Browse
Submit Data
Databases
API
Help

Dataset Information

0 Views

0 Connections

0 Citations

0 Reanalyses

0 Downloads

Omics score: 0

A two-step strategy for the preparation of 6-deoxy-l-sorbose.

ABSTRACT: A two-step enzymatic strategy for the efficient and convenient synthesis of 6-deoxy-l-sorbose was reported herein. In the first reaction step, the isomerization of l-fucose (6-deoxy-l-galactose) to l-fuculose (6-deoxy-l-tagatose) catalyzed by l-fucose isomerase (FucI), and the epimerization of l-fuculose to 6-deoxy-l-sorbose catalyzed by d-tagatose 3-epimerase (DTE) were coupled with the targeted phosphorylation of 6-deoxy-l-sorbose by fructose kinase from human (HK) in a one-pot reaction. The resultant 6-deoxy-l-sorbose 1-phosphate was purified by silver nitrate precipitation method. In the second reaction step, the phosphate group of the 6-deoxy-l-sorbose 1-phosphate was hydrolyzed with acid phosphatase (AphA) to produce 6-deoxy-l-sorbose in 81% yield with regard to l-fucose.

SUBMITTER: Wen L

PROVIDER: S-EPMC5067164 | biostudies-literature | 2016 Sep

REPOSITORIES: biostudies-literature

ACCESS DATA

Json Xml

Publications

A two-step strategy for the preparation of 6-deoxy-l-sorbose.

Wen Liuqing L Huang Kenneth K Zheng Yuan Y Liu Yunpeng Y Zhu He H Wang Peng George PG

Bioorganic & medicinal chemistry letters 20160325 17

A two-step enzymatic strategy for the efficient and convenient synthesis of 6-deoxy-l-sorbose was reported herein. In the first reaction step, the isomerization of l-fucose (6-deoxy-l-galactose) to l-fuculose (6-deoxy-l-tagatose) catalyzed by l-fucose isomerase (FucI), and the epimerization of l-fuculose to 6-deoxy-l-sorbose catalyzed by d-tagatose 3-epimerase (DTE) were coupled with the targeted phosphorylation of 6-deoxy-l-sorbose by fructose kinase from human (HK) in a one-pot reaction. The r ...[more]

PMID: 27485385

Similar Datasets

Two-step enzymatic synthesis of 6-deoxy-L-psicose.

Project description:Rare sugars offer a plethora of applications in the pharmaceutical, medicinal, and industries, as well as in synthetic chemistry. However, studies of rare sugars have been hampered by their relative scarcity. In this work, we describe a two-step strategy to efficiently and conveniently prepare 6-deoxy-L-psicose from L-rhamnose. In the first reaction step, the isomerization of L-rhamnose (6-deoxy-L-mannose) to L-rhamnulose (6-deoxy-L-fructose) catalyzed by L-rhamnose isomerase (RhaI), and the epimerization of L-rhamnulose to 6-deoxy-L-psicose catalyzed by D-tagatose 3-epimerase (DTE) were coupled with selective phosphorylation reaction by fructose kinase from human (HK), which selectively phosphorylate 6-deoxy-L-psicose at C-1 position. 6-deoxy-L-psicose 1-phosphate was purified by a silver nitrate precipitation method. In the second step, the phosphate group of the 6-deoxy-L-sorbose 1-phosphate was hydrolyzed with acid phosphatase (AphA) to produce 6-deoxy-L-psicose in 81% yield with respect to L-rhamnose. This method allows that the 6-deoxy-L-psicose to be obtained from readily available starting materials with high purity and without having to undergo isomer separation.

| S-EPMC4990140 | biostudies-literature

A two-step strategy for constructing specifically self-subtracted cDNA libraries.

