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At least 19 recordsLinked to original sources
PubMed1980

The reconstitution of L-3-glycerophosphate-cytochrome c oxidoreductase from L-3-glycerophosphate dehydrogenase, ubiquinone-10 and ubiquinol-cytochrome c oxidoreductase.

Purified L-3-glycerophosphate dehydrogenase from pig brain mitochondria interacts with ubiquinone-10 and ubiquinol-cytochrome c oxidoreductase (Complex III) from bovine heart mitochondria to reconstitute antimycin-sensitive L-3-glycerophosphate- cytochrome c oxidoreductase. This activity is completely dependent on the two enzymes and largely dependent on ubiquinone-10. Reconstitution requires that the two enzymes should be simultaneously present in the same membranous aggregate produced by removal of detergent from the enzymes. Reconstitution by removing detergent by dialysis or dilution is inefficient because of self-aggregation of the dehydrogenase. Highly efficient reconstitution can be achieved if the enzymes are co-precipitated by addition of ethanol. The rate with reconstituted enzyme approaches that expected from the turnover of the dehydrogenase with ubiquinone-1 as acceptor. The behaviour of the reconstituted system shows some of the characteristics expected for a stoicheiometric association of one molecule of dehydrogenase with one molecule of Complex III. On raising the phospholipid/protein ratio, the dehydrogenase and Complex III appear to operate as independent enzymes acting in sequence. These effects are very similar to those observed for the interaction of NADH dehydrogenase and Complex III and are explained in terms of the model proposed by Heron, Ragan & Trumpower [(1978) biochem. J. 174, 791-800].

Animals↗
PubMed1977

Origin of alpha-glycerophosphate dehydrogenase isozymes in Drosophila melanogaster and their functional relationship in the alpha-glycerophosphate cycle.

The basis for the differentiation of L-glycerol-3-phosphate dehydrogenase (alpha-GPDH) into larval and adult isozymes in Drosophila melanogaster was investigated by the correlation of a lack of appearance of each isozyme during development within Drosophila bearing alpha-GPDH "null" alleles and by the study of a putative conversion factor. Conversion studies indicate the presence of a heat-labile RNase-resistant conversion factor present in crude larval extracts with the ability to convert GPDH-1 to GPDH-2 and GPDH-3 but not vice versa. In addition, "null" mutations at the Gpdh locus obliterate all isozymatic species of alpha-GPDH in all developmental stages. These observations suggest that all alpha-GPDH isozymes are the product of a single structural gene and that the multiple forms of this enzyme arise during successive developmental stages through an epigenetic modification of the primary Gpdh+ polypeptide. Finally, observations are reported which bear on the functional divergence of the alpha-glycerophosphate cycle in the adult and larval stage of development.

Alleles↗
PubMed1976

Regulation of alpha-glycerophosphate dehydrogenase activity in human term placental mitochondria.

1. alpha-Glycerophosphate dehydrogenase (sn-glycerol-3-phosphate:(acceptor) oxidoreductase, EC 1.1.99.5) activity in mitochondria isolated from human term placenta was found to be inhibited by ethyleneglycolbis (beta-aminoethyl ether)-N,N'-tetraacetic acid (EGTA). Addition of an excess of calcium ions to the incubation medium completely restored the original activity. The concentration of free calcium ion required to activate the alpha-glycerophosphate dehydrogenase was found to vary between 10 and 100 nM. 2. The pH optimum for alpha-glycerophosphate dehydrogenase activity varied with substrate concentration. The pH optima were 7.4 and 8.0 in the presence of 2 or 8 mM alpha-glycerophosphate, respectively. The apparent Km for alpha-glycerophosphate also varied with pH; the values being 0.4 mM at pH 7.05, 1.5 mM at pH 7.8, and 3.5 mM at pH 8.5. 3. alpha-Glycerophosphate dehydrogenase activity was inhibited by palmitoyl-CoA in a competitive manner with an apparent Ki value of about 10 muM. This inhibition was less pronounced in the presence of calcium or magnesium ions. 4. The activity of alpha-glycerophosphate dehydrogenase was inhibited by phosphoenolpyruvate, D- and DL-glyceraldehyde 3-phosphate and 3-phosphoglyceric acid, in a competitive manner, the apparent Ki values being 0.5, 0.95, 0.12 and 1.5 mM, respectively. 5. alpha-Glycerophosphate dehydrogenase activity in human placental mitochondria was found to be more sensitive to phosphoenolpyruvate, than the activity of the same enzyme in rat skeletal muscle mitochondria. alpha-Glycerophosphate dehydrogenase activity in rat brown adipose tissue mitochondria was only slightly affected by phosphenolpyruvate under the same conditions. 6. The data obtained suggest that the activity of alpha-glycerophosphate dehydrogenase in human placental mitochondria may be controlled by changes of the cytosolic level of palmitoyl-CoA, some glycolytic intermediates, and pH.

