1.1.1.6: glycerol dehydrogenase
This is an abbreviated version!
For detailed information about glycerol dehydrogenase, go to the full flat file.
Reaction
Synonyms
B4100_2156, CglD, dehydrogenase, glycerol, GDH, GDH2, GLD, Gld3, GldA, GLDH
ECTree
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Application
Application on EC 1.1.1.6 - glycerol dehydrogenase
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analysis
biofuel production
proteome analysis as well as enzyme assays performed in cell-free extracts demonstrates that glycerol is degraded via glyceraldehyde-3-phosphate, which is further metabolized through the lower part of glycolysis leading to formation of mainly ethanol and hydrogen. Fermentation of glycerol to ethanol and hydrogen by this bacterium represents a remarkable option to add value to the biodiesel industries by utilization of surplus glycerol
biotechnology
brewing
molecular biology
synthesis
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glycerol dehydrogenase can be immobilised in a polycarbamoyl sulfonate-hydrogel and used as a sensor for glycerol
analysis
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development of an integrated multienzyme electrochemical biosensor for the determination of glycerol in wines. The biosensor is based on the glycerol dehydrogenase/diaphorase bienzyme system. The enzyme system is immobilized together with the mediator tetrathiafulvalene on a 3-mercaptopropionic acid self-assembled monolayer-modified gold electrode by using a dialysis membrane
analysis
the recombinant chimeric fusion enzyme GDH-NOX has a potential application for quick glycerol analysis and dioxyacetone biosynthesis
analysis
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assay for triglycerides. Triglycerides are hydrolysed to glycerol and fatty acids by lipoprotein lipase followed by the oxidation of glycerol to dihydroxyacetone with simultaneous production of NADH by glycerol dehydrogenase. Addition of 2-(2-methoxy-4-nitrophenyl)-3-(4-nitrophenyl)-5-(2,4-disulfophenyl)-2H-tetrazolium monosodium salt (WST-8) to the reaction mixture removes NADH, allowing the reaction to complete while showing stoichiometric production of reduced WST-8. The reaction is linear up to 6.4mM, no interference by 2.5 g/l haemoglobin, 65 microM free bilirubin and 359 microM conjugated bilirubin is observed
analysis
GldA shows a strong intrinsic fluorescence at 320 nm, when excited at 280 nm. The fluorescence intensity decreases in the presence of NAD+, NADH, and dihydroxyacetone, the substrate and products for GldA, which allows to determine the dissociation constants for those molecules as 110.6 microM, 9,1 microM, 33.3 mM, respectively
analysis
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accurate, simple and sensitive method for the quantitative analysis of triglycerides. Assay for triglycerides using glycerol dehydrogenase and a water-soluble formazan dye, WST-8
analysis
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the recombinant chimeric fusion enzyme GDH-NOX has a potential application for quick glycerol analysis and dioxyacetone biosynthesis
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biotechnology
GlyDH is active with immobilized N6-CM-NAD+, suggesting that N6-CM-NAD+ can be immobilized on an electrode to allow TmGlyDH activity in a system that reoxidizes the cofactor electrocatalytically, development of a bioelectrocatalytic reactor
biotechnology
Thermotoga maritima MSB8 / DSM 3109 / ATCC 43589
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GlyDH is active with immobilized N6-CM-NAD+, suggesting that N6-CM-NAD+ can be immobilized on an electrode to allow TmGlyDH activity in a system that reoxidizes the cofactor electrocatalytically, development of a bioelectrocatalytic reactor
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enzymatic assay for the determination of glycerol in wine and beer
brewing
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enzymatic assay for the determination of glycerol in wine and beer
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enzymatic redox cofactor regeneration in organic media: functionalization and application of recombinant glycerol dehydrogenase and soluble transhydrogenase in reverse micelles, overview
molecular biology
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enzymatic redox cofactor regeneration in organic media: functionalization and application of recombinant glycerol dehydrogenase and soluble transhydrogenase in reverse micelles, overview
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high specificity of enzyme for secondary alcohols in R-configuration, use of enzyme for production of chiral compounds
synthesis
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biotransformation of glycerol to dihydroxyacetone by recombinant Gluconobacter oxydans DSM 2343. Overproduction of the glycerol dehydrogenase to improve production of dihydroxyacetone
synthesis
Thermoanaerobacter mathranii can produce ethanol from lignocellulosic biomass at high temperatures. Deletion of the Ldh gene coding for lactate dehydrogenase eliminates an NADH oxidation pathway. To further facilitate NADH regeneration used for ethanol formation, heterologous gene GldA is expressed leading to increased ethanol yield in the presence of glycerol using xylose as a substrate. The metabolism of the cells is shifted toward the production of ethanol over acetate, hence restoring the redox balance. The recombinant acquired the capability to utilize glycerol as an extra carbon source in the presence of xylose resulting in a higher ethanol yield
