Synthesis of (1R,3R)-1-amino-3-methylcyclohexane by an enzyme cascade reaction

Skalden, Lilly; Peters, Christin; Ratz, Lukas; Bornscheuer, Uwe T.

doi:10.1016/j.tet.2015.11.005

Cited by 20 publications

(27 citation statements)

References 37 publications

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“…The OD 600 normalized SDS‐PAGE analysis (Figure S2) reveals that the tested variants were produced. Variant XenB T25D/Y66T did not yield any protein after affinity purification, confirming recent reports, so XenB studies were not further pursued. Mutagenesis and expression problems can sometimes be solved by changing the plasmid backbone to smaller or newest‐generation plasmids.…”

Section: Resultssupporting

confidence: 73%

“…Reports of facial selectivity for group 2 members are rare. XenA wt favours ( S )‐ 2 (>99 %), like almost all other OYE wts, and only YqjM wt produces ( R )‐ 2 , with 76 % ee . We expected that TsER wt and DrER wt, with their structurally almost identical active sites, would likewise produce the R enantiomer .…”

Section: Resultsmentioning

confidence: 94%

“…Engineered residues were selected to represent both OYE groups . Wild‐type scaffolds were partially selected on the basis of established potential as biocatalysts in cascade reactions, large‐scale synthesis, use of NAD(P)H mimics or stability . With this setup, we were interested in testing OYE family specific response when applying the scaffold sampling strategy.…”

Section: Introductionmentioning

confidence: 99%

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Revealing Additional Stereocomplementary Pairs of Old Yellow Enzymes by Rational Transfer of Engineered Residues

et al. 2017

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Every year numerous protein engineering and directed evolution studies are published, increasing the knowledge that could be used by protein engineers. Here we test a protein engineering strategy that allows quick access to improved biocatalysts with very little screening effort. Conceptually it is assumed that engineered residues previously identified by rational and random methods induce similar improvements when transferred to family members. In an application to ene-reductases from the Old Yellow Enzyme (OYE) family, the newly created variants were tested with three compounds, revealing more stereocomplementary OYE pairs with potent turnover frequencies (up to 660 h ) and excellent stereoselectivities (up to >99 %). Although systematic prediction of absolute enantioselectivity of OYE variants remains a challenge, "scaffold sampling" was confirmed as a promising addition to protein engineers' collection of strategies.

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Section: Resultssupporting

confidence: 73%

Section: Resultsmentioning

confidence: 94%

Section: Introductionmentioning

confidence: 99%

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Revealing Additional Stereocomplementary Pairs of Old Yellow Enzymes by Rational Transfer of Engineered Residues

et al. 2017

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“…Two small changes gave improved diastereoselectivity (up to 97 % de ). Following this, the enoate reductase was modified to give better enantioselectivity in the reduction of 2 . The stereochemistry at the beta‐position is determined by the ene‐reductase, and the amine stereochemistry is controlled by the transaminase.…”

Section: Enabling Technologymentioning

confidence: 99%

“…Following this, the enoate reductase was modified to give better enantioselectivity in the reduction of 2. [5] The stereochemistry at the beta-position is determined by the ene-reductase, and the amine stereochemistry is controlled by the transaminase. Although this is a good example of coexpression and engineering of enzymes, lactate dehydrogenase and glucose dehydrogenase required for cofactor regeneration still had to be added separately.…”

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confidence: 99%

The Impact of Recent Developments in Technologies which Enable the Increased Use of Biocatalysts

Foley

Maguire

2019

Eur J Org Chem

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While biocatalytic transformations are very powerful in enantioselective synthesis, frequently occurring under mild conditions, and proceed with extraordinary selectivity, there are practical challenges associated with the use of biocatalysis, such as limited substrate scope, stability, and reusability. Recent technological developments, for example immobilization, continuous flow, and molecular biology, all contribute towards enhancing the use of enzymes in synthesis.

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Recent Advances in Selective Biocatalytic (Hydrogen Transfer) Reductions

Gonzalo

Lavandera

2019

Homogeneous Hydrogenation With Non‐Precious Catalysts

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Synthesis of (1R,3R)-1-amino-3-methylcyclohexane by an enzyme cascade reaction

Cited by 20 publications

References 37 publications

Revealing Additional Stereocomplementary Pairs of Old Yellow Enzymes by Rational Transfer of Engineered Residues

Revealing Additional Stereocomplementary Pairs of Old Yellow Enzymes by Rational Transfer of Engineered Residues

The Impact of Recent Developments in Technologies which Enable the Increased Use of Biocatalysts

Recent Advances in Selective Biocatalytic (Hydrogen Transfer) Reductions

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