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Literature summary for 2.6.1.B16 extracted from

  • Weiss, M.S.; Pavlidis, I.V.; Spurr, P.; Hanlon, S.P.; Wirz, B.; Iding, H.; Bornscheuer, U.T.
    Amine transaminase engineering for spatially bulky substrate acceptance (2017), ChemBioChem, 18, 1022-1026 .
    View publication on PubMed

Application

Application Comment Organism
synthesis amine transaminase (ATA) catalyzing stereoselective amination of prochiral ketones is an attractive alternative to transition metal catalysis Ruegeria sp. TM1040

Protein Variants

Protein Variants Comment Organism
additional information mutational analysis of enzyme-substrate interactions and substrate specificity, overview Ruegeria sp. TM1040
P281S site-directed mutagenesis, the mutation seems to have a negative effect on specific activity Ruegeria sp. TM1040
Y152F site-directed mutagenesis, the mutation stabilizes the enzyme, the activity is slightly reduced compared to wild-type Ruegeria sp. TM1040
Y59W/T231A site-directed mutagenesis, inactive mutant Ruegeria sp. TM1040
Y59W/Y87F/T231A site-directed mutagenesis, inactive mutant Ruegeria sp. TM1040
Y59W/Y87L/T231A site-directed mutagenesis, specific and enantioimeric conversion of 2,2-dimethyl-1-phenylpropan-1-amine compared to wild-type Ruegeria sp. TM1040
Y59W/Y87L/T231A/G429A site-directed mutagenesis, specific and enantioimeric conversion of 2,2-dimethyl-1-phenylpropan-1-amine compared to wild-type Ruegeria sp. TM1040
Y59W/Y87L/T231A/L382M site-directed mutagenesis, specific and enantioimeric conversion of 2,2-dimethyl-1-phenylpropan-1-amine compared to wild-type Ruegeria sp. TM1040
Y59W/Y87L/T231A/L382M/G429A site-directed mutagenesis, specific and enantioimeric conversion of 2,2-dimethyl-1-phenylpropan-1-amine compared to wild-type Ruegeria sp. TM1040
Y59W/Y87L/Y152F/T231A/L382M/G429A site-directed mutagenesis, specific and enantioimeric conversion of 2,2-dimethyl-1-phenylpropan-1-amine compared to wild-type Ruegeria sp. TM1040
Y59W/Y87V/T231A site-directed mutagenesis Ruegeria sp. TM1040

Organism

Organism UniProt Comment Textmining
Ruegeria sp. TM1040
-
-
-

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
0.0065
-
pH 8.0, 30°C, substrate rac-2,2-dimethyl-1-phenylpropan-1-amine, mutant Y59W/Y87V/T231A Ruegeria sp. TM1040
0.0115
-
pH 8.0, 30°C, substrate rac-2,2-dimethyl-1-phenylpropan-1-amine, mutant Y59W/Y87L/T231A Ruegeria sp. TM1040
0.019
-
pH 8.0, 30°C, substrate rac-2,2-dimethyl-1-phenylpropan-1-amine, mutant Y59W/Y87L/T231A/L382M Ruegeria sp. TM1040
0.0324
-
pH 8.0, 30°C, substrate rac-2,2-dimethyl-1-phenylpropan-1-amine, mutant Y59W/Y87L/T231A/P281S/G429A Ruegeria sp. TM1040
0.0448
-
pH 8.0, 30°C, substrate rac-2,2-dimethyl-1-phenylpropan-1-amine, mutant Y59W/Y87L/T231A/G429A Ruegeria sp. TM1040
0.0771
-
pH 8.0, 30°C, substrate rac-2,2-dimethyl-1-phenylpropan-1-amine, mutant Y59W/Y87L/T231A/L382M/G429A Ruegeria sp. TM1040

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2,2-dimethyl-1-phenylpropan-1-one + isopropylamine the conversion by all active enzyme mutants lays between 22 and 71% with isopropylamine as amine donor, with enantiomeric excess above 99%, low activity Ruegeria sp. TM1040 (R)-2,2-dimethyl-1-phenylpropan-1-amine + acetone
-
r
2,2-dimethyl-1-phenylpropan-1-one + L-alanine the conversion by all active enzyme mutants is complete with L-alanine as amine donor, with enantiomeric excess above 99% Ruegeria sp. TM1040 (R)-2,2-dimethyl-1-phenylpropan-1-amine + pyruvate
-
r
additional information engineered ATAs perform asymmetric synthesis of the respective R-amine with high conversions by using either alanine or isopropylamine as amine donor. Asymmetric synthesis of (R)-2,2-dimethyl-1-phenylpropan-1-amine by amino group transfer to 2,2-dimethyl-1-phenylpropan-1-one catalyzed by ATAs. Isopropylamine or alanine serve as the amine donors. Analysis of specific activities of Rsp-ATA mutant variants towards rac-amine 2,2-dimethyl-1-phenylpropan-1-amine. Enzyme-ligand interaction analysis, overview Ruegeria sp. TM1040 ?
-
-
rac-2,2-dimethyl-1-phenylpropan-1-amine + pyruvate
-
Ruegeria sp. TM1040 2,2-dimethyl-1-phenylpropan-1-one + L-alanine
-
r

Synonyms

Synonyms Comment Organism
amine transaminase
-
Ruegeria sp. TM1040
ATA
-
Ruegeria sp. TM1040
Rsp-ATA
-
Ruegeria sp. TM1040

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
30
-
assay at Ruegeria sp. TM1040

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
8 9 assay at Ruegeria sp. TM1040

Cofactor

Cofactor Comment Organism Structure
pyridoxal 5'-phosphate PLP, dependent on Ruegeria sp. TM1040

General Information

General Information Comment Organism
evolution the ATA enzyme from Ruegeria sp. TM1040 (Rsp-ATA, PDB ID 3FCR) belongs to the ATAs of fold class I Ruegeria sp. TM1040