Investigation of one-​enzyme systems in the ω-​transaminase-​catalyzed synthesis of chiral amines

Kateryna Lypetska (Fesko), Kerstin Steiner, Rolf Breinbauer, Helmut Schwab, Martin Schuermann, Gernot Strohmeier

Research output: Contribution to journalArticleResearchpeer-review

Abstract

ω-​Transaminase (TA) catalyzed asym. syntheses of amines were carried out in the one enzyme systems with wild-​type enzymes (S)​-​TA from Pseudomonas aeruginosa, (S)​-​TA from Paracoccus denitrificans and (R)​-​TA from Aspergillus terreus. The scope of amine donors and arom. carbonyl substrates was thoroughly explored. Among the range of potential amino donors, 2-​propylamine, 2-​butylamine and 1-​phenylethylamine were found as promising candidates, which gave superior conversions in the amination reactions compared to other donors. Various prochiral arom. ketones were accepted as substrates by the investigated enzymes. In most cases, good to excellent conversions (up to 98​%) to the amine products with excellent e.e.-​values (>99.9​% for (S) or (R)​) were obtained by the action of a single enzyme and an appropriate amino donor. (S)​-​TA from Paracoccus denitrificans was found to accept bulky ketones, e.g. 1-​indanone, α- and β-​tetralone or 2-​acetonaphthone, in the asym. amination. In some cases the enantiomeric excesses in the amination reactions were dependent on the amino donor. Moreover, the influence of the pH, temp. and cosolvents on the outcome of reactions was addnl. investigated.
Original languageEnglish
Pages (from-to)103-110
Number of pages7
JournalJournal of molecular catalysis / B
Volume96
DOIs
Publication statusPublished - 2013

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Transaminases
Amination
Amines
Enzymes
Paracoccus denitrificans
Ketones
Tetralones
Aspergillus
Phenethylamines
Substrates
Pseudomonas aeruginosa

Keywords

  • ω-Transaminase; Aminotransferase; Chiral amines; Transamination; Asymmetric synthesis; Biocatalysis

Cite this

Investigation of one-​enzyme systems in the ω-​transaminase-​catalyzed synthesis of chiral amines. / Lypetska (Fesko), Kateryna; Steiner, Kerstin; Breinbauer, Rolf; Schwab, Helmut; Schuermann, Martin; Strohmeier, Gernot.

In: Journal of molecular catalysis / B, Vol. 96, 2013, p. 103-110.

Research output: Contribution to journalArticleResearchpeer-review

Lypetska (Fesko), Kateryna ; Steiner, Kerstin ; Breinbauer, Rolf ; Schwab, Helmut ; Schuermann, Martin ; Strohmeier, Gernot. / Investigation of one-​enzyme systems in the ω-​transaminase-​catalyzed synthesis of chiral amines. In: Journal of molecular catalysis / B. 2013 ; Vol. 96. pp. 103-110.
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abstract = "ω-​Transaminase (TA) catalyzed asym. syntheses of amines were carried out in the one enzyme systems with wild-​type enzymes (S)​-​TA from Pseudomonas aeruginosa, (S)​-​TA from Paracoccus denitrificans and (R)​-​TA from Aspergillus terreus. The scope of amine donors and arom. carbonyl substrates was thoroughly explored. Among the range of potential amino donors, 2-​propylamine, 2-​butylamine and 1-​phenylethylamine were found as promising candidates, which gave superior conversions in the amination reactions compared to other donors. Various prochiral arom. ketones were accepted as substrates by the investigated enzymes. In most cases, good to excellent conversions (up to 98​{\%}) to the amine products with excellent e.e.-​values (>99.9​{\%} for (S) or (R)​) were obtained by the action of a single enzyme and an appropriate amino donor. (S)​-​TA from Paracoccus denitrificans was found to accept bulky ketones, e.g. 1-​indanone, α- and β-​tetralone or 2-​acetonaphthone, in the asym. amination. In some cases the enantiomeric excesses in the amination reactions were dependent on the amino donor. Moreover, the influence of the pH, temp. and cosolvents on the outcome of reactions was addnl. investigated.",
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T1 - Investigation of one-​enzyme systems in the ω-​transaminase-​catalyzed synthesis of chiral amines

AU - Lypetska (Fesko), Kateryna

AU - Steiner, Kerstin

AU - Breinbauer, Rolf

AU - Schwab, Helmut

AU - Schuermann, Martin

AU - Strohmeier, Gernot

PY - 2013

Y1 - 2013

N2 - ω-​Transaminase (TA) catalyzed asym. syntheses of amines were carried out in the one enzyme systems with wild-​type enzymes (S)​-​TA from Pseudomonas aeruginosa, (S)​-​TA from Paracoccus denitrificans and (R)​-​TA from Aspergillus terreus. The scope of amine donors and arom. carbonyl substrates was thoroughly explored. Among the range of potential amino donors, 2-​propylamine, 2-​butylamine and 1-​phenylethylamine were found as promising candidates, which gave superior conversions in the amination reactions compared to other donors. Various prochiral arom. ketones were accepted as substrates by the investigated enzymes. In most cases, good to excellent conversions (up to 98​%) to the amine products with excellent e.e.-​values (>99.9​% for (S) or (R)​) were obtained by the action of a single enzyme and an appropriate amino donor. (S)​-​TA from Paracoccus denitrificans was found to accept bulky ketones, e.g. 1-​indanone, α- and β-​tetralone or 2-​acetonaphthone, in the asym. amination. In some cases the enantiomeric excesses in the amination reactions were dependent on the amino donor. Moreover, the influence of the pH, temp. and cosolvents on the outcome of reactions was addnl. investigated.

AB - ω-​Transaminase (TA) catalyzed asym. syntheses of amines were carried out in the one enzyme systems with wild-​type enzymes (S)​-​TA from Pseudomonas aeruginosa, (S)​-​TA from Paracoccus denitrificans and (R)​-​TA from Aspergillus terreus. The scope of amine donors and arom. carbonyl substrates was thoroughly explored. Among the range of potential amino donors, 2-​propylamine, 2-​butylamine and 1-​phenylethylamine were found as promising candidates, which gave superior conversions in the amination reactions compared to other donors. Various prochiral arom. ketones were accepted as substrates by the investigated enzymes. In most cases, good to excellent conversions (up to 98​%) to the amine products with excellent e.e.-​values (>99.9​% for (S) or (R)​) were obtained by the action of a single enzyme and an appropriate amino donor. (S)​-​TA from Paracoccus denitrificans was found to accept bulky ketones, e.g. 1-​indanone, α- and β-​tetralone or 2-​acetonaphthone, in the asym. amination. In some cases the enantiomeric excesses in the amination reactions were dependent on the amino donor. Moreover, the influence of the pH, temp. and cosolvents on the outcome of reactions was addnl. investigated.

KW - ω-Transaminase; Aminotransferase; Chiral amines; Transamination; Asymmetric synthesis; Biocatalysis

U2 - DOI:10.1016/j.molcatb.2013.06.015

DO - DOI:10.1016/j.molcatb.2013.06.015

M3 - Article

VL - 96

SP - 103

EP - 110

JO - Journal of molecular catalysis / B

JF - Journal of molecular catalysis / B

SN - 1381-1177

ER -