Asymmetric synthesis of chiral amines with ?-transaminase

Shin, Jong‐Shik; Kim, Byung‐Gee

doi:10.1002/(sici)1097-0290(19991020)65:2<206::aid-bit11>3.0.co;2-9

Cited by 200 publications

(111 citation statements)

References 28 publications

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“…The Greek letter "w" in this trivial name is not relevant to the actual position of the amino group relative to the carbon atom bonded to a carboxyl group but represents all non-α positions. Early studies on transaminase-catalyzed chiral amine production adopted the same convention in the enzyme nomenclature (Shin and Kim 1997, 1998, 1999a. Therefore, w-TA (or w-amino acid transaminase) is a trivial name designating all transaminases in the subgroup II.…”

Section: Enzyme Nomenclaturementioning

confidence: 99%

Features and technical applications of ω-transaminases

Malik

Park

Shin

2012

Appl Microbiol Biotechnol

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Chiral amines in enantiopure forms are important chemical building blocks, which are most well recognized in the pharmaceutical industries for imparting desirable biological activity to chemical entities. A number of synthetic strategies to produce chiral amines via biocatalytic as well as chemical transformation have been developed. Recently, ω-transaminase (ω-TA) has attracted growing attention as a promising catalyst which provides an environment-friendly access to production of chiral amines with exquisite stereoselectivity and excellent catalytic turnover. To obtain enantiopure amines using ω-TAs, either kinetic resolution of racemic amines or asymmetric amination of achiral ketones is employed. The latter is usually preferred because of twofold higher yield and no requirement of conversion of a ketone product back to racemic amine. However, the choice of a production process depends on several factors such as reaction equilibrium, substrate reactivity, enzyme inhibition, and commercial availability of substrates. This review summarizes the biochemical features of ω-TA, including reaction chemistry, substrate specificity, and active site structure, and then introduces recent advances in expanding the scope of ω-TA reaction by protein engineering and public database searching. We also address crucial factors to be considered for the development of efficient ω-TA processes.

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Section: Enzyme Nomenclaturementioning

confidence: 99%

Features and technical applications of ω-transaminases

Malik

Park

Shin

2012

Appl Microbiol Biotechnol

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185

146

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“…A typical example is the amination of acetophenone with alanine to produce (S)--MBA, where the equilibrium constant of transamination is 8:81 Â 10 À4 , and (S)--MBA and pyruvate are much more reactive transamination substrates than acetopheone or L-alanine. 7) Hence at least one of the products must be removed during the reaction to shift the equilibrium and reduce product inhibition. 8) We have reported that the synthetic yield of a whole-cell reaction using Vibrio fluvialis JS17, in which pyruvate was removed by cellular metabolism, was much higher than that of the cell-free reaction.…”

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confidence: 99%

“…8) We have reported that the synthetic yield of a whole-cell reaction using Vibrio fluvialis JS17, in which pyruvate was removed by cellular metabolism, was much higher than that of the cell-free reaction. 7) In this study, we constructed a recombinant E. coli co-expressing !-TA and acetolactate synthase (ALS). ALS catalyses the formation of one molecule of acetolactate from two molecules of pyruvate, and acetolactate is spontaneously decomposed to acetoin.…”

mentioning

confidence: 99%

Asymmetric Synthesis of (S)-α-Methylbenzylamine by RecombinantEscherichia coliCo-Expressing Omega-Transaminase and Acetolactate Synthase

Yun¹,

Kim²

2008

Bioscience, Biotechnology, and Biochemistry

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“…Two approaches were employed based upon kinetic resolution, which has been discussed above, and asymmetric synthesis. The asymmetric synthesis approach starts with a [58,59]. Severe inhibition of the transaminase by the amine and keto-acid reaction products, as well as extremely poor conversion, were observed.…”

Section: Asymmetric Synthesis Of Amines Using Transaminasesmentioning

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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Asymmetric synthesis of chiral amines with ?-transaminase

Cited by 200 publications

References 28 publications

Features and technical applications of ω-transaminases

Features and technical applications of ω-transaminases

Asymmetric Synthesis of (S)-α-Methylbenzylamine by RecombinantEscherichia coliCo-Expressing Omega-Transaminase and Acetolactate Synthase

Biocatalytic Routes to Nonracemic Chiral Amines

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