glycerol 3 phosphate  (Millipore)

 
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    Name:
    Glycerol 3 Phosphate Dehydrogenase
    Description:
    Glycerol 3 phosphate dehydrogenase is a NADH dependent cytosolic enzyme It can be used as a catalytic enzyme Its activity is higher under osmotic stress
    Catalog Number:
    GDH-RO
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    Structured Review

    Millipore glycerol 3 phosphate
    C. elegans GPATs, acl-4, acl-5, and acl-6, contribute to triacylglycerol synthesis. ( A ) In mammals and C. elegans , <t>glycerol-3-phosphate</t> acyltransferases (GPATs) are located on both the outer mitochondrial membrane (mitochondrial GPAT) and endoplasmic
    Glycerol 3 phosphate dehydrogenase is a NADH dependent cytosolic enzyme It can be used as a catalytic enzyme Its activity is higher under osmotic stress
    https://www.bioz.com/result/glycerol 3 phosphate/product/Millipore
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    1) Product Images from "Mitochondria-type GPAT is required for mitochondrial fusion"

    Article Title: Mitochondria-type GPAT is required for mitochondrial fusion

    Journal: The EMBO Journal

    doi: 10.1038/emboj.2013.77

    C. elegans GPATs, acl-4, acl-5, and acl-6, contribute to triacylglycerol synthesis. ( A ) In mammals and C. elegans , glycerol-3-phosphate acyltransferases (GPATs) are located on both the outer mitochondrial membrane (mitochondrial GPAT) and endoplasmic
    Figure Legend Snippet: C. elegans GPATs, acl-4, acl-5, and acl-6, contribute to triacylglycerol synthesis. ( A ) In mammals and C. elegans , glycerol-3-phosphate acyltransferases (GPATs) are located on both the outer mitochondrial membrane (mitochondrial GPAT) and endoplasmic

    Techniques Used:

    2) Product Images from "Sugar analog synthesis by in vitro biocatalytic cascade: A comparison of alternative enzyme complements for dihydroxyacetone phosphate production as a precursor to rare chiral sugar synthesis"

    Article Title: Sugar analog synthesis by in vitro biocatalytic cascade: A comparison of alternative enzyme complements for dihydroxyacetone phosphate production as a precursor to rare chiral sugar synthesis

    Journal: PLoS ONE

    doi: 10.1371/journal.pone.0184183

    Enzymatic cascades for the conversion of glycerol to DHAP via glycerol-3-phosphate. Glycerol is converted to glycerol-3-phosphate by a glycerol kinase enzyme with concomitant regeneration of ATP by an acetate or pyruvate kinase enzyme. The glycerol-3-phopshate is then oxidized to DHAP by either an L - glycerol-3-phosphate oxidase enzyme (A) or a glycerol-3-phosphate dehydrogenase enzyme (B).
    Figure Legend Snippet: Enzymatic cascades for the conversion of glycerol to DHAP via glycerol-3-phosphate. Glycerol is converted to glycerol-3-phosphate by a glycerol kinase enzyme with concomitant regeneration of ATP by an acetate or pyruvate kinase enzyme. The glycerol-3-phopshate is then oxidized to DHAP by either an L - glycerol-3-phosphate oxidase enzyme (A) or a glycerol-3-phosphate dehydrogenase enzyme (B).

    Techniques Used:

    Details of the optimized cascade for the production of DHAP from glycerol. Phosphorylation of glycerol by ATP mediated by GlpK Tk (EC 2.7.1.30) and Mg 2+ via a phosphotransfer mechanism [ 33 ] was accompanied by regeneration of ATP from ADP by AceK Ms (EC 2.7.2.1), which catalyzes reversibly the phosphorylation of acetate in the presence of a divalent cation and ATP with the formation of acetylphosphate and ADP[ 34 ]. Cytosolic glycerophosphate oxidase GlpO Mg (EC 1.1.3.21) likely converts glycerol-3-phosphate to DHAP by a similar mechanism to the related GlpO from Mycoplasma pneumoniae (4X9M) [ 35 ]), Similarly to other flavoprotein oxidases, glycerophosphate oxidase GlpO enzymes follow a hydride transfer mechanism to stabilize a positive charge on the flavin N(5)-sulfite adduct (C). The hydrogen peroxide generated from the oxidation of enzymatic FADH 2 was converted to water by the addition of catalase from Micrococcus lysodeikticus .
    Figure Legend Snippet: Details of the optimized cascade for the production of DHAP from glycerol. Phosphorylation of glycerol by ATP mediated by GlpK Tk (EC 2.7.1.30) and Mg 2+ via a phosphotransfer mechanism [ 33 ] was accompanied by regeneration of ATP from ADP by AceK Ms (EC 2.7.2.1), which catalyzes reversibly the phosphorylation of acetate in the presence of a divalent cation and ATP with the formation of acetylphosphate and ADP[ 34 ]. Cytosolic glycerophosphate oxidase GlpO Mg (EC 1.1.3.21) likely converts glycerol-3-phosphate to DHAP by a similar mechanism to the related GlpO from Mycoplasma pneumoniae (4X9M) [ 35 ]), Similarly to other flavoprotein oxidases, glycerophosphate oxidase GlpO enzymes follow a hydride transfer mechanism to stabilize a positive charge on the flavin N(5)-sulfite adduct (C). The hydrogen peroxide generated from the oxidation of enzymatic FADH 2 was converted to water by the addition of catalase from Micrococcus lysodeikticus .

