Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary 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

Application

EC Number Application Comment Organism
1.1.1.B4 synthesis the enzyme might be useful in application as a replacement of chemical synthesis of aromatic chiral beta-amino alcohols Kocuria rhizophila

Inhibitors

EC Number Inhibitors Comment Organism Structure
1.1.1.B4 Ag+ complete inhibition Kocuria rhizophila
1.1.1.B4 Al3+
-
Kocuria rhizophila
1.1.1.B4 Co2+
-
Kocuria rhizophila
1.1.1.B4 Cu2+ complete inhibition Kocuria rhizophila
1.1.1.B4 EDTA inhibitory at high concentration Kocuria rhizophila
1.1.1.B4 Fe2+
-
Kocuria rhizophila
1.1.1.B4 Hg2+ complete inhibition Kocuria rhizophila
1.1.1.B4 Pb2+
-
Kocuria rhizophila
1.1.1.B4 Zn2+ inhibits at 1 mM Kocuria rhizophila

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.1.1.B4 additional information
-
additional information Michaelis-Menten kinetics Kocuria rhizophila
1.1.1.B4 0.189
-
adrenalone pH 7.0, 40°C Kocuria rhizophila
1.1.1.B4 0.204
-
NADH pH 7.0, 40°C Kocuria rhizophila
1.1.1.B4 0.284
-
NADH pH 7.0, 40°C Kocuria rhizophila
1.1.1.B4 0.455
-
(R)-adrenaline pH 7.0, 40°C Kocuria rhizophila

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
1.1.1.B4 Ca2+ activates Kocuria rhizophila
1.1.1.B4 Mg2+ activates Kocuria rhizophila
1.1.1.B4 Mn2+ activates Kocuria rhizophila
1.1.1.B4 additional information (R)-epinephrine dehydrogenase is not a zinc metalloenzyme Kocuria rhizophila
1.1.1.B4 NH4+ activates Kocuria rhizophila

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
1.1.1.B4 67000
-
gel filtration Kocuria rhizophila

Organism

EC Number Organism UniProt Comment Textmining
1.1.1.B4 Kocuria rhizophila
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
1.1.1.B4 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]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
1.1.1.B4 190.2
-
purified native enzyme, pH 7.0, 40°C Kocuria rhizophila

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.1.1.B4 (R)-adrenaline + NAD+
-
Kocuria rhizophila ? + NADH + H+
-
r
1.1.1.B4 2-amino-3',4'-dihydroxyacetophenone + NADH + H+
-
Kocuria rhizophila ? + NAD+
-
r
1.1.1.B4 2-amino-4'-amino-acetophenone + NADH + H+
-
Kocuria rhizophila ? + NAD+
-
r
1.1.1.B4 2-amino-4'-hydroxyacetophenone + NADH + H+
-
Kocuria rhizophila ? + NAD+
-
r
1.1.1.B4 2-amino-acetophenone + NADH + H+
-
Kocuria rhizophila (R)-2-amino-1-phenylethanol + NAD+
-
r
1.1.1.B4 2-amino-acetophenone + NADH + H+
-
Kocuria rhizophila ? + NAD+
-
r
1.1.1.B4 2-bromoacetophenone + NADH + H+
-
Kocuria rhizophila ? + NAD+
-
r
1.1.1.B4 acetaldehyde + NAD+
-
Kocuria rhizophila ethanol + NADH + H+
-
r
1.1.1.B4 acetone + NADH + H+
-
Kocuria rhizophila propan-2-ol + NAD+
-
r
1.1.1.B4 acetophenone + NADH + H+
-
Kocuria rhizophila 1-phenylethanol + NAD+
-
r
1.1.1.B4 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
1.1.1.B4 adrenosterone + NADH + H+
-
Kocuria rhizophila ? + NAD+
-
r
1.1.1.B4 benzoylformic acid + NADH + H+
-
Kocuria rhizophila ? + NAD+
-
r
1.1.1.B4 ephedrine + NAD+
-
Kocuria rhizophila 1-(3,4-dihydroxyphenyl)-2-(methylamino)-propan-1-one + NADH + H+
-
r
1.1.1.B4 formaldehyde + NADH + H+
-
Kocuria rhizophila methanol + NAD+
-
r
1.1.1.B4 isoproterenol + NAD+
-
Kocuria rhizophila 1-(3,4-dihydroxyphenyl)-2-[(propan-2-yl)amino]ethane-1-one + NADH + H+
-
r
1.1.1.B4 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 ?
-
?
1.1.1.B4 norepinephrine + NAD+
-
Kocuria rhizophila ? + NADH + H+
-
r
1.1.1.B4 phenylephrine + NAD+
-
Kocuria rhizophila 1-(3-hydroxyphenyl)-2-(methylamino)ethane-1-one + NADH + H+
-
r

Subunits

EC Number Subunits Comment Organism
1.1.1.B4 homodimer 2 * 33000, SDS-PAGE Kocuria rhizophila

Synonyms

EC Number Synonyms Comment Organism
1.1.1.B4 (R)-epinephrine dehydrogenase
-
Kocuria rhizophila
1.1.1.B4 carbonyl reductase
-
Kocuria rhizophila

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
1.1.1.B4 45
-
-
Kocuria rhizophila

Temperature Range [°C]

EC Number Temperature Minimum [°C] Temperature Maximum [°C] Comment Organism
1.1.1.B4 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]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
1.1.1.B4 20 40 purified enzyme, stable at Kocuria rhizophila
1.1.1.B4 55
-
purified enzyme, retains almost 40% of maximal activity for 60 min Kocuria rhizophila
1.1.1.B4 60
-
purified enzyme, 60 min, inactivation Kocuria rhizophila

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
1.1.1.B4 6
-
-
Kocuria rhizophila

pH Range

EC Number pH Minimum pH Maximum Comment Organism
1.1.1.B4 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

EC Number pH Stability pH Stability Maximum Comment Organism
1.1.1.B4 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

EC Number Cofactor Comment Organism Structure
1.1.1.B4 additional information the enzyme shows no activity for NADPH or NADP+ Kocuria rhizophila
1.1.1.B4 NAD+
-
Kocuria rhizophila
1.1.1.B4 NADH
-
Kocuria rhizophila