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 |
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 |
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 |
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 |
EC Number | Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
---|---|---|---|---|
1.1.1.B4 | 67000 | - |
gel filtration | Kocuria rhizophila |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
1.1.1.B4 | Kocuria rhizophila | - |
- |
- |
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 |
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 |
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 |
EC Number | Subunits | Comment | Organism |
---|---|---|---|
1.1.1.B4 | homodimer | 2 * 33000, SDS-PAGE | Kocuria rhizophila |
EC Number | Synonyms | Comment | Organism |
---|---|---|---|
1.1.1.B4 | (R)-epinephrine dehydrogenase | - |
Kocuria rhizophila |
1.1.1.B4 | carbonyl reductase | - |
Kocuria rhizophila |
EC Number | Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|---|
1.1.1.B4 | 45 | - |
- |
Kocuria rhizophila |
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 |
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 |
EC Number | pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|---|
1.1.1.B4 | 6 | - |
- |
Kocuria rhizophila |
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 |
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 |
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 |