    Techniques Used: Mass Spectrometry, Generated

    Production of rare chiral sugars by combining optimized multi-enzyme cascades for DHAP production with a DHAP-dependant fructose-1,6-biphosphate aldolase. Glycerol (10mM substrate) was converted to glycerol-3-phosphate by a glycerol kinase enzyme GlpK Tk (28.6 pmoles) with concomitant regeneration of ATP by an acetate kinase enzyme AceK Ms (40.2 pmoles). The glycerol-3-phopshate was then oxidized to DHAP by a novel L -glycerol-3-phosphate oxidase enzyme GlpO Mg (154.2 pmoles), with mitigation of excess hydrogen peroxide by catalase (3U/mL) and an aldolase enzyme FruA Sc (3.1 nmoles) converted this and acceptor aldehydes (provided at 10mM) into chiral sugars D -fructose-1,6-biphosphate (3 S , 4 R ) and 3,4-dihydroxyhexulose phosphate (3 S , 4 R ) as depicted.
    Figure Legend Snippet: Production of rare chiral sugars by combining optimized multi-enzyme cascades for DHAP production with a DHAP-dependant fructose-1,6-biphosphate aldolase. Glycerol (10mM substrate) was converted to glycerol-3-phosphate by a glycerol kinase enzyme GlpK Tk (28.6 pmoles) with concomitant regeneration of ATP by an acetate kinase enzyme AceK Ms (40.2 pmoles). The glycerol-3-phopshate was then oxidized to DHAP by a novel L -glycerol-3-phosphate oxidase enzyme GlpO Mg (154.2 pmoles), with mitigation of excess hydrogen peroxide by catalase (3U/mL) and an aldolase enzyme FruA Sc (3.1 nmoles) converted this and acceptor aldehydes (provided at 10mM) into chiral sugars D -fructose-1,6-biphosphate (3 S , 4 R ) and 3,4-dihydroxyhexulose phosphate (3 S , 4 R ) as depicted.

    Techniques Used: Mass Spectrometry

    3) Product Images from "Insights into the molecular basis of long-term storage and survival of sperm in the honeybee (Apis mellifera)"

    Article Title: Insights into the molecular basis of long-term storage and survival of sperm in the honeybee (Apis mellifera)

    Journal: Scientific Reports

    doi: 10.1038/srep40236

    ATP produced from substrate metabolism in ejaculated sperm. ATP produced by ( A ) aerobic metabolism and ( B ) acidifying glycolytic metabolism of substrates. Error bars denote 1SE. n/s: p ≥ 0.05, ** p ≤ 0.01. GA3P, glyceraldehyde-3-phosphate; G3P, glycerol-3-phosphate; 3PG, 3-phosphoglycerate; GABA, gamma-aminobutyric acid.
    Figure Legend Snippet: ATP produced from substrate metabolism in ejaculated sperm. ATP produced by ( A ) aerobic metabolism and ( B ) acidifying glycolytic metabolism of substrates. Error bars denote 1SE. n/s: p ≥ 0.05, ** p ≤ 0.01. GA3P, glyceraldehyde-3-phosphate; G3P, glycerol-3-phosphate; 3PG, 3-phosphoglycerate; GABA, gamma-aminobutyric acid.

    Techniques Used: Produced

    4) Product Images from "Cell-Free Phospholipid Biosynthesis by Gene-Encoded Enzymes Reconstituted in Liposomes"

    Article Title: Cell-Free Phospholipid Biosynthesis by Gene-Encoded Enzymes Reconstituted in Liposomes

    Journal: PLoS ONE

    doi: 10.1371/journal.pone.0163058

    Functional reconstitution of complete biosynthesis pathways for PE and PG lipids. ( a ) Metabolic pathways that lead to the production of DPPG and DPPE starting from palmitoyl-CoA, glycerol-3-phosphate (G3P), cytidine triphosphate (CTP) and L-serine as main substrates. The two-step acyl transfer reaction and the first headgroup conversion step are common to the PE and PG pathways that then branch out into different headgroup modification reactions (see Supplementary text in S1 File for a description of the individual enzymatic steps). For the final step of PG synthesis there exist three alternative enzymes: PgpA, PgpB and PgpC, of which two (A/C) were used in this study. ( b ) Fluorescence scans of SDS-PAGE gels for the headgroup modifying enzymes produced in the PURE system. Fluorescently labeled lysine residues were incorporated during translation. The left gel is 15% polyacrylamide. In addition to the pssA gene product that was used as a control, the gene products of pgpA , pgpC and pgsA were synthesized. The right gel is 12% polyacrylamide and, besides the plsB gene product used as a control, the genes cdsA , pssA and psd were expressed. Size markers are in kDa. The arrowheads point to the observed protein molecular mass. The symbol “*” indicates the position of the band as expected from the nucleotide sequence of the genes (Supplementary text in S1 File ). ( c ) Schematic of the inside-out proteoliposome reconstitution experiments and enzymatic cascade reactions, where all genes of a given pathway were expressed in PURE frex and all specific substrates were supplied. ( d ) LC-MS data reporting lipid production in the PE and PG pathways under various experimental conditions. Combined gene expression and lipid biogenesis was carried out as illustrated in (c) using 25 ng of each linear DNA templates, 500 μM G3P, 100 μM palmitoyl-CoA, 1 mM CTP and 500 μM L-serine. Details of MS signatures for the different lipids are reported in Table A in S1 File . Lipids DPPE and DPPG were unambiguously detected in a pathway-specific manner. No PG is produced in the reconstituted PE pathway. Likewise, no PE was detected in the PG pathway. When the plsB gene is omitted the complete pathways are shut down. In the absence of the Psd enzyme, PE was not detected and its substrate lipid DPPS accumulated. Note that the MRM data for PS come from the MS optimizer results, not from separate experiments as used for the other compounds. Data are mean and s.e.m. of three independent experiments, except for the negative controls without plsB gene where two independent experiments were conducted. For each replicate the same sample was injected between one and four times in the MS, their averaged value was calculated and data are reported as the mean and standard error across the different trials.
    Figure Legend Snippet: Functional reconstitution of complete biosynthesis pathways for PE and PG lipids. ( a ) Metabolic pathways that lead to the production of DPPG and DPPE starting from palmitoyl-CoA, glycerol-3-phosphate (G3P), cytidine triphosphate (CTP) and L-serine as main substrates. The two-step acyl transfer reaction and the first headgroup conversion step are common to the PE and PG pathways that then branch out into different headgroup modification reactions (see Supplementary text in S1 File for a description of the individual enzymatic steps). For the final step of PG synthesis there exist three alternative enzymes: PgpA, PgpB and PgpC, of which two (A/C) were used in this study. ( b ) Fluorescence scans of SDS-PAGE gels for the headgroup modifying enzymes produced in the PURE system. Fluorescently labeled lysine residues were incorporated during translation. The left gel is 15% polyacrylamide. In addition to the pssA gene product that was used as a control, the gene products of pgpA , pgpC and pgsA were synthesized. The right gel is 12% polyacrylamide and, besides the plsB gene product used as a control, the genes cdsA , pssA and psd were expressed. Size markers are in kDa. The arrowheads point to the observed protein molecular mass. The symbol “*” indicates the position of the band as expected from the nucleotide sequence of the genes (Supplementary text in S1 File ). ( c ) Schematic of the inside-out proteoliposome reconstitution experiments and enzymatic cascade reactions, where all genes of a given pathway were expressed in PURE frex and all specific substrates were supplied. ( d ) LC-MS data reporting lipid production in the PE and PG pathways under various experimental conditions. Combined gene expression and lipid biogenesis was carried out as illustrated in (c) using 25 ng of each linear DNA templates, 500 μM G3P, 100 μM palmitoyl-CoA, 1 mM CTP and 500 μM L-serine. Details of MS signatures for the different lipids are reported in Table A in S1 File . Lipids DPPE and DPPG were unambiguously detected in a pathway-specific manner. No PG is produced in the reconstituted PE pathway. Likewise, no PE was detected in the PG pathway. When the plsB gene is omitted the complete pathways are shut down. In the absence of the Psd enzyme, PE was not detected and its substrate lipid DPPS accumulated. Note that the MRM data for PS come from the MS optimizer results, not from separate experiments as used for the other compounds. Data are mean and s.e.m. of three independent experiments, except for the negative controls without plsB gene where two independent experiments were conducted. For each replicate the same sample was injected between one and four times in the MS, their averaged value was calculated and data are reported as the mean and standard error across the different trials.