Adipose Tissue, Brown↗
PubMed1966

The components of an alpha-glycerophosphate cycle and their relation to oxidative metabolism in the lens.

1. The concentration of ATP in a lens brei is maintained when the brei is incubated in oxygen with alpha-glycerophosphate. Lack of alpha-glycerophosphate or incubation in nitrogen causes the concentration to decrease. alpha-Glycerophosphate has some effect under anaerobic conditions but this is not sufficient to account for the maintenance in oxygen. 2. Manometric experiments show that alpha-glycerophosphate enhances the respiration of lens preparations. This respiration can be further increased by the addition of ADP and is abolished by cyanide and antimycin. The inference from these experiments is that a mitochondrial system able to oxidize alpha-glycerophosphate is present, i.e. the particulate half of the alpha-glycerophosphate cycle. 3. More than the calculated proportion of NADH is used when limiting amounts of dihydroxyacetone phosphate are added to lens tissue in spectrophotometric experiments. Dihydroxyacetone phosphate is therefore regenerated and an alpha-glycerophosphate cycle is operative. 4. A preparation of a particulate alpha-glycerophosphate dehydrogenase that takes up oxygen with methylene blue as electron acceptor is described. 5. Methods for obtaining mitochondria from lens are compared, and a useful extraction medium is defined. 6. Mitochondria with activities of the same order of magnitude as those obtained from liver, with alpha-glycerophosphate and glutamate as substrates, are prepared from epithelium detached from the capsule; some respiratory control is observed.

Adenine Nucleotides↗
PubMed1965

Growth stasis by accumulated L-alpha-glycerophosphate in Escherichia coli.

Cozzarelli, N. R. (Harvard Medical School, Boston, Mass.), J. P. Koch, S. Hayashi, and E. C. C. Lin. Growth stasis by accumulated l-alpha-glycerophosphate in Escherichia coli. J. Bacteriol. 90:1325-1329.1965.-Cells of Escherichia coli K-12 can grow on either glycerol or l-alpha-glycerophosphate as the sole source of carbon and energy. The first step in the dissimilation of glycerol requires a kinase, and the initial process of utilization of l-alpha-glycerophosphate involves an active transport system. In either case, intracellular l-alpha-glycerophosphate is an intermediate whose further metabolism depends upon a dehydrogenase. When this enzyme is lost by mutation, the cells not only fail to grow on glycerol or l-alpha-glycerophosphate, but are subject to growth inhibition in the presence of either compound. Resistance to inhibition by glycerol can be achieved by the loss of glycerol kinase. Such cells are still susceptible to growth inhibition by l-alpha-glycerophosphate. Similarly, in dehydrogenase-deficient cells, immunity to exogenous l-alpha-glycerophosphate can be achieved by genetic blocking of the active transport system. Such cells are still sensitive to free glycerol in the growth medium. Reversal of inhibition by glycerol or l-alpha-glycerophosphate in cells lacking the dehydrogenase can also be brought about by the addition of glucose. Glucose achieves this effect without recourse to catabolite repression. Our results suggest that growth stasis associated with the over-accumulation of l-alpha-glycerophosphate is due to interference with other cellular processes by competition with physiological substrates rather than to depletion of cellular stores of adenosine triphosphate or inorganic phosphate.

Escherichia coli↗
PubMed1970

Specificity and locale of the L-3-glycerophosphate-flavoprotein oxidoreductase of mitochondria isolated from the flight muscle of Sarcophaga barbata thoms.

