Efficient bioconversion of l-threonine to 2-oxobutyrate using whole cells of Pseudomonas stutzeri SDM

Zhang, Wen; Gao, Chao; Che, Bin; Ma, Cuiqing; Zheng, Zhaojuan; Qin, Tong; Xu, Ping

doi:10.1016/j.biortech.2012.01.123

Cited by 11 publications

(6 citation statements)

References 14 publications

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“…It iswidely used in biology [43], medicine [44], and food additive productions [45,46,47]. Generally, α-ketobutyrate is determined by high-pressure liquid chromatography [45,48,49]. No new optical method for determination of α-ketobutyrate was published until now.…”

Section: Resultsmentioning

confidence: 99%

Development of Ratiometric Fluorescence Sensors Based on CdSe/ZnS Quantum Dots for the Detection of Hydrogen Peroxide

Duong

Rhee

2019

Sensors

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In this study, carboxyl group functionalized-CdSe/ZnS quantum dots (QDs) and aminofluorescein (AF)-encapsulated polymer particles were synthesized and immobilized to a sol–gel mixture of glycidoxypropyl trimethoxysilane (GPTMS) and aminopropyl trimethoxysilane (APTMS) for the fabrication of a hydrogen peroxide-sensing membrane. CdSe/ZnS QDs were used for the redox reaction of hydrogen peroxide (H2O2) via a reductive pathway by transferring electrons to the acceptor that led to fluorescence quenching of QDs, while AF was used as a reference dye. Herein, the ratiometric fluorescence intensity of CdSe/ZnS QDs and AF was proportional to the concentration of hydrogen peroxide. The fluorescence membrane (i.e., QD–AF membrane) could detect hydrogen peroxide in linear detection ranges from 0.1 to 1.0 mM with a detection limit (LOD) of 0.016 mM and from 1.0 to 10 mM with an LOD of 0.058 mM. The sensitivity of the QD–AF membrane was increased by immobilizing horseradish peroxidase (HRP) over the surface of the QD–AF membrane (i.e., HRP–QD–AF membrane). The HRP–QD–AF membrane had an LOD of 0.011 mM for 0.1–1 mM H2O2 and an LOD of 0.068 mM for 1–10 mM H2O2. It showed higher sensitivity than the QD–AF membrane only, although both membranes had good selectivity. The HRP–QD–AF membrane could be applied to determine the concentration of hydrogen peroxide in wastewater, while the QD–AF membrane could be employed for the detection of α-ketobutyrate.

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Section: Resultsmentioning

confidence: 99%

Development of Ratiometric Fluorescence Sensors Based on CdSe/ZnS Quantum Dots for the Detection of Hydrogen Peroxide

Duong

Rhee

2019

Sensors

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“…2-OBA is an important intermediate widely used in biosynthesis of l -isoleucine, d -2-hydroxybutyrate and 1-propanol [ 54 – 56 ]. Furthermore, 2-OBA could be bioconverted into a non-natural amino acid l -homoalanine, which is a key chiral precursor for production of levetiracetam, brivaracetam, and ethambutol [ 57 , 58 ]. Owing to the mild reaction conditions, high substrate conversion efficiency and simple compositions of the reaction mixture which is contributed to the convenience of recovery, whole cell catalysis becomes the preferred method for pyruvate and 2-OBA production [ 47 , 50 ].…”

Section: Resultsmentioning

confidence: 99%

A novel biocatalyst for efficient production of 2-oxo-carboxylates using glycerol as the cost-effective carbon source

Wang

Zhang

Jiang

et al. 2015

Biotechnol Biofuels

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BackgroundThe surplus of glycerol has increased remarkably as a main byproduct during the biofuel’s production. Exploiting an alternative route for glycerol utilization is significantly important for sustainability of biofuels.ResultsA novel biocatalyst that could be prepared from glycerol for producing 2-oxo-carboxylates was developed. First, Pseudomonas putida KT2440 was reconstructed by deleting lldR to develop a mutant expressing the NAD-independent lactate dehydrogenases (iLDHs) constitutively. Then, the Vitreoscilla hemoglobin (VHb) was heterologously expressed to further improve the biotransformation activity. The reconstructed strain, P. putida KT2440 (ΔlldR)/pBSPPcGm-vgb, exhibited high activities of iLDHs when cultured with glycerol as the carbon source. This cost-effective biocatalyst could efficiently produce pyruvate and 2-oxobutyrate from dl-lactate and dl-2-hydroxybutyrate with high molar conversion rates of 91.9 and 99.8 %, respectively.ConclusionsThe process would not only be a promising alternative for the production of 2-oxo-carboxylates, but also be an example for preparation of efficient biocatalysts for the value-added utilization of glycerol.

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“…The results indicate that ProXpx is a robust deacylase against tRNAs mischarged with a-aminobutyrate (2-aminobutyrate, 2-Abu, henceforth "Abu"), a non-proteinogenic amino acid (NPA) similar in size to L-Pro that is an intermediate in the biosynthesis of Ile, Thr, and Asp. [24][25][26][27] Thus, we propose that the substrate specificities of the INS-family of trans-editing factors are not limited to proteinogenic amino acids, but also encompass NPAs.…”

Section: Introductionmentioning

confidence: 99%

Quality control bytrans-editing factor prevents global mistranslation of non-protein amino acid α-aminobutyrate

et al. 2017

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Accuracy in protein biosynthesis is maintained through multiple pathways, with a critical checkpoint occurring at the tRNA aminoacylation step catalyzed by aminoacyl-tRNA synthetases (ARSs). In addition to the editing functions inherent to some synthetases, single-domain trans-editing factors, which are structurally homologous to ARS editing domains, have evolved as alternative mechanisms to correct mistakes in aminoacyl-tRNA synthesis. To date, ARS-like trans-editing domains have been shown to act on specific tRNAs that are mischarged with genetically encoded amino acids. However, structurally related non-protein amino acids are ubiquitous in cells and threaten the proteome. Here, we show that a previously uncharacterized homolog of the bacterial prolyl-tRNA synthetase (ProRS) editing domain edits a known ProRS aminoacylation error, Ala-tRNA, but displays even more robust editing of tRNAs misaminoacylated with the non-protein amino acid α-aminobutyrate (2-aminobutyrate, Abu) in vitro and in vivo. Our results indicate that editing by trans-editing domains such as ProXp-x studied here may offer advantages to cells, especially under environmental conditions where concentrations of non-protein amino acids may challenge the substrate specificity of ARSs.

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Efficient bioconversion of l-threonine to 2-oxobutyrate using whole cells of Pseudomonas stutzeri SDM

Cited by 11 publications

References 14 publications

Development of Ratiometric Fluorescence Sensors Based on CdSe/ZnS Quantum Dots for the Detection of Hydrogen Peroxide

Development of Ratiometric Fluorescence Sensors Based on CdSe/ZnS Quantum Dots for the Detection of Hydrogen Peroxide

A novel biocatalyst for efficient production of 2-oxo-carboxylates using glycerol as the cost-effective carbon source

Quality control bytrans-editing factor prevents global mistranslation of non-protein amino acid α-aminobutyrate

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