    Techniques Used: Functional Assay, Modification, Fluorescence, SDS Page, Produced, Labeling, Synthesized, Sequencing, Liquid Chromatography with Mass Spectroscopy, Expressing, Mass Spectrometry, Injection

    5) Product Images from "Apoptosis-related mitochondrial dysfunction defines human monocyte-derived dendritic cells with impaired immuno-stimulatory capacities"

    Article Title: Apoptosis-related mitochondrial dysfunction defines human monocyte-derived dendritic cells with impaired immuno-stimulatory capacities

    Journal: Journal of Cellular and Molecular Medicine

    doi: 10.1111/j.1582-4934.2008.00358.x

    Spontaneous DC death involves caspase activation and mitochondrial dysfunction. Immediately after maturation, human monocyte-derived DCs were cultured under standard conditions for 4 days and an aliquot of cells was collected every day (0, 1, 2, 3 or 4 days of culture) for determination of caspase activation (A) and mitochondrial dysfunction (B, C, D). (A) Caspases 3/7 activity was measured (left part) as described in Materials and Methods. When indicated, DCs were exposed for 1 hr to z-VAD-fmk (100 μM) as a positive control for caspase inhibition. Mean ± S.D. from three independent experiments are shown. Active caspase 3 was identified by Western blotting (right part). Three independent experiments gave similar results. (B) Cytosolic protein fractions were obtained and cytochrome C, AIF and Smac Diablo mitochondrial release in DCs was evaluated by Western blotting. (left part). When indicated, DCs were treated for 24 hrs with z-VAD-fmk (100 μM). Equal loading was checked by probing with anti-G3PDH antibody. Blots were also probed for cyt c oxidase to exlude mitochondria contamination in the cytosol. As a control for detection of cyt c oxidase, a total lysate was loaded. Fluorescence images (right part) of immunostaining with cytochrome c (green) or AIF (green) and nuclear Hoechst 33342 staining (blue) of DCs at day 0 (D0) or day 1 (D1) of culture. Original magnification ×630. (C) Simultaneous assessment of Δψm and ROS production performed with DiOC6(3) and HE. As a control, DCs were incubated with the protonophore mClCCP (100 μM, 15 min., 37°C) as a negative control for DiOC6(3) staining. One representative experiment of four is shown. (D and E). Mature DCs were cultured for 36 hrs under standard conditions, and cells then stained with DiOC6(3) and PI before flow cytometric analysis. Same results were obtained with CMX-ROS and YOPRO-1 staining.These flow cytometric parameters were used for sorting (D). The left square depicts the viable sorted Δψm low subpopulation and the right square represents the ΔΨm high counterparts. (E) Determination of caspase activity in Δψm-sorted populations as shown in D. Caspases -3/7, -8, and -9 activity was estimated after short-term culture of sorted viable Δψm high and low DC subpopulations (E). Mean ± S.D. from three independent experiments are shown. *Statistically significant between purified Δψm low and Δψm high subpopulations. (F) Mitochondrial calcium retention capacity. At day 0 (D0, left panel) or day 2 (D2, right panel) of culture, DCs were permeabilized with digitonin and calcium uptake measured with a calcium-sensitive electrode after the addition of calcium (each 10 μM CaCl 2 pulse [arrows] was detected as a peak in calcium concentration). Three independent experiments gave similar results.
    Figure Legend Snippet: Spontaneous DC death involves caspase activation and mitochondrial dysfunction. Immediately after maturation, human monocyte-derived DCs were cultured under standard conditions for 4 days and an aliquot of cells was collected every day (0, 1, 2, 3 or 4 days of culture) for determination of caspase activation (A) and mitochondrial dysfunction (B, C, D). (A) Caspases 3/7 activity was measured (left part) as described in Materials and Methods. When indicated, DCs were exposed for 1 hr to z-VAD-fmk (100 μM) as a positive control for caspase inhibition. Mean ± S.D. from three independent experiments are shown. Active caspase 3 was identified by Western blotting (right part). Three independent experiments gave similar results. (B) Cytosolic protein fractions were obtained and cytochrome C, AIF and Smac Diablo mitochondrial release in DCs was evaluated by Western blotting. (left part). When indicated, DCs were treated for 24 hrs with z-VAD-fmk (100 μM). Equal loading was checked by probing with anti-G3PDH antibody. Blots were also probed for cyt c oxidase to exlude mitochondria contamination in the cytosol. As a control for detection of cyt c oxidase, a total lysate was loaded. Fluorescence images (right part) of immunostaining with cytochrome c (green) or AIF (green) and nuclear Hoechst 33342 staining (blue) of DCs at day 0 (D0) or day 1 (D1) of culture. Original magnification ×630. (C) Simultaneous assessment of Δψm and ROS production performed with DiOC6(3) and HE. As a control, DCs were incubated with the protonophore mClCCP (100 μM, 15 min., 37°C) as a negative control for DiOC6(3) staining. One representative experiment of four is shown. (D and E). Mature DCs were cultured for 36 hrs under standard conditions, and cells then stained with DiOC6(3) and PI before flow cytometric analysis. Same results were obtained with CMX-ROS and YOPRO-1 staining.These flow cytometric parameters were used for sorting (D). The left square depicts the viable sorted Δψm low subpopulation and the right square represents the ΔΨm high counterparts. (E) Determination of caspase activity in Δψm-sorted populations as shown in D. Caspases -3/7, -8, and -9 activity was estimated after short-term culture of sorted viable Δψm high and low DC subpopulations (E). Mean ± S.D. from three independent experiments are shown. *Statistically significant between purified Δψm low and Δψm high subpopulations. (F) Mitochondrial calcium retention capacity. At day 0 (D0, left panel) or day 2 (D2, right panel) of culture, DCs were permeabilized with digitonin and calcium uptake measured with a calcium-sensitive electrode after the addition of calcium (each 10 μM CaCl 2 pulse [arrows] was detected as a peak in calcium concentration). Three independent experiments gave similar results.

