Discovery and Protein Engineering of Biocatalysts for Organic Synthesis

Behrens, Geoffrey A.; Hummel, Anke; Padhi, Santosh Kumar; Schätzle, Sebastian; Bornscheuer, Uwe T.

doi:10.1002/adsc.201100446

Cited by 95 publications

(51 citation statements)

References 264 publications

(290 reference statements)

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“…To overcome these limitations, structure-based protein engineering has been often successfully applied to meet desired biochemical needs (Behrens et al 2011). Yun et al (2005) reported a (S)-selective mutant of V. fluvialis 5-TA which showed reduced product inhibition by aliphatic ketone.…”

Section: Protein Engineeringmentioning

confidence: 99%

Features and technical applications of ω-transaminases

Malik

Park

Shin

2012

Appl Microbiol Biotechnol

188

143

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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: Protein Engineeringmentioning

confidence: 99%

Features and technical applications of ω-transaminases

Malik

Park

Shin

2012

Appl Microbiol Biotechnol

188

143

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“…The improved variants H201S and H201S/K168I showed, respectively, 60% and 100% improved stability towards octanal, while preserving the specific activity of the wt enzyme. M A N U S C R I P T ACCEPTED MANUSCRIPT 7 …”

Section: Improving Lipase Stability By Protein Engineeringmentioning

confidence: 99%

Engineering and application of enzymes for lipid modification, an update

Zorn

Oroz‐Guinea

Brundiek³

et al. 2016

Progress in Lipid Research

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This review first provides a brief introduction into the most important tools and strategies for protein engineering (i.e. directed evolution and rational protein design combined with high-throughput screening methods) followed by examples from literature, in which enzymes have been optimized for biocatalytic applications. This covers engineered lipases with altered fatty acid chain length selectivity, fatty acid specificity and improved performance in esterification reactions. Furthermore, recent achievements reported for phospholipases, lipoxygenases, P450 monooxygenases, decarboxylating enzymes, fatty acid hydratases and the use of enzymes in cascade reactions are treated.

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“…Several comprehensive reviews discussed the discovery and engineering tools developed to obtain naturally evolved or tailor-made enzymes with enhanced properties for chemical synthesis [29,30,40]. In the case of microbial strains isolated from natural environment, enzymes could be discovered through protein purification, insertional mutation, chromosome walking, shotgun library, etc.…”

Section: Discovery and Characterization Of Opbe Reductasesmentioning

confidence: 99%

“…Various enzyme discovery and protein engineering tools have been proposed and proved, which would greatly shorten the developing period and increase the availability of robust enzymes. Several literatures on the biocatalytic asymmetric reduction for pharmaceuticals, protein engineering strategies for robust enzymes in chemical synthesis have been reviewed [28][29][30][31][32]. Also, various OPBE reductases have been successfully identified from natural samples or genome databases.…”

Section: Introductionmentioning

confidence: 99%

Bioreductive preparation of ACE inhibitors precursor (R)-2-hydroxy-4-phenylbutanoate esters: Recent advances and future perspectives

2015

Bioresour. Bioprocess.

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Optically active (R)-2-hydroxy-4-phenylbutanoate esters ((R)-HPBE) are key precursors for the production of angiotension-converting enzyme (ACE) inhibitors, which are important prescriptive drugs for preventing the formation of angiotensin II and lowering the blood pressure. The biocatalytic asymmetric reduction of ethyl 2-oxo-4-phenylbutanoate (OPBE) to (R)-HPBE with carbonyl reductases has several advantageous attributes, including high enantioselectivity, mild reaction condition, high catalytic efficiency, and environmental benignity. An increasing number of OPBE reductases have been discovered owing to the drastic achievements in genomics, screening and evolution technologies, and process engineering. The potential of (R)-HPBE production process has also been intensively evaluated. This review covers recent progress on the bioreductive preparation of (R)-HPBE, especially on various screening approaches for the identification of OPBE reductases and their characterization.

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Discovery and Protein Engineering of Biocatalysts for Organic Synthesis

Cited by 95 publications

References 264 publications

Features and technical applications of ω-transaminases

Features and technical applications of ω-transaminases

Engineering and application of enzymes for lipid modification, an update

Bioreductive preparation of ACE inhibitors precursor (R)-2-hydroxy-4-phenylbutanoate esters: Recent advances and future perspectives

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