Project description:We have developed a new strategy for producing subtracted cDNA libraries that is optimized for connective and epithelial tissues, where a few exceptionally abundant (super-prevalent) RNA species account for a large fraction of the total mRNA mass. Our method consists of a two-step subtraction of the most abundant mRNAs: the first step involves a novel use of oligo-directed RNase H digestion to lower the concentration of tissue-specific, super-prevalent RNAs. In the second step, a highly specific subtraction is achieved through hybridization with probes from a 3'-end ESTs collection. By applying this technique in skeletal muscle, we have constructed subtracted cDNA libraries that are effectively enriched for genes expressed at low levels. We further report on frequent premature termination of transcription in human muscle mitochondria and discuss the importance of this phenomenon in designing subtractive approaches. The tissue-specific collections of cDNA clones generated by our method are particularly well suited for expression profiling.

| S-EPMC113861 | biostudies-literature

A two-step strategy to enhance activity of low potency peptides.

Project description:Novel strategies are needed to expedite the generation and optimization of peptide probes targeting G protein-coupled receptors (GPCRs). We have previously shown that membrane tethered ligands (MTLs), recombinant proteins comprised of a membrane anchor, an extracellular linker, and a peptide ligand can be used to identify targeted receptor modulators. Although MTLs provide a useful tool to identify and/or modify functionally active peptides, a major limitation of this strategy is the reliance on recombinant protein expression. We now report the generation and pharmacological characterization of prototype peptide-linker-lipid conjugates, synthetic membrane anchored ligands (SMALs), which are designed as mimics of corresponding MTLs. In this study, we systematically compare the activity of selected peptides as MTLs versus SMALs. As prototypes, we focused on the precursor proteins of mature Substance P (SubP) and Cholecystokinin 4 (CCK4), specifically non-amidated SubP (SubP-COOH) and glycine extended CCK4 (CCK4-Gly-COOH). As low affinity soluble peptides these ligands each presented a challenging test case for assessment of MTL/SMAL technology. For each ligand, MTLs and corresponding SMALs showed agonist activity and comparable subtype selectivity. In addition, our results illustrate that membrane anchoring increases ligand potency. Furthermore, both MTL and SMAL induced signaling can be blocked by specific non-peptide antagonists suggesting that the anchored constructs may be orthosteric agonists. In conclusion, MTLs offer a streamlined approach for identifying low activity peptides which can be readily converted to higher potency SMALs. The ability to recapitulate MTL activity with SMALs extends the utility of anchored peptides as probes of GPCR function.

| S-EPMC4229100 | biostudies-literature

A Two-Step Strategy for Fabrication of Biocompatible 3D Magnetically Responsive Photonic Crystals.

Project description:Extremely stable and biocompatible 3D magnetically responsive photonic crystals (MRPCs) are successfully prepared in aqueous solution. Classic hydrothermal synthesis was applied for preparation of the Fe3O4@C core. Modified Stöber method was then employed for synthesis of the different size of Fe3O4@C@SiO2. Unlike the traditional magnetic nanoparticles, the highly negative charged superparamagnetic nanospheres (SMNs), i.e., the double-shell structure Fe3O4@C@SiO2 are capable of rapidly self-assembling into 3D MRPCs with full visible and various colors that can be periodically and reversibly tuned under different kinds of external magnetic fields (EMFs) within 1 s. The assembling behavior and mechanism of the 3D MRPCs under EMF were monitored and analyzed. The preparation is simple and the size of the SMN is easily controllable by adjusting the amount of catalyst. Compared with the previous works, the synthesized 3D MRPCs are hydrophilic, and exhibit extremely high stability after 6-month storage. To conclude, our study provides an effective two-step strategy for fabrication of biocompatible 3D MRPCs and it reveals great potentials in biological fields.

| S-EPMC6367226 | biostudies-literature

Membrane-bound pyrroloquinoline quinone-dependent dehydrogenase in Gluconobacter oxydans M5, responsible for production of 6-(2-hydroxyethyl) amino-6-deoxy-L-sorbose.