    Techniques Used: Activation Assay, Derivative Assay, Cell Culture, Activity Assay, Positive Control, Inhibition, Western Blot, Fluorescence, Immunostaining, Staining, Incubation, Negative Control, Flow Cytometry, Purification, Concentration Assay

    6) Product Images from "Identification of a Mammalian-type Phosphatidylglycerophosphate Phosphatase in the Eubacterium Rhodopirellula baltica *"

    Article Title: Identification of a Mammalian-type Phosphatidylglycerophosphate Phosphatase in the Eubacterium Rhodopirellula baltica *

    Journal: The Journal of Biological Chemistry

    doi: 10.1074/jbc.M112.413617

    Identification of a putative PTPMT1 ortholog in R. baltica . A , schematic diagram of the CL biosynthesis pathway. Enzymes are highlighted in blue . CDP-DAG, cytidine diphosphate diacylglycerol; G3P, glycerol-3-phosphate. B , active site primary sequence alignment of PTPMT1 orthologs using PROMALS3D and illustrated by ESPript ( 49 , 50 ). H. sap ( H. sapiens ), NP_783859; D. mel ( D. melanogaster ), NP_732901 ; and R. balt ( R. baltica ), NP_865112. C , a phylogenetic tree of human and bacterial DSPs constructed using maximum likelihood (ML) method in PHYML. Each branch was tested by 100 bootstrap replicates, and only branches with bootstrap values above 50% were shown. Human PTPMT1 is bolded and bacterial PTPMT1 orthologs are highlighted in red. D , domain architecture of PGP phosphatases. All domains are presented based on analyses using PFAM, CDD, and PROSITE. Catalytic active site sequences are indicated above. MTS , mitochondrial targeting sequence; DSP , dual specificity phosphatase; HAD , haloacid dehalogenase; PAP2 , phosphatidic acid phosphatase 2. E , presence and absence matrix for CL de novo synthesis enzymes in Rhodeopirellula. Dark gray squares indicate presence of CL enzyme (column) in target species (row). Peach squares mean no ortholog has been identified, i.e. blast search failed to identify sequences that meet the bidirectional-best-hit criterion (cut-off E-values of 10 −10 or less). Sequences of E. coli pgsA, S. cerevisiae GEP4, H. sapiens PTPMT1, E. coli pgpA, pgpB, pgpC, and E. coli cls1 were used as queries for the blast searches.
    Figure Legend Snippet: Identification of a putative PTPMT1 ortholog in R. baltica . A , schematic diagram of the CL biosynthesis pathway. Enzymes are highlighted in blue . CDP-DAG, cytidine diphosphate diacylglycerol; G3P, glycerol-3-phosphate. B , active site primary sequence alignment of PTPMT1 orthologs using PROMALS3D and illustrated by ESPript ( 49 , 50 ). H. sap ( H. sapiens ), NP_783859; D. mel ( D. melanogaster ), NP_732901 ; and R. balt ( R. baltica ), NP_865112. C , a phylogenetic tree of human and bacterial DSPs constructed using maximum likelihood (ML) method in PHYML. Each branch was tested by 100 bootstrap replicates, and only branches with bootstrap values above 50% were shown. Human PTPMT1 is bolded and bacterial PTPMT1 orthologs are highlighted in red. D , domain architecture of PGP phosphatases. All domains are presented based on analyses using PFAM, CDD, and PROSITE. Catalytic active site sequences are indicated above. MTS , mitochondrial targeting sequence; DSP , dual specificity phosphatase; HAD , haloacid dehalogenase; PAP2 , phosphatidic acid phosphatase 2. E , presence and absence matrix for CL de novo synthesis enzymes in Rhodeopirellula. Dark gray squares indicate presence of CL enzyme (column) in target species (row). Peach squares mean no ortholog has been identified, i.e. blast search failed to identify sequences that meet the bidirectional-best-hit criterion (cut-off E-values of 10 −10 or less). Sequences of E. coli pgsA, S. cerevisiae GEP4, H. sapiens PTPMT1, E. coli pgpA, pgpB, pgpC, and E. coli cls1 were used as queries for the blast searches.