1. The oxidation of l-3-glycerophosphate by flight-muscle mitochondria isolated from the flesh fly Sarcophaga barbata has been studied. Use of substrate analogues indicates that the catalytic and effector l-3-glycerophosphate binding sites on the allosteric l-3-glycerophosphate-flavoprotein oxidoreductase differ markedly in specificity. 2. The l-3-glycerophosphate-cyanoferrate oxidoreductase system in these mitochondria is antimycin-insensitive whereas the corresponding NADH-cyanoferrate oxidoreductase is extremely sensitive to this respiratory-chain inhibitor. Also no swelling is observed when these mitochondria are suspended in iso-osmotic solutions of ammonium glycerophosphate in contrast with the extensive swelling seen in similar solutions of ammonium pyruvate. These observations indicate that l-3-glycerophosphate does not penetrate the mitochondrial matrix whereas pyruvate does. 3. Submitochondrial particles catalyse the ATP-driven reduction of NAD(+) by l-3-glycerophosphate but at a far lower rate than that seen when succinate is the electron donor. These particles do not have an energy-linked pyridine nucleotide transhydrogenase activity. 4. We conclude that the l-3-glycerophosphate-flavoprotein oxidoreductase is located on the outer surface of the inner membrane of the flight-muscle mitochondria.

Adenosine Triphosphate↗
PubMed1979

Purification and properties of L-alpha-glycerophosphate oxidase from Streptococcus faecium ATCC 12755.

A procedure was developed to purify the Streptococcus faecium ATCC 12755 L-alpha-glycerophosphate oxidase. The molecular weight of the purified enzyme was 131,000 and the subunit molecular weight was 72,000. Two moles of FAD were bound/mol of enzyme. Apo-L-alpha-glycerophosphate oxidase displayed physical properties similar to the holoenzyme as judged by electrophoresis in 10% buffer gels at pH 8.5 and by centrifugation in a 5 to 20% linear sucrose gradient. The apoenzyme was completely reactivated by incubation with FAD. L-alpha-Glycerophosphate oxidase was specific for L-alpha-glycerophosphate when compared with several other pohsphorylated glycerol and sugar derivatives. Oxygen was the preferred electron acceptor. At 10 mM DL-alpha-glycerophosphate (below the Km of 26 mM for L-alpha-glycerophosphate), activity was increased from 2.6- to 10-fold by increasing the buffer concentration from 0.01 to 0.1 m. This buffer effect was observed with potassium phosphate and other anionic buffers. In 0.001 m potassium phosphate buffer, pH 7.0, activity was increased by several divalent metal ions, including 10 mM CaCl2 (7.7-fold activation) and 10 mM MgCl, (6.8-fold activation). Fructose 6-phosphate and fructose1-phosphate were inhibitors of the L-alpha-glycerophosphate oxidase.

Cations, Divalent↗
PubMed1976

High activity of alpha-glycerophosphate oxidation by human placental mitochondria.

Human term placental mitochondria oxidize alpha-glycerophosphate at an unusually high rate as compared to other substrates. The apparent Km both for oxidation and alpha-glycerophosphate dehydrogenase (EC 1.1.99.5) activity of DL-alpha glycerophosphate determined in a medium containing 2mM EDTA and 5 mM MgSO4 was approx. 0.7 mM. EDTA inhibited the alpha-glycerophosphate oxidation if the later was used at low concentrations. A subsequent addition of MgSO4 or CaCl2 restored the original activity. EDTA had no effect on mitochondrial respiration at high concentration of alpha-glycerophosphate. Possible physiological role of relatively high activity of human placental mitochondrial alpha-glycerophosphate dehydrogenase is discussed.

Carbonyl Cyanide m-Chlorophenyl Hydrazone↗
PubMed1982

Structure of the Escherichia coli K2 capsular antigen. Stereochemical configuration of the glycerophosphate and distribution of galactopyranosyl and galactofuranosyl residues.

