Non-conventional hydrolase chemistry: amide and carbamate bond formation catalyzed by lipases

Gotor, Vicente

doi:10.1016/s0968-0896(99)00150-9

Cited by 149 publications

(70 citation statements)

References 98 publications

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“…In addition to "conventional" substrates (acid and alcohol), lipases can also catalyze the amidation of an acid with an amine or ammonia [52,53]. Ragupathy et al [54] investigated a system of hydrophobic amines and lactones and found that instead of the expected direct amidation of the lactone, first the lactone is hydrolyzed to the ω-hydroxycarboxylic acid and then amidation takes place (see Figure 4).…”

Section: Small Moleculesmentioning

confidence: 99%

Enzymatic Catalysis at Interfaces—Heterophase Systems as Substrates for Enzymatic Action

Weiss

Landfester

2013

Catalysts

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Several important enzymatic reactions occurring in nature, such as, e.g., the digestion of fat, proceed only at the interface of two immiscible phases. Typically, these systems consist of an organic substrate, dispersed in an aqueous continuous phase, with a specialized enzyme capable of working at the interface. For adopting such a system for organic synthesis, a stable heterophase system with a large interfacial area is required. These prerequisites can be found in so-called miniemulsions. Such liquid-liquid heterophase systems feature droplets with sizes smaller than 500 nm, and more importantly, these emulsions do not suffer from Ostwald ripening, as conventional emulsions do. Consequently, the droplets show long-term stability, even throughout reactions conducted in the droplets. In this review, we will briefly discuss the physicochemical background of miniemulsions, provide a comprehensive overview of the enzymatically catalyzed reactions conducted in miniemulsions and, as data are available, to compare the most important features to conventional systems, as reverse microemulsions, (macro)emulsions and solvent-based systems.

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Section: Small Moleculesmentioning

confidence: 99%

Enzymatic Catalysis at Interfaces—Heterophase Systems as Substrates for Enzymatic Action

Weiss

Landfester

2013

Catalysts

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“…This mild method can afford excellent yields of amides in a shorter reaction time (1 h) under room temperature (R.T.) than the results from the reported literature (Scheme 1a). Moreover, compared with traditional amide synthesis catalyzed by lipase using carboxylic acids, anhydrides, or esters as acyl donors reported so far [8][9][10], lipase-mediated oxidative amidation presents the highest catalytic efficiency-even at room temperature. To the best of our knowledge, no other reports have presented the lipase-mediated oxidative formation of amides.…”

Section: Introductionmentioning

confidence: 97%

“…Some methods for the acylation of amines catalyzed by enzyme (lipase, protease, amidase, penicillin G acylase, etc.) have been developed by utilizing carboxylic acids, anhydrides, or esters as acyl donors [8][9][10][11][12][13]. Nevertheless, one of the main drawbacks of enzymatic synthesis of amides is the low reaction rate, which seriously limits its industrial applications.…”

Section: Introductionmentioning

confidence: 99%

Lipase-Mediated Amidation of Anilines with 1,3-Diketones via C–C Bond Cleavage

Zhang

Wang

et al. 2017

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Abstract:In this work, an efficient and green lipase-mediated technique has been mined for the amidation of anilines with 1,3-diketones via C-C bond cleavage. Under the optimal conditions, high yields (64.3%-96.2%) could be obtained when Novozym 435 was used as the catalyst. Furthermore, Novozym 435 exhibited a satisfying reusability and more than 80% of yield can be obtained after seven cycles. This work provides a more rapid and mild strategy for amide synthesis with high yield and expands the application of enzyme in organic synthesis.

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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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Non-conventional hydrolase chemistry: amide and carbamate bond formation catalyzed by lipases

Cited by 149 publications

References 98 publications

Enzymatic Catalysis at Interfaces—Heterophase Systems as Substrates for Enzymatic Action

Enzymatic Catalysis at Interfaces—Heterophase Systems as Substrates for Enzymatic Action

Lipase-Mediated Amidation of Anilines with 1,3-Diketones via C–C Bond Cleavage

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

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