizophila ? + NAD+
-
 r
ephedrine + NAD+
-
 Kocuria rhizophila 1-(3,4-dihydroxyphenyl)-2-(methylamino)-propan-1-one + NADH + H+
-
 r
formaldehyde + NADH + H+
-
 Kocuria rhizophila methanol + NAD+
-
 r
isoproterenol + NAD+
-
 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 Kocuria rhizophila ?
-
 ?
norepinephrine + NAD+
-
 Kocuria rhizophila ? + NADH + H+
-
 r
phenylephrine + NAD+
-
 Kocuria rhizophila 1-(3-hydroxyphenyl)-2-(methylamino)ethane-1-one + NADH + H+
-
 r

Subunits

Subunits Comment Organism
homodimer 2 * 33000, SDS-PAGE Kocuria rhizophila

Synonyms

Synonyms Comment Organism
(R)-epinephrine dehydrogenase
-
 Kocuria rhizophila
carbonyl reductase
-
 Kocuria rhizophila

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
45
-
-
 Kocuria rhizophila

Temperature Range [°C]

Temperature Minimum [°C] Temperature Maximum [°C] Comment 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] Comment 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 Comment Organism
6
-
-
 Kocuria rhizophila

pH Range

pH Minimum pH Maximum Comment 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 Comment 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 Comment Organism Structure
additional information the enzyme shows no activity for NADPH or NADP+ Kocuria rhizophila
NAD+
-
 Kocuria rhizophila
NADH
-
 Kocuria rhizophila