Production and properties of threonine aldolase immobilisates

Kurjatschij, Sandra; Katzberg, Michael; Bertau, Martin

doi:10.1016/j.molcatb.2014.01.021

Cited by 7 publications

(2 citation statements)

References 32 publications

(31 reference statements)

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“…coli on different supports was studied to increase the stability of the enzyme. The entrapment into a matrix of orthosilicate gel was the most promising immobilization method (Kurjatschij et al 2014 ). In another study, l TA from T .…”

Section: Enzyme Engineeringmentioning

confidence: 99%

Threonine aldolases: perspectives in engineering and screening the enzymes with enhanced substrate and stereo specificities

Fesko

2016

Appl Microbiol Biotechnol

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Threonine aldolases have emerged as a powerful tool for asymmetric carbon-carbon bond formation. These enzymes catalyse the unnatural aldol condensation of different aldehydes and glycine to produce highly valuable β-hydroxy-α-amino acids with complete stereocontrol at the α-carbon and moderate specificity at the β-carbon. A range of microbial threonine aldolases has been recently recombinantly produced by several groups and their biochemical properties were characterized. Numerous studies have been conducted to improve the reaction protocols to enable higher conversions and investigate the substrate scope of enzymes. However, the application of threonine aldolases in organic synthesis is still limited due to often moderate yields and low diastereoselectivities obtained in the aldol reaction. This review briefly summarizes the screening techniques recently applied to discover novel threonine aldolases as well as enzyme engineering and mutagenesis studies which were accomplished to improve the catalytic activity and substrate specificity. Additionally, the results from new investigations on threonine aldolases including crystal structure determinations and structural-functional characterization are reviewed.

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Section: Enzyme Engineeringmentioning

confidence: 99%

Threonine aldolases: perspectives in engineering and screening the enzymes with enhanced substrate and stereo specificities

Fesko

2016

Appl Microbiol Biotechnol

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“…Due to a mixture of racemates, tedious and expensive resolution and purification steps are needed to obtain optically pure products . Therefore, enzymatic synthesis of chiral β-hydroxy-α-amino acids by LTA (Scheme B) requires more attention attributed to its advantages such as high diastereoselectivity, high atom-efficiency, mild reaction conditions (neutral pH, room temperature), and environmental friendliness. − …”

mentioning

confidence: 99%

Construction of a Highly Diastereoselective Aldol Reaction System with l-Threonine Aldolase by Computer-Assisted Rational Molecular Modification and Medium Engineering

Zheng

Chen

Wang³

et al. 2020

Org. Lett.

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Diastereoselectivity of l-threonine aldolase (LTA) was determined by paths of aldehydes attacking a pyridoxal phosphate–glycine complex. Thus, strategies of enhancing the syn path and blocking the anti path were performed to modify LTA. A mutant (Y31H/N305R) was constructed with a substrate preference increase from 3.32 to 42.04. Medium engineering was investigated. Consequently, the de value of l-syn-3-[4-(methylsulfonyl)phenylserine] reached 93.1% (87.2%conv). The study clarified the factors affecting diastereoselectivity of LTA and provided a theorem for rational modification of LTA’s diastereoselectivity.

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Biocatalyzed Carbon–Carbon bond formation in enantioselective synthesis

Gamenara,

Seoane

2024

Biocatalysis in Asymmetric Synthesis

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Production and properties of threonine aldolase immobilisates

Cited by 7 publications

References 32 publications

Threonine aldolases: perspectives in engineering and screening the enzymes with enhanced substrate and stereo specificities

Threonine aldolases: perspectives in engineering and screening the enzymes with enhanced substrate and stereo specificities

Construction of a Highly Diastereoselective Aldol Reaction System with l-Threonine Aldolase by Computer-Assisted Rational Molecular Modification and Medium Engineering

Biocatalyzed Carbon–Carbon bond formation in enantioselective synthesis

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