The Escherichia coli K2 capsular antigen is known to be composed of alpha-D-galactopyranosyl(1--2)glycerophosphate and alpha-D-galactofuranosyl(1--2)glycerophosphate units which are connected by phosphodiester bonds to C-4 of the galactopyranosyl and C-5 or C-6 of the galactofuranosyl moieties. In the present study the glycerophosphates were released by two different procedures and shown to have the sn-glycero-3-phosphate stereochemical configuration. In the first, the chain was fragmented by Smith degradation to glycerophosphothreitol from which the glycerophosphate was released by alkali hydrolysis. The structure-dependent low recovery of alpha-glycerophosphate (less than 10%) initiated the development of another degradative sequence which consisted of periodate oxidation, beta elimination, hydrazinolysis, and alkaline treatment. This way, approximately 90% of the glycerophosphate was released as sn-glycero-3-phosphate. beta elimination revealed in addition that most of the galactofuranosyl residues carry the phosphodiester bond at position 5. Separation by gel permeation chromatography and analysis of the fragments obtained by beta elimination showed that pyranosidic and furanosidic galactosyl residues alternate in the same chain and suggested the sequences Galf(p)GroP-(GalpGroP)n-Galf- and -GalfGroP-(GalpGroP)n-Galf-, where n is 6, 4, and 3, respectively.

Antigens↗
PubMed1975

Acylation of carnitine and glycerophosphate in suspensions of rat liver mitochondria at varying levels of palmitate and coenzyme A.

Rates of acylation of carnitine and glycerophosphate in suspensions of isolated rat liver mitochondria were measured at varying levels of palmitate and coenzyme A in the presence of ATP. Addition of glycerophosphate caused considerable reduction in carnitine acylation at low, but not at high palmitate levels. Glycerophosphate acylation was less reduced by added carnitine. These results can be explained by a lower Km(acyl-CoA) in glycerophosphate acylation than in carnitine acylation. High levels of free coenzyme A caused inhibition of carnitine acylation, while the inhibitory effect of glycerophosphate acylation was small. Competition between palmitate and acyl-CoA for binding sites on protein (e.g., albumine added to the mitochondrial suspensions) was indicated by stimulation of carnitine acylation by palmitate with palmityl-CoA added as substrate in the absence of ATP. Refeeding a carbohydrate-rich diet to previously fasted rats resulted in increased glycerophosphate acylation and decreased carnitine acylation in isolated liver mitochondria.

Acylation↗
PubMed1990

On the basic structure of poly(glycerophosphate) lipoteichoic acids.

Poly(glycerophosphate) lipoteichoic acids from 24 Gram-positive bacteria of the genera Bacillus, Enterococcus, Lactobacillus, Lactococcus, Listeria, Staphylococcus, and the streptococcal pyogenic and oral group were analyzed. The 1,3-linked poly(glycerophosphate) structure was proved by analysis of glycerol and glycerophosphates after acid and alkaline hydrolysis. Using the molar ratios of glycolipid to phosphorus (A) and phosphomonoester to phosphorus after periodate oxidation followed by hydrazinolysis (B) or beta-elimination (C), we show that all lipoteichoic acids contain a single unbranched poly(glycerophosphate) chain and that the chain is uniformly phosphodiester-linked to C-6 of the nonreducing hexopyranosyl residue of the glycolipid moiety. On some chains minor phosphate-containing substituents were detected whose structure remains to be clarified. The lipoteichoic acids of enterococci and listeria strains were separated by hydrophobic interaction chromatography into glycolipid- and phosphatidylglycolipid-containing molecular species. The phosphatidylglycolipid moieties were structurally characterized after liberation from lipoteichoic acids with moist acetic acid. After periodate oxidation of lipoteichoic acids beta-elimination released both phosphatidic acid and the poly(glycerophosphate) chain. This indicates together with the sequence analysis of the released phosphatidylglycolipid that the phosphatidyl residue is located at C-6 of the reducing hexosyl residue of the glycolipid moiety and the poly(glycerophosphate) chain at C-6 of the nonreducing one. Together with earlier observations these results complete the evidence for the structural and possibly biosynthetic relationship between lipoteichoic acids and glycerophosphoglycolipids.

