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evolution
structural and phylogenetic comparisons reveal four main structure types among the five families of glycerol-3-phosphate and glycerol-1-phosphate dehydrogenases, overview
evolution
Gpd1p from Saccharomyces kudriavzevii presented five conserved amino acid replacements compared to Saccharomyces cerevisiae (Ala31Ile, Ile67leu, Glu76Asp, Asp142Asn and Ser143Pro) out of 391 total residues, corresponding to an identity of 98.7%
evolution
Gpd1p from Saccharomyces kudriavzevii presented five conserved amino acid replacements compared to Saccharomyces cerevisiae (Ala31Ile, Ile67leu, Glu76Asp, Asp142Asn and Ser143Pro) out of 391 total residues, corresponding to an identity of 98.7%
evolution
the intronless genes Cagpd1 and Cagpd2, encoding the two isozymes of the organism, are both predicted to encode a 378 amino acid polypeptide, and the deduced amino acid sequences mutually show 76% identity. Genes Cagpd1 and Cagpd2 are located tandemly in a locus of genomic DNA within a 262 bp interval
evolution
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the intronless genes Cagpd1 and Cagpd2, encoding the two isozymes of the organism, are both predicted to encode a 378 amino acid polypeptide, and the deduced amino acid sequences mutually show 76% identity. Genes Cagpd1 and Cagpd2 are located tandemly in a locus of genomic DNA within a 262 bp interval
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malfunction
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Drosophila GPDH-1-null mutants cannot fly
malfunction
mutation N270A results in a 7.7 kcal/mol decrease in the intrinsic phosphodianion binding energy, which is larger than the 5.6 kcal/mol effect of the mutation on the stability of the transition state for reduction of DHAP. A 2.2 kcal/mol stabilization of the transition state for unactivated hydride transfer to the truncated substrate glycolaldehyde, and a change in the effect of phosphite dianion on GPDH-catalyzed reduction of glycolaldehyde, from strongly activating to inhibiting. The N270A mutation breaks the network of hydrogen bonding side chains, Asn270, Thr264, Asn205, Lys204, Asp260, and Lys120, which connect the dianion activation and catalytic sites of GPDH. The disruption dramatically alters the performance of GPDH at these sites
metabolism
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glycerol-3-phosphate dehydrogenase is a key enzyme in the pathway of glycerol synthesis, which converts dihydroxyacetone phosphate to glycerol-3-phosphate
metabolism
the interconversion of glycerol 3-phosphate and dihydroxyacetone phosphate by glycerol-3-phosphate dehydrogenases provides a link between carbohydrate and lipid metabolism. Glycerol 3-phosphate from the breakdown of phospholipids and triglycerides (via glycerol kinase) is converted into the glycolysis intermediate dihydroxyacetone phosphate, while the reverse reaction produces glycerol 3-phosphate, which is required for the synthesis of triglycerides and phospholipids
metabolism
glycerol-3-phosphate dehydrogenase (G3PDH) is a key enzyme in the pathway of glycerol synthesis, which converts dihydroxyacetone phosphate (DHAP) to glycerol-3-phosphate
metabolism
Gpd1p is the flux controlling enzyme in the glycerol biosynthetic pathway
metabolism
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isoform G3PD1 plays an important role during fatty acid accumulation in Mortierelle alpine
metabolism
Saccharomyces kudriavzevii has changed the metabolism to promote the branch of the glycolytic pathway involved in glycerol production to adapt to low temperature environments and maintain the NAD+/NADH ratio in alcoholic fermentations. Gpd1p is the flux controlling enzyme in the glycerol biosynthetic pathway
metabolism
the enzyme is a key enzyme in the glycerol biosynthesis pathway
metabolism
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isoform G3PD1 plays an important role during fatty acid accumulation in Mortierelle alpine
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metabolism
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the enzyme is a key enzyme in the glycerol biosynthesis pathway
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metabolism
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glycerol-3-phosphate dehydrogenase is a key enzyme in the pathway of glycerol synthesis, which converts dihydroxyacetone phosphate to glycerol-3-phosphate
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physiological function
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GPDH-1 in the cytoplasm and a glycerophosphate oxidase in the mitochondrion cooperate in Drosophila flight muscles to generate the ATP needed for muscle contraction
physiological function
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in spermatozoa from homozygous Gpd2 deletion mice, in the absence of Gpd2, hyperactivation and acrosome reaction are significantly altered, and a few changes in protein tyrosine phosphorylation are also observed during capacitation. GPD2 activity is required for generation of reactive oxygen species in mouse spermatozoa during capacitation, failing which, capacitation is impaired
physiological function
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no change in G3PDH activity is observed under salt stress of 0.5 M NaCl, while significant increase in G3PDH activity is observed at high salt concentration of 1.5 M NaCl. G3PDH activity is suppressed at all growth phases of the organism under temperature stress of 20°C and 40°C. No significant change in G3PDH activity is observed at mid log/stationary phase of growth under pH stress condition. At late stationary phase of growth, G3PDH activity increases with decrease in pH of the medium as compared to control
physiological function
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G3PDH is an important locus in fuel catabolism in hibernating species
physiological function
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glycerol 3-phosphate dehydrogenase plays an important role in the energy metabolism and nutrition metabolism
physiological function
the cytosolic activity of glycerol-3-phosphate dehydrogenase 1 plays an important role in the synthesis of triacylglycerol and in the transport of reducing equivalents from the cytosol to mitochondria
physiological function
the interconversion of glycerol 3-phosphate and dihydroxyacetone phosphate by glycerol-3-phosphate dehydrogenases provides Saccharomyces cerevisiae with protection against osmotic and anoxic stress. The concerted action of cytosolic (NAD+-dependent) G3PDHs and membrane-bound (FAD-dependent) G3PDHs transfers reducing equivalents from cytosolic NADH into the electron-transport chain of both bacteria and mitochondria
physiological function
glycerol is increased in Saccharomyces kudriavzevii mainly due to increased Vmax of the Gpd1p enzyme
