Metabolically driven equilibrium shift of asymmetric amination of ketones by ω-transaminase using alanine as an amino donor

Han, Shunsheng; Shin, Jaeyoung

doi:10.1080/09168451.2014.930328

Cited by 7 publications

(3 citation statements)

References 21 publications

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“…A combination of shifting the equilibrium while simultaneously removing the desired amine product from the reaction phase would be desired. In fact, several drawbacks from using IPA as amine donor are evident: While there can be little to now activity of wild type amine transaminases towards IPA 12,13 , also undesired side reactions can arise from the basicity of the amine donor. 14 Furthermore, IPA is highly toxic, derived fossil resources and complicates the downstream processing, which stands in the way of a sustainable production process with little residual, polluting waste streams.…”

Section: Introductionmentioning

confidence: 99%

Extractivein situproduct removal for the application of naturally producedl-alanine as an amine donor in enzymatic metaraminol production

et al. 2021

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Section: Introductionmentioning

confidence: 99%

Extractivein situproduct removal for the application of naturally producedl-alanine as an amine donor in enzymatic metaraminol production

et al. 2021

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“…Similar approaches employed a pyruvate decarboxylase (Scheme b) and a metabolically driven equilibrium shift that uses the native metabolism of the cell was designed by Han and Shin . The carbon-starved E.…”

Section: Engineeringmentioning

confidence: 92%

Discovery, Engineering, and Synthetic Application of Transaminase Biocatalysts

et al. 2017

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Transaminases have attracted considerable interest in their use as biocatalysts for the synthesis of compounds containing chiral amine units, which are widespread within the pharmaceutical, agrochemical, and fine chemical industry. Recent developments in enzyme- and process-engineering have expedited their use in asymmetric synthesis; however, industrial applications are still hindered by a number of factors, including equilibrium thermodynamics, product inhibition, and poor substrate tolerance. Detailed and comprehensive approaches to each of these challenges have been reported during the last two decades; the most representative enzyme discovery and screening strategies, protein and equilibrium engineering, and immobilization techniques are reviewed herein. Furthermore, we present a detailed look into the applications of transaminases for the synthesis of a variety of amine-containing compounds and the integration of transaminases into multienzymatic systems that allow access to a variety of highly complex products for the end user.

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“…Because the structure of the donor and the acceptor might differ and because the reaction is reversible, the enzymes accept 2 different amines as amino donors, which is known as dual substrate recognition . As a further consequence of the reversibility of the transamination, subsequent reaction steps or product separation are required in biosynthetic applications . Other members of the family of PLP‐dependent enzymes include lyases, oxidoreductases, and hydrolases .…”

Section: Introductionmentioning

confidence: 99%

The ω‐transaminase engineering database (oTAED): A navigation tool in protein sequence and structure space

et al. 2018

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The ω-Transaminase Engineering Database (oTAED) was established as a publicly accessible resource on sequences and structures of the biotechnologically relevant ω-transaminases (ω-TAs) from Fold types I and IV. The oTAED integrates sequence and structure data, provides a classification based on fold type and sequence similarity, and applies a standard numbering scheme to identify equivalent positions in homologous proteins. The oTAED includes 67 210 proteins (114 655 sequences) which are divided into 169 homologous families based on global sequence similarity. The 44 and 39 highly conserved positions which were identified in Fold type I and IV, respectively, include the known catalytic residues and a large fraction of glycines and prolines in loop regions, which might have a role in protein folding and stability. However, for most of the conserved positions the function is still unknown. Literature information on positions that mediate substrate specificity and stereoselectivity was systematically examined. The standard numbering schemes revealed that many positions which have been described in different enzymes are structurally equivalent. For some positions, multiple functional roles have been suggested based on experimental data in different enzymes. The proposed standard numbering schemes for Fold type I and IV ω-TAs assist with analysis of literature data, facilitate annotation of ω-TAs, support prediction of promising mutation sites, and enable navigation in ω-TA sequence space. Thus, it is a useful tool for enzyme engineering and the selection of novel ω-TA candidates with desired biochemical properties.

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Metabolically driven equilibrium shift of asymmetric amination of ketones by ω-transaminase using alanine as an amino donor

Cited by 7 publications

References 21 publications

Extractivein situproduct removal for the application of naturally producedl-alanine as an amine donor in enzymatic metaraminol production

Extractivein situproduct removal for the application of naturally producedl-alanine as an amine donor in enzymatic metaraminol production

Discovery, Engineering, and Synthetic Application of Transaminase Biocatalysts

The ω‐transaminase engineering database (oTAED): A navigation tool in protein sequence and structure space

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