A template-based mnemonic for monoamine oxidase (MAO-N) catalyzed reactions and its application to the chemo-enzymatic deracemisation of the alkaloid (±)-crispine A

Bailey, Kevin; Ellis, Andrew J.; Reiss, Renate; Snape, Timothy J.; Turner, Nicholas J.

doi:10.1039/b710456a

Cited by 90 publications

(46 citation statements)

References 17 publications

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“…Biocatalytic synthesis with purified enzymes, including aldolases, 1 epoxide hydrolases, 2 Baeyer-Villigerases, 3 amine oxidases, 4 lipases, 5 and alcohol dehydrogenases, 6 is emerging as a viable alternative to traditional asymmetric synthesis. The recent transaminase-based asymmetric synthesis of the Januvia™ core by the Merck-Codexis team highlights the viability of such approaches, and was recognized with the 2010 Presidential Green Challenge Award.…”

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confidence: 99%

“…The L-β 3 -phenylalanine building block, in turn, is useful for the assembly of β-peptides, 30 whereas the D-β-hydroxy ester obtained directly from the CaADH reduction serves is a precursor for the important anti-depressent, fluoxetine. 31 Finally, the D-γ-hydroxy ester itself is a valuable chiron for the assembly of crytophycin, 32 and L-γ 4 -homophenylalanine is as useful monomer for γ-peptides. 33 …”

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confidence: 99%

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A new dehydrogenase from Clostridium acetobutylicum for asymmetric synthesis: dynamic reductive kinetic resolution entry into the Taxotère side chain

et al. 2011

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A new dehydrogenase from Clostridium acetobutylicum for asymmetric synthesis: dynamic reductive kinetic resolution entry into the Taxotère side chain

et al. 2011

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“…55 In our group, a completely different approach was applied to obtain optically pure tert -amines: in the asymmetric key step, an enzyme catalyzed C–C bond was formed in an aerobic oxidative enantioselective reaction by employing the berberine bridge enzyme (BBE) (Scheme 12). BBE transforms the natural substrate ( S )-reticuline to ( S )-scoulerine at the expense of molecular oxygen.…”

Section: Tertiary Aminesmentioning

confidence: 99%

Asymmetric Preparation of prim-, sec-, and tert-Amines Employing Selected Biocatalysts

Kroutil

Fischereder

Fuchs

et al. 2013

Org. Process Res. Dev.

117

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This account focuses on the application of ω-transaminases, lyases, and oxidases for the preparation of amines considering mainly work from our own lab. Examples are given to access α-chiral primary amines from the corresponding ketones as well as terminal amines from primary alcohols via a two-step biocascade. 2,6-Disubstituted piperidines, as examples for secondary amines, are prepared by biocatalytical regioselective asymmetric monoamination of designated diketones followed by spontaneous ring closure and a subsequent diastereoselective reduction step. Optically pure tert-amines such as berbines and N-methyl benzylisoquinolines are obtained by kinetic resolution via an enantioselective aerobic oxidative C–C bond formation.

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“…This model was successfully used to predict the deracemization of racemic crispine A 72, an alkaloid with potent biological activity (Figure 14.38) [51]. Recently, in collaboration with scientists at the University of York, the crystal structure of MAO-N D5 has been determined at 1.8 A resolution (Figure 14.4) [52].…”

Section: Deracemization Reactions Using Amine Oxidasesmentioning

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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A template-based mnemonic for monoamine oxidase (MAO-N) catalyzed reactions and its application to the chemo-enzymatic deracemisation of the alkaloid (±)-crispine A

Abstract: A template-based mnemonic has been developed for the enzyme monoamine oxidase from Aspergillus niger and has been used to successfully identify the alkaloid (+/-)-crispine A as a target for chemo-enzymatic deracemisation yielding the biologically active (R)-enantiomer in 97% e.e.

Cited by 90 publications

References 17 publications

A new dehydrogenase from Clostridium acetobutylicum for asymmetric synthesis: dynamic reductive kinetic resolution entry into the Taxotère side chain

A new dehydrogenase from Clostridium acetobutylicum for asymmetric synthesis: dynamic reductive kinetic resolution entry into the Taxotère side chain

Asymmetric Preparation of prim-, sec-, and tert-Amines Employing Selected Biocatalysts

Biocatalytic Routes to Nonracemic Chiral Amines

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