physiological function
isoform GPDH-1 is involved in flight metabolism
physiological function
isoform GPDH-2 provides lipid precursors
physiological function
isoform GPDH2 is involved in glycerol synthesis and osmotic stress tolerance
physiological function
isoform GPDH3 is involved in glycerol synthesis and osmotic stress tolerance
physiological function
role for Asn270 in glycerol 3-phosphate dehydrogenase-catalyzed hydride transfer
physiological function
the enzyme catalyzes the formation of glycerol 3-phosphate, the backbone of many membrane lipids. Overexpression of plastidic enzyme G3pDH enhances biosynthesis of plastid-localized lipids in rice, and photosynthetic efficiency is enhanced in the transgenic plants
physiological function
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the enzyme is important for osmotolerance
physiological function
the enzyme is involved in osmotic stress response
physiological function
the glycerol-DHAP cycle pathway, which is driven by enzyme G3PDH, is considered as the rate-limiting enzyme to regulate the glycerol level under osmotic shocks
physiological function
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the hibernating form of G3PDH from the liver of Richardson's ground squirrels maintains better functionality at low temperatures and has greater temperature stability. These properties help sustain G3PDH function over the wide range of body temperatures experienced by the species as they cycle though torpor-arousal bouts over the hibernating season
physiological function
two glycerol 3-phosphate dehydrogenase isozymes from Candida versatilis SN-18 play an important role in glycerol biosynthesis under osmotic stress. The enzyme is involved in osmotic stress response
physiological function
Camelina sativa coexpressing Arabidopsis thaliana diacylglycerol acyltransferase1 (DGAT1) and yeast cytosolic glycerol-3-phosphate dehydrogenase (GPD1) genes exhibit up to 13% higher seed oil content and up to 52% increase in seed mass compared to wild-type plants. DGAT1- and GDP1-coexpressing lines show significantly higher seed and oil yields on a dry weight basis than the wild-type controls or plants expressing DGAT1 and GPD1 alone. The oil harvest index (g oil per g total dry matter) for DGTA1- and GPD1-coexpressing lines is almost twofold higher as compared to wild type and the lines expressing DGAT1 and GPD1 alone
physiological function
exogenous expression of GPD1 in human MCF-7 and MDA-MB-231 breast cancer cells significantly inhibits cell proliferation, migration, and invasion
physiological function
GPDH1 regulates larval NAD+/NADH redox balance and ATP levels. Larvae lacking both lactate dehydrogenase and G3P dehydrogenase (GPDH1) exhibit growth defects, synthetic lethality and decreased glycolytic flux, simultaneous loss of LDH and GPDH1 disrupts ATP homeostasis and glycolytic flux
physiological function
the enzyme plays an essential role in glycerolipid metabolism and in response to various stresses in different species
physiological function
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no change in G3PDH activity is observed under salt stress of 0.5 M NaCl, while significant increase in G3PDH activity is observed at high salt concentration of 1.5 M NaCl. G3PDH activity is suppressed at all growth phases of the organism under temperature stress of 20°C and 40°C. No significant change in G3PDH activity is observed at mid log/stationary phase of growth under pH stress condition. At late stationary phase of growth, G3PDH activity increases with decrease in pH of the medium as compared to control
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physiological function
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the enzyme is involved in osmotic stress response
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physiological function
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two glycerol 3-phosphate dehydrogenase isozymes from Candida versatilis SN-18 play an important role in glycerol biosynthesis under osmotic stress. The enzyme is involved in osmotic stress response
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physiological function
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Camelina sativa coexpressing Arabidopsis thaliana diacylglycerol acyltransferase1 (DGAT1) and yeast cytosolic glycerol-3-phosphate dehydrogenase (GPD1) genes exhibit up to 13% higher seed oil content and up to 52% increase in seed mass compared to wild-type plants. DGAT1- and GDP1-coexpressing lines show significantly higher seed and oil yields on a dry weight basis than the wild-type controls or plants expressing DGAT1 and GPD1 alone. The oil harvest index (g oil per g total dry matter) for DGTA1- and GPD1-coexpressing lines is almost twofold higher as compared to wild type and the lines expressing DGAT1 and GPD1 alone
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physiological function
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the cytosolic activity of glycerol-3-phosphate dehydrogenase 1 plays an important role in the synthesis of triacylglycerol and in the transport of reducing equivalents from the cytosol to mitochondria
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physiological function
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the enzyme is important for osmotolerance
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additional information
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when Dunaliella salina is cultured chronically at various salinities, the accumulation of single cell glycerol increases with increased salinity, Dunaliella salina also can rapidly decrease or increase single cell glycerol contents to adapt to hypoosmotic or hyperosmotic shock
additional information
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structure-function analysis of wild-type and mutant enzymes, overview
additional information
structure-function analysis of wild-type and mutant enzymes, overview
additional information
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three-dimensional structure modeling of enzyme G3PDH to identify the potential phosphorylation site (83Tyr) responsible for the differential phosphorylation between euthermic and hibernator G3PDH. Structural and functional changes in G3PDH support the enzyme's function at a low core body temperature experienced during the species hibernating season
additional information
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when Dunaliella salina is cultured chronically at various salinities, the accumulation of single cell glycerol increases with increased salinity, Dunaliella salina also can rapidly decrease or increase single cell glycerol contents to adapt to hypoosmotic or hyperosmotic shock
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