Project description:A membrane-bound protein purified from Gluconobacter oxydans M5 was confirmed to be a pyrroloquinoline quinone-dependent D-sorbitol dehydrogenase. Gene disruption and complementation experiments demonstrated that this enzyme is responsible for the oxidation of 1-(2-hydroxyethyl) amino-1-deoxy-D-sorbitol (1NSL) to 6-(2-hydroxyethyl) amino-6-deoxy-L-sorbose (6NSE), which is the precursor of an antidiabetic drug, miglitol.

| S-EPMC2519276 | biostudies-literature

Minicircles for a two-step blood biomarker and PET imaging early cancer detection strategy.

Project description:Early cancer detection can dramatically increase treatment options and survival rates for patients, yet detection of early-stage tumors remains difficult. Here, we demonstrate a two-step strategy to detect and locate cancerous lesions by delivering tumor-activatable minicircle (MC) plasmids encoding a combination of blood-based and imaging reporter genes to tumor cells. We genetically engineered the MCs, under the control of the pan-tumor-specific Survivin promoter, to encode: 1) Gaussia Luciferase (GLuc), a secreted biomarker that can be easily assayed in blood samples; and 2) Herpes Simplex Virus Type 1 Thymidine Kinase mutant (HSV-1 sr39TK), a PET reporter gene that can be used for highly sensitive and quantitative imaging of the tumor location. We evaluated two methods of MC delivery, complexing the MCs with the chemical transfection reagent jetPEI or encapsulating the MCs in extracellular vesicles (EVs) derived from a human cervical cancer HeLa cell line. MCs delivered by EVs or jetPEI yielded significant expression of the reporter genes in cell culture versus MCs delivered without a transfection reagent. Secreted GLuc correlated with HSV-1 sr39TK expression with R2 = 0.9676. MC complexation with jetPEI delivered a larger mass of MC for enhanced transfection, which was crucial for in vivo animal studies, where delivery of MCs via jetPEI resulted in GLuc and HSV-1 sr39TK expression at significantly higher levels than controls. To the best of our knowledge, this is the first report of the PET reporter gene HSV-1 sr39TK delivered via a tumor-activatable MC to tumor cells for an early cancer detection strategy. This work explores solutions to endogenous blood-based biomarker and molecular imaging limitations of early cancer detection strategies and elucidates the delivery capabilities and limitations of EVs.

| S-EPMC8262353 | biostudies-literature

A two-step lineage reprogramming strategy to generate functionally competent human hepatocytes from fibroblasts.

Project description:Terminally differentiated cells can be generated by lineage reprogramming, which is, however, hindered by incomplete conversion with residual initial cell identity and partial functionality. Here, we demonstrate a new reprogramming strategy by mimicking the natural regeneration route, which permits generating expandable hepatic progenitor cells and functionally competent human hepatocytes. Fibroblasts were first induced into human hepatic progenitor-like cells (hHPLCs), which could robustly expand in vitro and efficiently engraft in vivo. Moreover, hHPLCs could be efficiently induced into mature human hepatocytes (hiHeps) in vitro, whose molecular identity highly resembles primary human hepatocytes (PHHs). Most importantly, hiHeps could be generated in large quantity and were functionally competent to replace PHHs for drug-metabolism estimation, toxicity prediction and hepatitis B virus infection modeling. Our results highlight the advantages of the progenitor stage for successful lineage reprogramming. This strategy is promising for generating other mature human cell types by lineage reprogramming.

| S-EPMC6796870 | biostudies-literature

Subjective Opinions of Patients About Step-by-Step Cataract Surgery Preparation.

Project description:PurposeWe analyzed the subjective feelings and opinions of patients regarding modified cataract phacoemulsification procedures.Patients and methodsA consecutive case series of patients undergoing phacoemulsification of cataracts, who completed questionnaires designed by the authors to evaluate their subjective opinions about hospital admission, medical examination, and intraoperative procedures carried out at the operating theater.ResultsTwo hundred patients (82 men and 118 women) were included in the study. Subjects aged ≥65 years more often than younger respondents presented negative opinions about hospital admission procedures (15% vs. 2.5%, p=0.032) and were less satisfied with physicians' explanations about the matter of phacoemulsification (71.3% vs. 92.5%, p=0.004), type of artificial lens to be implanted (43.8% vs. 85%, p<0.001), and potential complications (69.4% vs. 95%, p<0.001). The most unpleasant intraoperative experiences included venipuncture (35.5%), artificial lens implantation (30.5%), and peeling off of a sterile surgical drape (24%).ConclusionPersons aged ≥65 years presented with negative opinions about routine procedures related to phacoemulsification. Older age seems to be associated with less tolerance to time-consuming bureaucratic procedures and a lesser understanding of the specific stages of the surgery. Older patients should be notified in advance about all routine procedures to be carried out and provided with a rationale for these activities.Trial registrationThe study was registered on clinicaltrials. gov (NCT04327856).

