Evidence for <scp>l</scp>-threonine cleavage and allothreonine formation by different enzymes from <i>Clostridium pasteurianum</i>: threonine aldolase and serine hydroxymethyltransferase

Stöcklein, Walter; Schmidt, H.‐L.

doi:10.1042/bj2320621

Cited by 11 publications

(3 citation statements)

References 10 publications

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“…Benzaldehyde (substrate) inhibition of the free enzyme or enzyme trapped at the interfacial area explains this behavior, which is supported by our own experiments with DMSO ( Fig. 8a) and by Stöcklein and Schmidt (1985) who reported that TA binding sites are inhibited by acetaldehyde.…”

Section: Parametrical Studiessupporting

confidence: 83%

Aldolase catalyzed L-phenylserine synthesis in a slug-flow microfluidic system – Performance and diastereoselectivity studies

Čech

Hessel

Přibyl

2017

Chemical Engineering Science

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L-phenylserine was produced by threonine aldolase in slug-flow microfluidic system. Substrate benzaldehyde was continuously supplied from the organic phase. TBME solvent provides mild conditions and high product concentration. MeTHF solvent provides high concentration of L-syn-phenylserine. Toluene provides low value of syn-anti forms ratio in short residence time. a b s t r a c tWe study synthesis of L-phenylserine catalyzed by the enzyme L-threonine aldolase in a slug-flow microfluidic system. Slug-flow arrangement allows for the continuous refilling of sparingly soluble substrate (benzaldehyde) into an aqueous reaction mixture. We identified suitable composition of an organic phase to provide stable slug-flow in a wide range of operational parameters. Solvent screening revealed that tert-butyl methyl ether (TBME) as the organic solvent provides the most friendly environment for L-phenylserine synthesis due to a low degree of enzyme deactivation and high benzaldehyde concentration in the reaction mixture. The effects of substrate concentrations, enzyme concentration, and dimethylsulfoxide (DMSO) concentration on the L-phenylserine concentration in the product stream were examined and proper reaction conditions were identified. Experimental results on the L-phenylserine diastereoselectivity demonstrate that the amount of syn-conformation of L-phenylserine increases with the reaction time. High syn-to anti-concentration ratio is achieved with 2-methyltetrahydrofuran (MeTHF) solvent in a system with long residence time and, finally, low syn-to anticoncentration ratio is provided by toluene environment and short residence time. (J. Čech), v.hessel@tue.nl (V. Hessel), pribylm@vscht.cz (M. Přibyl). Please cite this article as: Čech, J., et al., Aldolase catalyzed L-phenylserine synthesis in a slug-flow microfluidic system -Performance and diastereoselectivity studies. Chem. Eng. Sci. (2016), http://dx.

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Section: Parametrical Studiessupporting

confidence: 83%

Aldolase catalyzed L-phenylserine synthesis in a slug-flow microfluidic system – Performance and diastereoselectivity studies

Čech

Hessel

Přibyl

2017

Chemical Engineering Science

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“…Earlier studies reported occurrence of two distinct enzymes in sheep liver 19 ) that catalyze respectively the cleavage of L-threonine and of L-allothreonine. Stocklein and Schmidt 20 ) also showed that SHMT with L-allothreonine aldolase activity and L-threonine aldolase in Clostridium pasteurianum were readily separated by ion exchange.…”

Section: Discussionmentioning

confidence: 98%

Purification and Characterization of Cytosolic Serine Hydroxymethyltransferase fromEuglena gracilisz

Sakamoto¹,

Masuda²,

Yanagimoto³

et al. 1991

Agricultural and Biological Chemistry

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“…Threonine aldolase (EC 4.1.2.5), catalyzing the reversible aldol cleavage of threonine into glycine and acetaldehyde, is one of the threonine‐degrading enzymes. 1–4 Its enzyme activity has been found in several microorganisms, in such genera as Pseudomonas , 5 Clostridium , 3,6,7 Bacillus , 8 and Candida , 9,10 as well as in mammalian organs. 11,12 Studies on the mechanism underlying its catalytic action revealed that l‐threonine aldolase belongs to a group of enzymes that require pyridoxal 5′‐phosphate (PLP) as a coenzyme.…”

Section: Introductionmentioning

confidence: 99%

Novel Threonine Aldolases and Their Application to Stereospecific Synthesis of β‐Hydroxy‐α‐amino Acids

Kataoka

Wada

Ikemi

et al. 1998

Annals of the New York Academy of Sciences

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Evidence for l-threonine cleavage and allothreonine formation by different enzymes from Clostridium pasteurianum: threonine aldolase and serine hydroxymethyltransferase

Cited by 11 publications

References 10 publications

Aldolase catalyzed L-phenylserine synthesis in a slug-flow microfluidic system – Performance and diastereoselectivity studies

Aldolase catalyzed L-phenylserine synthesis in a slug-flow microfluidic system – Performance and diastereoselectivity studies

Purification and Characterization of Cytosolic Serine Hydroxymethyltransferase fromEuglena gracilisz

Novel Threonine Aldolases and Their Application to Stereospecific Synthesis of β‐Hydroxy‐α‐amino Acids

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