    Techniques Used: Sequencing, Construct

    7) Product Images from "Sugar analog synthesis by in vitro biocatalytic cascade: A comparison of alternative enzyme complements for dihydroxyacetone phosphate production as a precursor to rare chiral sugar synthesis"

    Article Title: Sugar analog synthesis by in vitro biocatalytic cascade: A comparison of alternative enzyme complements for dihydroxyacetone phosphate production as a precursor to rare chiral sugar synthesis

    Journal: PLoS ONE

    doi: 10.1371/journal.pone.0184183

    Enzymatic cascades for the conversion of glycerol to DHAP via glycerol-3-phosphate. Glycerol is converted to glycerol-3-phosphate by a glycerol kinase enzyme with concomitant regeneration of ATP by an acetate or pyruvate kinase enzyme. The glycerol-3-phopshate is then oxidized to DHAP by either an L - glycerol-3-phosphate oxidase enzyme (A) or a glycerol-3-phosphate dehydrogenase enzyme (B).
    Figure Legend Snippet: Enzymatic cascades for the conversion of glycerol to DHAP via glycerol-3-phosphate. Glycerol is converted to glycerol-3-phosphate by a glycerol kinase enzyme with concomitant regeneration of ATP by an acetate or pyruvate kinase enzyme. The glycerol-3-phopshate is then oxidized to DHAP by either an L - glycerol-3-phosphate oxidase enzyme (A) or a glycerol-3-phosphate dehydrogenase enzyme (B).

    Techniques Used:

    Details of the optimized cascade for the production of DHAP from glycerol. Phosphorylation of glycerol by ATP mediated by GlpK Tk (EC 2.7.1.30) and Mg 2+ via a phosphotransfer mechanism [ 33 ] was accompanied by regeneration of ATP from ADP by AceK Ms (EC 2.7.2.1), which catalyzes reversibly the phosphorylation of acetate in the presence of a divalent cation and ATP with the formation of acetylphosphate and ADP[ 34 ]. Cytosolic glycerophosphate oxidase GlpO Mg (EC 1.1.3.21) likely converts glycerol-3-phosphate to DHAP by a similar mechanism to the related GlpO from Mycoplasma pneumoniae (4X9M) [ 35 ]), Similarly to other flavoprotein oxidases, glycerophosphate oxidase GlpO enzymes follow a hydride transfer mechanism to stabilize a positive charge on the flavin N(5)-sulfite adduct (C). The hydrogen peroxide generated from the oxidation of enzymatic FADH 2 was converted to water by the addition of catalase from Micrococcus lysodeikticus .
    Figure Legend Snippet: Details of the optimized cascade for the production of DHAP from glycerol. Phosphorylation of glycerol by ATP mediated by GlpK Tk (EC 2.7.1.30) and Mg 2+ via a phosphotransfer mechanism [ 33 ] was accompanied by regeneration of ATP from ADP by AceK Ms (EC 2.7.2.1), which catalyzes reversibly the phosphorylation of acetate in the presence of a divalent cation and ATP with the formation of acetylphosphate and ADP[ 34 ]. Cytosolic glycerophosphate oxidase GlpO Mg (EC 1.1.3.21) likely converts glycerol-3-phosphate to DHAP by a similar mechanism to the related GlpO from Mycoplasma pneumoniae (4X9M) [ 35 ]), Similarly to other flavoprotein oxidases, glycerophosphate oxidase GlpO enzymes follow a hydride transfer mechanism to stabilize a positive charge on the flavin N(5)-sulfite adduct (C). The hydrogen peroxide generated from the oxidation of enzymatic FADH 2 was converted to water by the addition of catalase from Micrococcus lysodeikticus .

    Techniques Used: Mass Spectrometry, Generated

    Production of rare chiral sugars by combining optimized multi-enzyme cascades for DHAP production with a DHAP-dependant fructose-1,6-biphosphate aldolase. Glycerol (10mM substrate) was converted to glycerol-3-phosphate by a glycerol kinase enzyme GlpK Tk (28.6 pmoles) with concomitant regeneration of ATP by an acetate kinase enzyme AceK Ms (40.2 pmoles). The glycerol-3-phopshate was then oxidized to DHAP by a novel L -glycerol-3-phosphate oxidase enzyme GlpO Mg (154.2 pmoles), with mitigation of excess hydrogen peroxide by catalase (3U/mL) and an aldolase enzyme FruA Sc (3.1 nmoles) converted this and acceptor aldehydes (provided at 10mM) into chiral sugars D -fructose-1,6-biphosphate (3 S , 4 R ) and 3,4-dihydroxyhexulose phosphate (3 S , 4 R ) as depicted.
    Figure Legend Snippet: Production of rare chiral sugars by combining optimized multi-enzyme cascades for DHAP production with a DHAP-dependant fructose-1,6-biphosphate aldolase. Glycerol (10mM substrate) was converted to glycerol-3-phosphate by a glycerol kinase enzyme GlpK Tk (28.6 pmoles) with concomitant regeneration of ATP by an acetate kinase enzyme AceK Ms (40.2 pmoles). The glycerol-3-phopshate was then oxidized to DHAP by a novel L -glycerol-3-phosphate oxidase enzyme GlpO Mg (154.2 pmoles), with mitigation of excess hydrogen peroxide by catalase (3U/mL) and an aldolase enzyme FruA Sc (3.1 nmoles) converted this and acceptor aldehydes (provided at 10mM) into chiral sugars D -fructose-1,6-biphosphate (3 S , 4 R ) and 3,4-dihydroxyhexulose phosphate (3 S , 4 R ) as depicted.

    Techniques Used: Mass Spectrometry

    Related Articles

    other:

    Article Title: Cell-Free Phospholipid Biosynthesis by Gene-Encoded Enzymes Reconstituted in Liposomes
    Article Snippet: Texas Red 1,2-dihexadecanoyl-sn -glycero-3-phosphoethanolamine, triethylammonium salt (Texas Red DHPE), 212 μm-300 μm acid washed glass beads, chloroform, methanol, acetylacetone, glycerol-3-phosphate (G3P), β-mercaptoethanol, and L-serine were from Sigma-Aldrich.