synthesis
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efficiency of a cofactor regeneration enzyme co-expressed with a glycerol dehydrogenase for the production of 1,3-dihydroxyacetone. In vitro biotransformation of glycerol is achieved with the cell-free extracts containing recombinant glycerol dehydrogenase from Escherichia coli, lactate dehydrogenase form Bacillus subtilis, or NADH oxidase LpNox1 from Lactobacillus pentosus, giving1,3-dihydroxyacetone (DHA), no expensive consumption of NAD+ for the production of DHA, overview. DHA is a valuable chemical with a wide range of applications in the cosmetics
synthesis
GlyDH is active with immobilized N6-CM-NAD+, suggesting that N6-CM-NAD+ can be immobilized on an electrode to allow TmGlyDH activity in a system that reoxidizes the cofactor electrocatalytically, development of a bioelectrocatalytic reactor
synthesis
engineering and immobilizing of glycerol dehydrogenase to accept alkyl/aryl glyceryl monoethers and catalyze their enantioselective oxidation to yield the corresponding 3-alkoxy/aryloxy-1-hydroxyacetones. The enzyme is highly enantioselective towards S-isomers (ee > 99%). Application of mutant L252A in a one-pot chemoenzymatic process to convert glycidol and ethanol into 3-ethoxy-1-hydroxyacetone and (R)-3-ethoxypropan-1,2-diol, without affecting the oxidation activity
synthesis
engineering of a hypertransformable variant of Clostridium pasteurianum for bioconversion of glycerol into hydrogen via increasing product yield by overexpression of enzyme catalyzing H2 production, and increasing substrate uptake by overexpression of enzymes involved in glycerol utilization. Overexpression of the HydA gene encoding hydrogenase, and overexpression of DhaD1 and DhaK genes encoding glycerol dehydrogenase and dihydroxyacetone kinase result in two recombinant strains (HydA++/HhaD1K++) capable of producing 97% H2 (v/v), with yields of 1.1 mol H2/mol glycerol in HydA overexpressed strain, and 0.93 mol H2/mol glycerol in DhaD1K overexpressing strain
synthesis
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immobilization of Escherichia coli cells harboring the recombinant glycerol dehydrogenase gene on mannose-functionalized magnetic nanoparticles for conversion of glycerol to 1,3-dihydroxyacetone. Immobilization uses specific binding between mannose on the nanoparticles and the FimH lectin on the Escherichia coli cell surface via hydrogen bonds and hydrophobic interactions. Compared with the free cells, the thermostability of the immobilized cells is improved 2.56fold at 37°C. More than 50% of the initial activity of the immobilized cells remains after 10 cycles
synthesis
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regeneration of NAD+ in enzyme-catalyzed reactions using aggreagets of glycerol dehydrogenase and NADH oxidase. After optimization, the activities of combi-aggregates and separate aggregates mixtures are 950 and 580 U/g, respectively. After ten cycles of reuse, the catalytic efficiency may still retain 63.3% of its initial activity. The conversion of glycerol to 1,3-dihydroxyacetone is 4.6%, which is 2.5 times of the free enzyme system
synthesis
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engineering of a hypertransformable variant of Clostridium pasteurianum for bioconversion of glycerol into hydrogen via increasing product yield by overexpression of enzyme catalyzing H2 production, and increasing substrate uptake by overexpression of enzymes involved in glycerol utilization. Overexpression of the HydA gene encoding hydrogenase, and overexpression of DhaD1 and DhaK genes encoding glycerol dehydrogenase and dihydroxyacetone kinase result in two recombinant strains (HydA++/HhaD1K++) capable of producing 97% H2 (v/v), with yields of 1.1 mol H2/mol glycerol in HydA overexpressed strain, and 0.93 mol H2/mol glycerol in DhaD1K overexpressing strain
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synthesis
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high specificity of enzyme for secondary alcohols in R-configuration, use of enzyme for production of chiral compounds
-
synthesis
Thermotoga maritima MSB8 / DSM 3109 / ATCC 43589
-
Thermoanaerobacter mathranii can produce ethanol from lignocellulosic biomass at high temperatures. Deletion of the Ldh gene coding for lactate dehydrogenase eliminates an NADH oxidation pathway. To further facilitate NADH regeneration used for ethanol formation, heterologous gene GldA is expressed leading to increased ethanol yield in the presence of glycerol using xylose as a substrate. The metabolism of the cells is shifted toward the production of ethanol over acetate, hence restoring the redox balance. The recombinant acquired the capability to utilize glycerol as an extra carbon source in the presence of xylose resulting in a higher ethanol yield
-
synthesis
Thermotoga maritima MSB8 / DSM 3109 / ATCC 43589
-
GlyDH is active with immobilized N6-CM-NAD+, suggesting that N6-CM-NAD+ can be immobilized on an electrode to allow TmGlyDH activity in a system that reoxidizes the cofactor electrocatalytically, development of a bioelectrocatalytic reactor
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