Carbohydrate Sequence↗
PubMed1988

Rapid stimulation of liver palmitoyl-CoA synthetase, carnitine palmitoyltransferase and glycerophosphate acyltransferase compared to peroxisomal beta-oxidation and palmitoyl-CoA hydrolase in rats fed high-fat diets.

Key enzymes involved in oxidation and esterification of long-chain fatty acids were investigated in male rats fed different types and amounts of oil in their diet. A diet with 20% (w/w) fish oil, partially hydrogenated fish oil (PHFO) and partially hydrogenated soybean oil (PHSO) was shown to stimulate the mitochondrial and microsomal palmitoyl-CoA synthetase activity (EC 6.2.1.3) compared to soybean oil-fed animals after 1 week of feeding. Rapeseed oil had no effect. Partially hydrogenated oils in the diet resulted in significantly higher levels of mitochondrial glycerophosphate acyltransferase compared to unhydrogenated oils in the diet. Rats fed 20% (w/w) rapeseed oil had a decreased activity of this mitochondrial enzyme, whereas the microsomal glycerophosphate acyltransferase activity was stimulated to a comparable extent with 20% (w/w) rapeseed oil, fish oil or PHFO in the diet. Increasing the amount of PHFO (from 5 to 25% (w/w)) in the diet for 3 days led to increased mitochondrial and microsomal palmitoyl-CoA synthetase and microsomal glycerophosphate acyltransferase activities with 5% of this oil in the diet. The mitochondrial glycerophosphate acyltransferase was only marginally affected by increasing the oil dose. Administration of 20% (w/w) PHFO increased rapidly the mitochondrial and microsomal palmitoyl-CoA synthetase, carnitine palmitoyltransferase and microsomal glycerophosphate acyltransferase activities almost to their maximum value within 36 h. In contrast, the glycerophosphate acyltransferase and palmitoyl-CoA hydrolase (EC 3.1.2.2) activities of the mitochondrial fraction and the peroxisomal beta-oxidation reached their maximum activities after administration of the dietary oil for 6.5 days. This sequence of enzyme changes (a) is in accordance with the proposal that an increased cellular level of long-chain acyl-CoA species act as metabolic messages for induction of peroxisomal beta-oxidation and palmitoyl-CoA hydrolase, i.e., these enzymes are regulated by a substrate-induced mechanism, and (b) indicates that, with PHFO, a greater part of the activated fatty acids are directed from triacylglycerol esterification and hydrolysis towards oxidation in the mitochondria. It is also conceivable that the mitochondrial beta-oxidation is proceeding before the enhancement of peroxisomal beta-oxidation.

Acyltransferases↗
PubMed1991

Hexose metabolism in pancreatic islets. Glucose-induced and Ca(2+)-dependent activation of FAD-glycerophosphate dehydrogenase.

A rise in extracellular D-glucose concentration causes in pancreatic islets a preferential stimulation of aerobic, relative to total, glycolysis. The possible participation in such a phenomenon of a glucose-induced and Ca(2+)-dependent activation of FAD-glycerophosphate dehydrogenase was investigated. In islet homogenates, the activity of the mitochondrial and Ca(2+)-responsive FAD-glycerophosphate dehydrogenase was about two orders of magnitude lower than that of the cytosolic and Ca(2+)-insensitive NAD-glycerophosphate dehydrogenase. In islet mitochondria, Ca2+ increased the affinity of the FAD-glycerophosphate dehydrogenase for L-glycerol 3-phosphate, but did not affect the maximal reaction velocity. In the presence of 0.1 mM-L-glycerol 3-phosphate, the Ka for Ca2+ was close to 0.1 microM. When intact islets were preincubated in the presence of both D-glucose and Ca2+, the activity of FAD-glycerophosphate dehydrogenase measured in intact mitochondria incubated in the presence of 1.2 microM-Ca2+ was higher than that recorded under the same conditions in islets preincubated in the absence of D-glucose and/or Ca2+. These findings support the view that, in islets exposed to a high concentration of D-glucose, a Ca(2+)-induced activation of mitochondrial FAD-glycerophosphate dehydrogenase favours the transfer of reducing equivalents by the glycerol phosphate shuttle, and hence accounts, in part at least, for the preferential stimulation of aerobic glycolysis.

Animals↗