Enzymatic Aminolysis and Ammonolysis Processes in the Preparation of Chiral Nitrogenated Compounds

Gotor‐Fernández, Vicente; Gotor, Vicente

doi:10.2174/138527206777698084

Cited by 70 publications

(23 citation statements)

References 74 publications

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“…Biocatalytic options to prepare optically active amines11,12 involve the use of (i) hydrolases such as amidases, proteases and lipases either in a kinetic resolution13 or dynamic kinetic resolution14,15 as well as (ii) monoamine oxidases16–18 in combination with a reducing agent. Pyridoxal 5′‐phosphate (PLP)‐dependent ω‐transaminases represent a third option, which has received tremendous attention during the last few years,19–33 leading recently also to the launch of an industrial process 34–36.…”

Section: Methodsmentioning

confidence: 99%

Stereoselectivity of Four (R)‐Selective Transaminases for the Asymmetric Amination of Ketones

et al. 2011

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Four (R)-w-transaminases originating from Hyphomonas neptunium (HN-wTA), Aspergillus terreus (AT-wTA) and Arthrobacter sp. (ArRwTA), as well as an evolved transaminase (ArRmut11-wTA) were successfully employed for the amination of prochiral ketones leading to optically pure (R)-amines. The first three transaminases displayed perfect stereoselectivity for the amination of all substrates tested (ee > 99%). Furthermore, the transaminase AT-wTA led in most cases to better conversion than ArR-wTA and HN-wTA using d-alanine as amine donor. a-Tetralone, which was the only substrate not accepted by HN-wTA, ArR-wTA, and AT-wTA, was successfully transformed with perfect enantioselectivity (ee > 99%) into the corresponding optically pure amine employing the variant ArRmut11-wTA.

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Section: Methodsmentioning

confidence: 99%

Stereoselectivity of Four (R)‐Selective Transaminases for the Asymmetric Amination of Ketones

et al. 2011

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“…Biocatalysis allows the use of esters or the direct use of carboxylic acids to obtain amides, which is advantageous from economic and environmental viewpoints. [30] To date, very little has been reported regarding enzymatic syntheses of endocannabinoids. Under various reaction conditions and using Candida antarctica B lipase immobilized on an acrylic resin, the preparation of some unsaturated fatty acylethanolamines has been reported.…”

Section: Introductionmentioning

confidence: 99%

Improved Enzymatic Procedure for the Synthesis of Anandamide and N‐Fatty Acylalkanolamine Analogues: A Combination Strategy to Antitumor Activity

et al. 2015

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Twenty N-fatty acylamines from linolenic and arachidonic acids, fifteen of them new compounds, were obtained through Candida antarctica B lipase-catalyzed esterification and aminolysis reactions in very good yields and with high chemoselectivity. The optimal reaction conditions were achieved by studying the reaction parameters (temperature, E/S ratio, alcohol and alkanolamine/fatty acid ratio, time, solvent, free-solvent system, etc.). To identify ideal enzymatic methods for generating the alkanolamides we evaluated enzyme performance in three procedures: i) aminolysis of ethyl ester, ii) direct condensation between the fatty acid and the alkanolamine, and iii) a

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“…Racemic amines have been resolved by acylation or deacylation using lipases or proteases [1,2] or by oxidation using amine oxidases. [3] Enantioselective acylation combined with chemical racemization of the amines [1,2,4] and enantioselective oxidation combined with non-selective chemical reduction of the imine product [3] have allowed deracemization reactions giving > 50% yields in some cases. Enzymatic hydrolysis of the oxalamic esters of racemic amines has also been described for the preparation of chiral secondary amines.…”

Section: Introductionmentioning

confidence: 99%

Preparation of (R)‐Amines from Racemic Amines with an (S)‐Amine Transaminase from Bacillus megaterium

et al. 2008

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Screening was carried out to identify strains useful for the preparation of (R)-1-cyclopropylethylamine and (R)-sec-butylamine by resolution of the racemic amines with an (S)-specific transaminase. Several Bacillus megaterium strains from our culture collection as well as several soil isolates were found to have the desired activity for the resolution of the racemic amines to give the (R)-enantiomers. Using an extract of the best strain, Bacillus megaterium SC6394, the reaction was shown to be a trans-A C H T U N G T R E N N U N G amination requiring pyruvate as amino acceptor and pyridoxal phosphate as a cofactor. Initial batches of both amines were produced using whole cells of Bacillus megaterium SC6394. The transaminase was purified to homogeneity to obtain N-terminal as well as internal amino acid sequences. The sequences were used to design polymerase chain reaction (PCR) primers to enable cloning and expression of the trans-A C H T U N G T R E N N U N G aminase in E. coli SC16578. In contrast to the original B. megaterium process, pH control and aeration were not required for the resolution of sec-butyl-A C H T U N G T R E N N U N G amine and an excess of pyruvate was not consumed by the recombinant cells. The resolution of sec-butylamine (0.68 M) using whole cells of E. coli SC16578 was scaled up to give (R)-sec-butylamine· 1 = 2 H 2 SO 4 in 46.6% isolated yield with 99.2% ee. An alternative isolation procedure was also used to isolate (R)-secbutylamine as the free base.

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Enzymatic Aminolysis and Ammonolysis Processes in the Preparation of Chiral Nitrogenated Compounds

Cited by 70 publications

References 74 publications

Stereoselectivity of Four (R)‐Selective Transaminases for the Asymmetric Amination of Ketones

Stereoselectivity of Four (R)‐Selective Transaminases for the Asymmetric Amination of Ketones

Improved Enzymatic Procedure for the Synthesis of Anandamide and N‐Fatty Acylalkanolamine Analogues: A Combination Strategy to Antitumor Activity

Preparation of (R)‐Amines from Racemic Amines with an (S)‐Amine Transaminase from Bacillus megaterium

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