Transketolase from Escherichia coli: A practical procedure for using the biocatalyst for asymmetric carbon-carbon bond synthesis

Morris, Katie; Smith, Mark E.; Turner, Nicholas J.; Lilly, M. D.; Mitra, Robin; Woodley, John M.

doi:10.1016/0957-4166(96)00266-2

Cited by 80 publications

(32 citation statements)

References 11 publications

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“…Petroleum ether (bp 40–60 °C) was freshly distilled before usage. Lithium hydroxypyruvate was obtained both commercially and synthesized as previously described …”

Section: Methodsmentioning

confidence: 99%

Separating Thermodynamics from Kinetics—A New Understanding of the Transketolase Reaction

et al. 2017

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Transketolase catalyzes asymmetric C−C bond formation of two highly polar compounds. Over the last 30 years, the reaction has unanimously been described in literature as irreversible because of the concomitant release of CO2 if using lithium hydroxypyruvate (LiHPA) as a substrate. Following the reaction over a longer period of time however, we have now found it to be initially kinetically controlled. Contrary to previous suggestions, for the non‐natural conversion of synthetically more interesting apolar substrates, the complete change of active‐site polarity is therefore not necessary. From docking studies it was revealed that water and hydrogen‐bond networks are essential for substrate binding, thus allowing aliphatic aldehydes to be converted in the charged active site of transketolase.

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“…Petroleum ether (bp 40–60 °C) was freshly distilled before usage. Lithium hydroxypyruvate was obtained both commercially and synthesized as previously described …”

Section: Methodsmentioning

confidence: 99%

Separating Thermodynamics from Kinetics—A New Understanding of the Transketolase Reaction

et al. 2017

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“…All chemicals were obtained from Sigma and used as supplied, except β -hydroxypyruvate (HPA) which was prepared as the lithium salt by modification of a previously described procedure (Morris et al, 1996). …”

Section: Methodsmentioning

confidence: 99%

Directed evolution to re-adapt a co-evolved network within an enzyme

Strafford

Payongsri

Hibbert

et al. 2012

Journal of Biotechnology

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“…TK accepts a large number of aldehydes as substrates [59,67,106], in particular those containing an a-hydroxy group in 2R con®guration; the products are ketoses with a 3 S,4R con®gur-ation (threo con®guration) [27,31]. As an example, TK from spinach can catalyse a reaction between 2,3-dihydroxybutyraldehyde and hydroxypyruvate, yielding a mixture of 6-deoxy-D-fructose and 6-deoxy-L-sorbose [53] which can serve as precursors of 2,5-dimethyl-4-hydroxy-3(2H)-furanone (furaneol), an important industrial aromatic product with caramel-like¯avour used in the food industry [54].…”

Section: Industrial Uses Of Tkmentioning

confidence: 99%

Properties and functions of the thiamin diphosphate dependent enzyme transketolase

Schenk

Duggleby

Nixon

1998

The International Journal of Biochemistry & Cell Biology

226

164

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This review highlights recent research on the properties and functions of the enzyme transketolase, which requires thiamin diphosphate and a divalent metal ion for its activity. The transketolase-catalysed reaction is part of the pentose phosphate pathway, where transketolase appears to control the non-oxidative branch of this pathway, although the overall¯ux of labelled substrates remains controversial. Yeast transketolase is one of several thiamin diphosphate dependent enzymes whose three-dimensional structures have been determined. Together with mutational analysis these structural data have led to detailed understanding of thiamin diphosphate catalysed reactions. In the homodimer transketolase the two catalytic sites, where dihydroxyethyl groups are transferred from ketose donors to aldose acceptors, are formed at the interface between the two subunits, where the thiazole and pyrimidine rings of thiamin diphosphate are bound. Transketolase is ubiquitous and more than 30 full-length sequences are known. The encoded protein sequences contain two motifs of high homology; one common to all thiamin diphosphate-dependent enzymes and the other a unique transketolase motif. All characterised transketolases have similar kinetic and physical properties, but the mammalian enzymes are more selective in substrate utilisation than the nonmammalian representatives. Since products of the transketolase-catalysed reaction serve as precursors for a number of synthetic compounds this enzyme has been exploited for industrial applications. Putative mutant forms of transketolase, once believed to predispose to disease, have not stood up to scrutiny. However, a modi®cation of transketolase is a marker for Alzheimer's disease, and transketolase activity in erythrocytes is a measure of thiamin nutrition. The cornea contains a particularly high transketolase concentration, consistent with the proposal that pentose phosphate pathway activity has a role in the removal of light-generated radicals. #

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Transketolase from Escherichia coli: A practical procedure for using the biocatalyst for asymmetric carbon-carbon bond synthesis

Cited by 80 publications

References 11 publications

Separating Thermodynamics from Kinetics—A New Understanding of the Transketolase Reaction

Separating Thermodynamics from Kinetics—A New Understanding of the Transketolase Reaction

Directed evolution to re-adapt a co-evolved network within an enzyme

Properties and functions of the thiamin diphosphate dependent enzyme transketolase

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