    Article Title: Pivotal role of inter-organ aspartate metabolism for treatment of mitochondrial aspartate-glutamate carrier 2 (citrin) deficiency, based on the mouse model
    Article Snippet: Glutamate dehydrogenase, glycerol-3-phosphate dehydrogenase and lactate dehydrogenase were purchased from Sigma-Aldrich Japan, Osaka, Japan.

    FLAG-tag:

    Article Title: The Ca2+/Mn2+ ion-pump PMR1 links elevation of cytosolic Ca2+ levels to α-synuclein toxicity in Parkinson's disease models
    Article Snippet: .. Blots were probed with monoclonal antibodies against FLAG-epitope (Sigma), GFP (Sigma), glyceraldehyd-3-phosphate dehydrogenase (Sigma) and Aequorin (Abcam, Cambridge, UK) and the respective peroxidase-conjugated affinity-purified secondary antibodies (Sigma). ..

    Affinity Purification:

    Article Title: The Ca2+/Mn2+ ion-pump PMR1 links elevation of cytosolic Ca2+ levels to α-synuclein toxicity in Parkinson's disease models
    Article Snippet: .. Blots were probed with monoclonal antibodies against FLAG-epitope (Sigma), GFP (Sigma), glyceraldehyd-3-phosphate dehydrogenase (Sigma) and Aequorin (Abcam, Cambridge, UK) and the respective peroxidase-conjugated affinity-purified secondary antibodies (Sigma). ..

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    Millipore glyceraldehyd 3 phosphate dehydrogenase
    Expression of α Syn causes a slight upregulation of PMR1 and CCH1 mRNA levels. ( a ) Representative micrographs of yeast cells expressing endogenously GFP-tagged Pmr1p in combination with α Syn or corresponding vector control at indicated time points after induction of α Syn expression. ( b ) Western blot analysis of cells described in ( a ) at indicated time points after induction of α Syn expression. Blots were probed with antibodies against GFP to detect Pmr1p-GFP fusion protein, against FLAG-epitope to detect FLAG-tagged α Syn and against <t>glyceraldehyd-3-phosphate</t> dehydrogenase (GAPDH) as loading control. ( c and d ) Q-PCR-based quantification of PMR1 mRNA levels ( c ) and of CCH1 and MID1 mRNA levels ( d ) in WT cells expressing α Syn or harbouring the empty vector control for 14 h or 24 h, respectively, normalized to actin mRNA levels. Means±S.E.M., n =6–9; * P
    Glyceraldehyd 3 Phosphate Dehydrogenase, supplied by Millipore, used in various techniques. Bioz Stars score: 93/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Expression of α Syn causes a slight upregulation of PMR1 and CCH1 mRNA levels. ( a ) Representative micrographs of yeast cells expressing endogenously GFP-tagged Pmr1p in combination with α Syn or corresponding vector control at indicated time points after induction of α Syn expression. ( b ) Western blot analysis of cells described in ( a ) at indicated time points after induction of α Syn expression. Blots were probed with antibodies against GFP to detect Pmr1p-GFP fusion protein, against FLAG-epitope to detect FLAG-tagged α Syn and against glyceraldehyd-3-phosphate dehydrogenase (GAPDH) as loading control. ( c and d ) Q-PCR-based quantification of PMR1 mRNA levels ( c ) and of CCH1 and MID1 mRNA levels ( d ) in WT cells expressing α Syn or harbouring the empty vector control for 14 h or 24 h, respectively, normalized to actin mRNA levels. Means±S.E.M., n =6–9; * P

    Journal: Cell Death and Differentiation

    Article Title: The Ca2+/Mn2+ ion-pump PMR1 links elevation of cytosolic Ca2+ levels to α-synuclein toxicity in Parkinson's disease models

    doi: 10.1038/cdd.2012.142

    Figure Lengend Snippet: Expression of α Syn causes a slight upregulation of PMR1 and CCH1 mRNA levels. ( a ) Representative micrographs of yeast cells expressing endogenously GFP-tagged Pmr1p in combination with α Syn or corresponding vector control at indicated time points after induction of α Syn expression. ( b ) Western blot analysis of cells described in ( a ) at indicated time points after induction of α Syn expression. Blots were probed with antibodies against GFP to detect Pmr1p-GFP fusion protein, against FLAG-epitope to detect FLAG-tagged α Syn and against glyceraldehyd-3-phosphate dehydrogenase (GAPDH) as loading control. ( c and d ) Q-PCR-based quantification of PMR1 mRNA levels ( c ) and of CCH1 and MID1 mRNA levels ( d ) in WT cells expressing α Syn or harbouring the empty vector control for 14 h or 24 h, respectively, normalized to actin mRNA levels. Means±S.E.M., n =6–9; * P

    Article Snippet: Blots were probed with monoclonal antibodies against FLAG-epitope (Sigma), GFP (Sigma), glyceraldehyd-3-phosphate dehydrogenase (Sigma) and Aequorin (Abcam, Cambridge, UK) and the respective peroxidase-conjugated affinity-purified secondary antibodies (Sigma).