| S-EPMC7917310 | biostudies-literature

Two-Step Preparation of CCF/PEEK Wrapped Yarn for 3D Printing Composites with Enhanced Mechanical Properties.

Project description:Continuous fiber reinforced thermoplastic composites (CFTPCs) have shown advantages such as high strength, long life, corrosion resistance, and green recyclability. Three-dimensional printing of CFTPCs opened up a new strategy for the fabrication of composites with complicated structures, low cost, and short production cycles. However, a traditional 3D printing process usually causes poor impregnation of the fiber or surface damage of the fiber due to the short impregnation time or high viscosity of the thermoplastic resin. Here, continuous carbon fiber/poly(ether-ether-ketones) (CCF/PEEK) wrapped yarn was fabricated via powder impregnation and using double spinning technology for the 3D printing. The concentration of PEEK powder suspension and wire speed were optimized as 15% and 2.0 m/min. The twist of wrapped yarn was optimized as 1037 T/m. Mechanical testing showed that the 3D-printed composite wire had excellent tensile and bending strength, which was about 1.6~4.2 times larger than those without the powder pre-impregnation process. It is mainly attributed to the improved impregnation of the CF which took place during the powder pre-impregnation process. We believe that our research on wrapped yarn for 3D-printed composites provides an effective strategy for the 3D printing of composites with enhanced mechanical properties.

| S-EPMC9921352 | biostudies-literature

L-sorbose reductase and its transcriptional regulator involved in L-sorbose utilization of Gluconobacter frateurii.

Project description:Upstream of the gene for flavin adenine dinucleotide (FAD)-dependent D-sorbitol dehydrogenase (SLDH), sldSLC, a putative transcriptional regulator was found in Gluconobacter frateurii THD32 (NBRC 101656). In this study, the whole sboR gene and the adjacent gene, sboA, were cloned and analyzed. sboR mutation did not affect FAD-SLDH activity in the membrane fractions. The SboA enzyme expressed and purified from an Escherichia coli transformant showed NADPH-dependent L-sorbose reductase (NADPH-SR) activity, and the enzyme was different from the NADPH-SR previously reported for Gluconobacter suboxydans IFO 3291 in molecular size and amino acid sequence. A mutant defective in sboA showed significantly reduced growth on L-sorbose, indicating that the SboA enzyme is required for efficient growth on L-sorbose. The sboR mutant grew on L-sorbose even better than the wild-type strain did, and higher NADPH-SR activity was detected in cytoplasm fractions. Reverse transcription-PCR experiments indicated that sboRA comprises an operon. These data suggest that sboR is involved in the repression of sboA, but not in the induction of sldSLC, on D-sorbitol and that another activator is required for the induction of these genes by D-sorbitol or L-sorbose.

| S-EPMC1913458 | biostudies-literature

OmicsDI is part of the ELIXIR infrastructure

OmicsDI is an Elixir interoperability service. Learn more ›

Tweets

OmicsDI Databases

PRIDE
PeptideAtlas
MassIVE
JPOST Repository
Physiome Model Repository

EGA
EVA
ENA
LINCS
PAXDB
Cell Collective

MetaboLights
Metabolomics Workbench
MetabolomeExpress
GNPS
BioModels
FAIRDOMHub

ArrayExpress
dbGaP
ExpressionAtlas
GEO
NODE

Information

Databases
Help
API
Contact us
Code on GitHub
Terms of use
Submit Data