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Literature summary for 1.1.1.B3 extracted from

  • Rocha-Martin, J.; Vega, D.; Cabrera, Z.; Bolivar, J.; Fernandez-Lafuente, R.; Berenguer, J.; Guisan, J.
    Purification, immobilization and stabilization of a highly enantioselective alcohol dehydrogenase from Thermus thermophilus HB27 cloned in E. coli (2009), Process Biochem., 44, 1004-1012.
No PubMed abstract available
Search for more literature for 1.1.1.B3

Application

Application Comment Organism
synthesis the immobilized enzyme is utilized in the asymmetric reduction of acetophenone to produce (S)-1-phenylethanol, with an enantiomeric excess of more than 99% Thermus thermophilus

Cloned(Commentary)

Cloned (Comment) Organism
expression in Escherichia coli strain BL21(DE3) Thermus thermophilus

Protein Variants

Protein Variants Comment Organism
additional information covalent immobilization of the purified recombinant enzyme on different supports, i.e. on glyoxyl agarose, amino epoxy agarose, CNBr-activated sepharose, monoaminoethyl-N-ethylagarose-glutaraldehyde, monoaminoethyl-N-ethyl agarose, or polyethyleneimine agarose, immobilized enzyme activities, overview Thermus thermophilus

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
140000
-
 recombinant enzyme, gel filtration Thermus thermophilus

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
(S)-1-phenylethanol + NAD+ Thermus thermophilus
-
 acetophenone + NADH + H+
-
 r
(S)-1-phenylethanol + NAD+ Thermus thermophilus HB27 / ATCC BAA-163 / DSM 7039
-
 acetophenone + NADH + H+
-
 r

Organism

Organism UniProt Comment Textmining
Thermus thermophilus
-
-
-
Thermus thermophilus HB27 / ATCC BAA-163 / DSM 7039
-
-
-

Purification (Commentary)

Purification (Comment) Organism
by heat treatment at 70°C and/or adsorption chromatography on an IDA-Cu2+ support, both methods combined result in 8.8fold purification Thermus thermophilus

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
1.5
-
 immobilized recombinant enzyme Thermus thermophilus

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
(S)-1-phenylethanol + NAD+
-
 Thermus thermophilus acetophenone + NADH + H+
-
 r
(S)-1-phenylethanol + NAD+ asymmetric reduction of acetophenone to produce (S)-1-phenylethanol, with an enantiomeric excess of more than 99% Thermus thermophilus acetophenone + NADH + H+
-
 r
(S)-1-phenylethanol + NAD+
-
 Thermus thermophilus HB27 / ATCC BAA-163 / DSM 7039 acetophenone + NADH + H+
-
 r
(S)-1-phenylethanol + NAD+ asymmetric reduction of acetophenone to produce (S)-1-phenylethanol, with an enantiomeric excess of more than 99% Thermus thermophilus HB27 / ATCC BAA-163 / DSM 7039 acetophenone + NADH + H+
-
 r

Subunits

Subunits Comment Organism
tetramer
-
 Thermus thermophilus

Synonyms

Synonyms Comment Organism
More the enzyme belongs to the short-chain dehydrogenases/reductase superfamily Thermus thermophilus
TtADH
-
 Thermus thermophilus

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
73
-
-
 Thermus thermophilus

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
additional information
-
 the thermal stability of the enzyme adsorbed by ionic exchange is very similar to the stability of the covalently immobilized enzymes in the pH range 5-9, thermal inactivation kinetics, overview Thermus thermophilus
70
-
 after a thermal treatment at pH 7.0 and 70°C for 1 h, the remaining TtADH activity is over 90%, while the soluble protein concentration decreases by a 85% Thermus thermophilus
90
-
 half-life is 30 min Thermus thermophilus

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7
-
-
 Thermus thermophilus

pH Stability

pH Stability pH Stability Maximum Comment Organism
7
-
 after a thermal treatment at pH 7.0 and 70°C for 1 h, the remaining TtADH activity is over 90%, while the soluble protein concentration decreases by a 85% Thermus thermophilus

Cofactor

Cofactor Comment Organism Structure
NAD+
-
 Thermus thermophilus
NADH
-
 Thermus thermophilus