Threonine aldolases—an emerging tool for organic synthesis

Steinreiber, Johannes; Fesko, Kateryna; Reisinger, Christoph; Schürmann, Martin; Assema, Friso van; Wolberg, Michael; Mink, Daniel; Griengl, Herfried

doi:10.1016/j.tet.2006.11.035

Cited by 113 publications

(94 citation statements)

References 82 publications

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“…[130] Shifting equilibrium in onepot reactions, without introducing further steps and unit operations, is an effective way to reach this aim, as it was successfully reported. [119,131,132] When one or more reversible reactions are in series with an irreversible one controlling the kinetics, very high yield and selectivity are reached; [103] this is of paramount importance in dynamic processes. [133] Thus, higher yields are a consequence of equilibrium shifts and they result in a reduction of waste and no need for further separation; from the process point of view this means low equipment and operational costs and also a reduction of raw material costs because of the complete conversion of substrates into desired products.…”

Section: The Gain Of One-pot In Biocatalytic Reactionsmentioning

confidence: 99%

Multi‐Enzymatic Cascade Reactions: Overview and Perspectives

Brucher²,

2011

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Multi-enzymatic cascade reactions, i.e., the combination of several enzymatic transformations in concurrent one-pot processes, offer considerable advantages: the demand of time, costs and chemicals for product recovery may be reduced, reversible reactions can be driven to completion and the concentration of harmful or unstable compounds can be kept to a minimum. This review summarizes the developments in multi-enzymatic cascades employed for the asymmetric synthesis of chiral alcohols, amines and amino acids, as well as for C À C bond formation. In addition, a general classification of biocatalytic cascade systems is provided and bioprocess engineering aspects associated with the topic are discussed.

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Section: The Gain Of One-pot In Biocatalytic Reactionsmentioning

confidence: 99%

Multi‐Enzymatic Cascade Reactions: Overview and Perspectives

Brucher²,

2011

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“…The aldol addition of glycine to aldehydes is catalyzed by pyridoxal-5 -phosphatedependent (PLP) lyases such as threonine aldolases (ThrA; EC 4.1.2.5) and serine hydroxymethyl transefrases (SHMTs; EC 2.1.2.1) [16,18,19,[122][123][124][125][126][127][128].…”

Section: Glycine/alanine Aldolasesmentioning

confidence: 99%

Enzyme‐Catalyzed Aldol Additions

Clapés¹,

Joglar²

2013

Modern Methods in Stereoselective Aldol Reactions

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“…For example, a threonine aldolase-catalyzed reaction was initially used to prepare L-83 from glycine 82 and benzaldehyde 81. L-83 was then converted to (R)-84 in high ee by an irreversible decarboxylation catalyzed by L-tyrosine decarboxylase [73].…”

Section: Conclusion and Future Perspectivesmentioning

confidence: 99%

Biocatalytic Routes to Nonracemic Chiral Amines

Turner

Truppo

2010

Chiral Amine Synthesis

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Enantiomerically pure chiral amines are highly valuable functionalized molecules with a wide range of applications including (i) intermediates for the synthesis of pharmaceutical and agrochemical active ingredients, (ii) resolving agents for the separation of enantiomers via diastereomeric salt formation, and (iii) ligands for asymmetric synthesis using either transition metal catalysis or organocatalysis [1]. The option of preparing chiral amines using biocatalytic approaches is now viewed as attractive as a result of recent developments in biocatalyst availability, methods for improving biocatalyst stability, and the inherent high selectivity and catalytic activity that can be obtained through enzyme catalysis. This chapter reviews the methods that are currently available for the preparation of chiral amines using biocatalysis. The review focuses on those biocatalytic methods in which the amine functionality is involved directly in the biocatalytic transformation (e.g., the synthesis of amino alcohols in which the alcohol functionality is manipulated by lipase-catalyzed acylation or hydrolysis are omitted). In addition, biocatalytic methods for the preparation of amino acids are also outside the scope of this review. The chapter is organized according to the three general approaches that have been developed, namely, kinetic resolution (KR), dynamic kinetic resolution (DKR) and deracemization, and finally asymmetric synthesis. A final section deals with emerging approaches including the use of imine reductases. As summarized in Figure 14.1, using a-methylbenzylamine 1 as a model compound, each of the methods discussed in this chapter possesses advantages and disadvantages in terms of (i) availability of starting material, (ii) efficiency of the process (i.e., kinetic resolution versus asymmetric synthesis), (iii) range of chiral amines that can be prepared (1 , 2 , 3 ), (iv) availability of biocatalyst, and (v) possible requirement for cofactor recycling. Each of these issues is dealt with throughout the chapter. Table 14.1 provides details of commercial sources of the enzymes referred to in the text.

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Threonine aldolases—an emerging tool for organic synthesis

Cited by 113 publications

References 82 publications

Multi‐Enzymatic Cascade Reactions: Overview and Perspectives

Multi‐Enzymatic Cascade Reactions: Overview and Perspectives

Enzyme‐Catalyzed Aldol Additions

Biocatalytic Routes to Nonracemic Chiral Amines

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