    Techniques: Expressing, Plasmid Preparation, Western Blot, FLAG-tag, Polymerase Chain Reaction

    Ca 2+ rather than Mn 2+ transport activity of Pmr1p contributes to α Syn toxicity. ( a ) Spotting assays of WT and Δ pmr1 yeast cells expressing either Pmr1p or the point mutants Pmr1p D53A and Pmr1p Q783A alone or in combination with α Syn. Cells were grown for 24 h in galactose media and spotted in fivefold serial dilutions onto glucose (Pmr1p and α Syn expression repressed) and galactose (Pmr1p and α Syn expression induced) plates supplemented or not with 1 mM and 4 mM Mn 2+ . ( b ) Cells described in ( a ) were subjected to clonogenic survival plating on galactose plates supplemented or not with 1 mM Mn 2+ . Survival has been normalized to WT cells harbouring both empty vectors plated on galactose plates without manganese. Mean±S.E.M., n =12–16. ( c ) Western blot analysis of Pmr1p, Pmr1p D53A and Pmr1p Q783A overexpression as well as of α Syn expression in WT and Δ pmr1 yeast cells. Blots were probed with antibodies directed against FLAG-epitope to detect FLAG-tagged Pmr1p variants and α Syn and against glyceraldehyd-3-phosphate dehydrogenase (GAPDH) as loading control

    Journal: Cell Death and Differentiation

    Article Title: The Ca2+/Mn2+ ion-pump PMR1 links elevation of cytosolic Ca2+ levels to α-synuclein toxicity in Parkinson's disease models

    doi: 10.1038/cdd.2012.142

    Figure Lengend Snippet: Ca 2+ rather than Mn 2+ transport activity of Pmr1p contributes to α Syn toxicity. ( a ) Spotting assays of WT and Δ pmr1 yeast cells expressing either Pmr1p or the point mutants Pmr1p D53A and Pmr1p Q783A alone or in combination with α Syn. Cells were grown for 24 h in galactose media and spotted in fivefold serial dilutions onto glucose (Pmr1p and α Syn expression repressed) and galactose (Pmr1p and α Syn expression induced) plates supplemented or not with 1 mM and 4 mM Mn 2+ . ( b ) Cells described in ( a ) were subjected to clonogenic survival plating on galactose plates supplemented or not with 1 mM Mn 2+ . Survival has been normalized to WT cells harbouring both empty vectors plated on galactose plates without manganese. Mean±S.E.M., n =12–16. ( c ) Western blot analysis of Pmr1p, Pmr1p D53A and Pmr1p Q783A overexpression as well as of α Syn expression in WT and Δ pmr1 yeast cells. Blots were probed with antibodies directed against FLAG-epitope to detect FLAG-tagged Pmr1p variants and α Syn and against glyceraldehyd-3-phosphate dehydrogenase (GAPDH) as loading control

    Article Snippet: Blots were probed with monoclonal antibodies against FLAG-epitope (Sigma), GFP (Sigma), glyceraldehyd-3-phosphate dehydrogenase (Sigma) and Aequorin (Abcam, Cambridge, UK) and the respective peroxidase-conjugated affinity-purified secondary antibodies (Sigma).

    Techniques: Activity Assay, Expressing, Western Blot, Over Expression, FLAG-tag

    C. elegans GPATs, acl-4, acl-5, and acl-6, contribute to triacylglycerol synthesis. ( A ) In mammals and C. elegans , glycerol-3-phosphate acyltransferases (GPATs) are located on both the outer mitochondrial membrane (mitochondrial GPAT) and endoplasmic

    Journal: The EMBO Journal

    Article Title: Mitochondria-type GPAT is required for mitochondrial fusion

    doi: 10.1038/emboj.2013.77

    Figure Lengend Snippet: C. elegans GPATs, acl-4, acl-5, and acl-6, contribute to triacylglycerol synthesis. ( A ) In mammals and C. elegans , glycerol-3-phosphate acyltransferases (GPATs) are located on both the outer mitochondrial membrane (mitochondrial GPAT) and endoplasmic

    Article Snippet: Glycerol-3-phosphate and 1-monopalmitoyl-rac-glycerol were purchased from Sigma. sn -1-palmitoyl lysophosphatidic acid, sn -1-palmitoyl- sn -2-oleoyl phosphatidic acid, sn -1-palmitoyl lysophosphatidylcholine, and sn -1-oleoyl lysophosphatidylserine were purchased from Avanti Polar Lipids (Alabaster, AL, USA).

    Techniques:

    Enzymatic cascades for the conversion of glycerol to DHAP via glycerol-3-phosphate. Glycerol is converted to glycerol-3-phosphate by a glycerol kinase enzyme with concomitant regeneration of ATP by an acetate or pyruvate kinase enzyme. The glycerol-3-phopshate is then oxidized to DHAP by either an L - glycerol-3-phosphate oxidase enzyme (A) or a glycerol-3-phosphate dehydrogenase enzyme (B).

    Journal: PLoS ONE

    Article Title: Sugar analog synthesis by in vitro biocatalytic cascade: A comparison of alternative enzyme complements for dihydroxyacetone phosphate production as a precursor to rare chiral sugar synthesis

    doi: 10.1371/journal.pone.0184183

    Figure Lengend Snippet: Enzymatic cascades for the conversion of glycerol to DHAP via glycerol-3-phosphate. Glycerol is converted to glycerol-3-phosphate by a glycerol kinase enzyme with concomitant regeneration of ATP by an acetate or pyruvate kinase enzyme. The glycerol-3-phopshate is then oxidized to DHAP by either an L - glycerol-3-phosphate oxidase enzyme (A) or a glycerol-3-phosphate dehydrogenase enzyme (B).

    Article Snippet: GCMS analysis of glycerol, glycerol-3-phosphate (G3P) and dihydroxyacetone phosphate (DHAP) All three compounds could be separated and detected after derivatization with N -Methyl-N -(trimethylsilyl)trifluoroacetamide (MSTFA) in pyridine (Sigma-Aldrich, USA).

    Techniques:

    Details of the optimized cascade for the production of DHAP from glycerol. Phosphorylation of glycerol by ATP mediated by GlpK Tk (EC 2.7.1.30) and Mg 2+ via a phosphotransfer mechanism [ 33 ] was accompanied by regeneration of ATP from ADP by AceK Ms (EC 2.7.2.1), which catalyzes reversibly the phosphorylation of acetate in the presence of a divalent cation and ATP with the formation of acetylphosphate and ADP[ 34 ]. Cytosolic glycerophosphate oxidase GlpO Mg (EC 1.1.3.21) likely converts glycerol-3-phosphate to DHAP by a similar mechanism to the related GlpO from Mycoplasma pneumoniae (4X9M) [ 35 ]), Similarly to other flavoprotein oxidases, glycerophosphate oxidase GlpO enzymes follow a hydride transfer mechanism to stabilize a positive charge on the flavin N(5)-sulfite adduct (C). The hydrogen peroxide generated from the oxidation of enzymatic FADH 2 was converted to water by the addition of catalase from Micrococcus lysodeikticus .

    Journal: PLoS ONE

    Article Title: Sugar analog synthesis by in vitro biocatalytic cascade: A comparison of alternative enzyme complements for dihydroxyacetone phosphate production as a precursor to rare chiral sugar synthesis

    doi: 10.1371/journal.pone.0184183

    Figure Lengend Snippet: Details of the optimized cascade for the production of DHAP from glycerol. Phosphorylation of glycerol by ATP mediated by GlpK Tk (EC 2.7.1.30) and Mg 2+ via a phosphotransfer mechanism [ 33 ] was accompanied by regeneration of ATP from ADP by AceK Ms (EC 2.7.2.1), which catalyzes reversibly the phosphorylation of acetate in the presence of a divalent cation and ATP with the formation of acetylphosphate and ADP[ 34 ]. Cytosolic glycerophosphate oxidase GlpO Mg (EC 1.1.3.21) likely converts glycerol-3-phosphate to DHAP by a similar mechanism to the related GlpO from Mycoplasma pneumoniae (4X9M) [ 35 ]), Similarly to other flavoprotein oxidases, glycerophosphate oxidase GlpO enzymes follow a hydride transfer mechanism to stabilize a positive charge on the flavin N(5)-sulfite adduct (C). The hydrogen peroxide generated from the oxidation of enzymatic FADH 2 was converted to water by the addition of catalase from Micrococcus lysodeikticus .

    Article Snippet: GCMS analysis of glycerol, glycerol-3-phosphate (G3P) and dihydroxyacetone phosphate (DHAP) All three compounds could be separated and detected after derivatization with N -Methyl-N -(trimethylsilyl)trifluoroacetamide (MSTFA) in pyridine (Sigma-Aldrich, USA).

    Techniques: Mass Spectrometry, Generated

    Production of rare chiral sugars by combining optimized multi-enzyme cascades for DHAP production with a DHAP-dependant fructose-1,6-biphosphate aldolase. Glycerol (10mM substrate) was converted to glycerol-3-phosphate by a glycerol kinase enzyme GlpK Tk (28.6 pmoles) with concomitant regeneration of ATP by an acetate kinase enzyme AceK Ms (40.2 pmoles). The glycerol-3-phopshate was then oxidized to DHAP by a novel L -glycerol-3-phosphate oxidase enzyme GlpO Mg (154.2 pmoles), with mitigation of excess hydrogen peroxide by catalase (3U/mL) and an aldolase enzyme FruA Sc (3.1 nmoles) converted this and acceptor aldehydes (provided at 10mM) into chiral sugars D -fructose-1,6-biphosphate (3 S , 4 R ) and 3,4-dihydroxyhexulose phosphate (3 S , 4 R ) as depicted.

    Journal: PLoS ONE

    Article Title: Sugar analog synthesis by in vitro biocatalytic cascade: A comparison of alternative enzyme complements for dihydroxyacetone phosphate production as a precursor to rare chiral sugar synthesis

    doi: 10.1371/journal.pone.0184183

    Figure Lengend Snippet: Production of rare chiral sugars by combining optimized multi-enzyme cascades for DHAP production with a DHAP-dependant fructose-1,6-biphosphate aldolase. Glycerol (10mM substrate) was converted to glycerol-3-phosphate by a glycerol kinase enzyme GlpK Tk (28.6 pmoles) with concomitant regeneration of ATP by an acetate kinase enzyme AceK Ms (40.2 pmoles). The glycerol-3-phopshate was then oxidized to DHAP by a novel L -glycerol-3-phosphate oxidase enzyme GlpO Mg (154.2 pmoles), with mitigation of excess hydrogen peroxide by catalase (3U/mL) and an aldolase enzyme FruA Sc (3.1 nmoles) converted this and acceptor aldehydes (provided at 10mM) into chiral sugars D -fructose-1,6-biphosphate (3 S , 4 R ) and 3,4-dihydroxyhexulose phosphate (3 S , 4 R ) as depicted.

    Article Snippet: GCMS analysis of glycerol, glycerol-3-phosphate (G3P) and dihydroxyacetone phosphate (DHAP) All three compounds could be separated and detected after derivatization with N -Methyl-N -(trimethylsilyl)trifluoroacetamide (MSTFA) in pyridine (Sigma-Aldrich, USA).

    Techniques: Mass Spectrometry

    Effects of amino acid supplementation on hepatic glycerol 3-phosphate (G3P; panel (a)), aspartate (Asp; panel (b)), and citrulline ( c ) levels in mGPD-KO mice administered 5% ethanol. Amino acid solutions (1 M; with the exception of glutamine and asparagine at 0.5 M) was enterally administered with 5% ethanol (20 ml/kg bw), and the liver was removed by freeze-cramp procedure 1 h after administration. Data are expressed as mean ± SEM. Asterisks (*P 

    Journal: Scientific Reports

    Article Title: Pivotal role of inter-organ aspartate metabolism for treatment of mitochondrial aspartate-glutamate carrier 2 (citrin) deficiency, based on the mouse model

    doi: 10.1038/s41598-019-39627-y

    Figure Lengend Snippet: Effects of amino acid supplementation on hepatic glycerol 3-phosphate (G3P; panel (a)), aspartate (Asp; panel (b)), and citrulline ( c ) levels in mGPD-KO mice administered 5% ethanol. Amino acid solutions (1 M; with the exception of glutamine and asparagine at 0.5 M) was enterally administered with 5% ethanol (20 ml/kg bw), and the liver was removed by freeze-cramp procedure 1 h after administration. Data are expressed as mean ± SEM. Asterisks (*P 

    Article Snippet: Glutamate dehydrogenase, glycerol-3-phosphate dehydrogenase and lactate dehydrogenase were purchased from Sigma-Aldrich Japan, Osaka, Japan.

    Techniques: Mouse Assay