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PubMed1983

Serine: glyoxylate, alanine:glyoxylate, and glutamate:glyoxylate aminotransferase reactions in peroxisomes from spinach leaves.

Two different aminotransferases, that have glyoxylate as the amino acceptor, have specific activities of 1 to 2 mumol . min-1 . mg of protein-1 in the isolated peroxisomal fraction from spinach leaves. Their properties were evaluated after separation on a hydroxylapatite column. Both enzymes had a Km for glyoxylate of 0.15 mM and an amino acid Km of 2 to 3 mM. Reactions proceeded by a Ping Pong Bi Bi mechanism. Serine:glyoxylate aminotransferase was relatively specific for both substrates and could only be slightly reversed with 100 mM glycine, although the Ki of glycine was 33 mM. The glutamate:glyoxylate amino-transferase protein was equally active in catalyzing an alanine:glyoxylate aminotransferase reaction, but the reverse reactions with 100 mM glycine were hardly measureable, although the Ki (glycine) was 8.7 mM. Protection against hydroxylamine inhibition from reaction with pyridoxal phosphate was used to investigate the specificity of amino acid binding. Substrate amino acids protected at about the same concentration as their Km, while glycine protected at its Ki concentration. Thus, the nearly irreversible catalysis with glycine is not due to a failure to bind glycine. The significance of a peroxisomal alanine:glyoxylate aminotransferase activity has not been incorporated into schemes for the oxidative photosynthetic carbon cycle.

Alanine Transaminase↗

PubMed2000

Urinary oxalate, glycolate, glyoxylate, and citrate after acute intravenous administration of glyoxylate in rats.

BACKGROUND AND PURPOSE: Urinary oxalate plays an important role in the formation of calcium oxalate renal stones, and approximately 50% to 60% of urinary oxalate is derived from the endogenous metabolism of glyoxylate. Therefore, we measured urinary oxalate, glycolate, glyoxylate, and citrate concentrations after acute intravenous administration of various doses of glyoxylate in rats to study oxalate metabolism. MATERIALS AND METHODS: Male Wistar rats weighing approximately 200 g were divided into six groups of eight animals each. Anesthetized rats received glyoxylate (0, 1, 2, 5, 10, and 20 mg) intravenously. Urine specimens were collected before and every hour after each dose for 4 hours, and the concentrations of oxalate, glycolate, glyoxylate, and citrate were measured by capillary electrophoresis. RESULTS: Hourly oxalate excretion in the urine peaked at 1 hour after glyoxylate administration, and the peak concentration increased in a dose-dependent manner. Approximately 15% to 30% (mol/mol) of the dose was converted to oxalate within 4 hours and 2% to 4.6% was converted to glycolate. Urinary glyoxylate was not detectable before glyoxylate administration, but large doses resulted in a significant amount of glyoxylate (0.7%-2.3%) appearing in the urine, and the level peaked at 1 hour after administration. Urinary glycolate also peaked at 1 hour after administration of glyoxylate. The urinary citrate concentration generally decreased by 3% to 33% after each dose of glyoxylate, except that it increased slightly after the 20-mg dose. CONCLUSION: Administration of glyoxylate increased urinary oxalate and glycolate excretion in rats, supporting the importance of the glycolate-glyoxylate-oxalate pathway.

Animals↗

PubMed1980

Crystallization and characterization of human liver kynurenine--glyoxylate aminotransferase. Identity with alanine--glyoxylate aminotransferase and serine--pyruvate aminotransferase.

Kynurenine-glyoxylate aminotransferase, alanine-glyoxylate aminotransferase and serine-pyruvate aminotransferase were co-purified and crystallized as yellow cubes from human liver particulate fraction. The crystalline enzyme was homogeneous by the criteria of electrophoresis, isoelectric focusing, gel filtration, sucrose-density-gradient centrifugation and analytical ultracentrifugation. The molecular weight of the enzyme was calculated as approx. 90000, 89000 and 99000 by the use of gel filtration, analytical ultracentrifugation and sucrose-density-gradient centrifugation respectively, with two identical subunits. The enzyme has a s(20,w) value of 5.23S, an isoelectric point of 8.3 and a pH optimum between 9.0 and 9.5. The enzyme solution showed absorption maxima at 280 and 420nm. The enzyme catalysed transamination between several l-amino acids and pyruvate or glyoxylate. The order of effectiveness of amino acids was alanine>serine>glutamine>glutamate>methionine>kynurenine = phenylalanine = asparagine>valine>histidine>lysine>leucine>isoleucine>arginine>tyrosine = threonine>aspartate, with glyoxylate as amino acceptor. The enzyme was active with glyoxylate, oxaloacetate, hydroxypyruvate, pyruvate, 4-methylthio-2-oxobutyrate and 2-oxobutyrate, but showed little activity with phenylpyruvate, 2-oxoglutarate and 2-oxoadipate, with kynurenine as amino donor. Kynurenine-glyoxylate aminotransferase activity was competitively inhibited by the addition of l-alanine or l-serine. From these results we conclude that kynurenine-glyoxylate aminotransferase, alanine-glyoxylate aminotransferase and serine-pyruvate aminotransferase activities of human liver are catalysed by a single protein. Kinetic parameters for the kynurenine-glyoxylate aminotransferase, alanine-glyoxylate aminotransferase, serine-pyruvate aminotransferase and alanine-hydroxypyruvate aminotransferase reactions of the enzyme are presented.

Aged↗

PubMed2000

Localization of glyoxylate dehydrogenase and glyoxylate-complex molecules in the rat prefrontal cortex: enzymohistochemical and immunocytochemical study.

Glyoxylic acid is synthesized and catabolized in cells of vertebrates; several pathways have been described. In previous papers, we have demonstrated the localization in some areas of the rat cerebral cortex both of beta-NAD-dependent glyoxylate dehydrogenase (glyoDH), using an enzymohistochemical method, and of glyoxylate-complex molecules, using immunocytochemical procedures. In this study we have applied these two techniques in various areas of the prefrontal cortex with different histological cytoarchitecture. GlyoDH has been located in most neurons, in some glial cells, and in capillary wall structures in all cortical layers of all areas of the rat prefrontal cortex. Antibodies against glyoxylate-complex molecules showed positive immunoreactivity in scattered neurons, mostly of multipolar or stellate appearance, from layers III, IV, and V in the medial precentral area, but not in cortical areas 24, 25, or 32 of the prefrontal cortex. Immunoreaction was found in the periphery of neuronal perikarya and in some of their processes. These results demonstrate the existence of a particular area-dependent neuronal cortical system, of specific but uncertain function, related to glyoxylic acid and/or glyoxylate compounds. At the electron microscope level, positive reaction was associated with synaptic sites, axonal filaments, glial cells, and several components of the blood-brain barrier. These localizations suggest the involvement of glyoxylate derivatives in synaptic functioning and also in glial cell functions.

Aldehyde Oxidoreductases↗

PubMedDate not supplied

Studies on the nitroso-glyoxylate reaction. Relative hydroxamic acid production by glyoxylate, pyruvate, and formaldehyde in reactions with 4-nitrosobiphenyl.

The pH rate profiles for the reactions of 4-nitrosobiphenyl with three carbonyl substrates in aqueous buffers were determined by use of chromatographic and spectrophotometric methods. Glyoxylate and formaldehyde caused the conversion of 4-nitrosobiphenyl to N-(4-biphenyl)-formohydroxamic acid, while pyruvate resulted in the production of N-(4-biphenyl)acetohydroxamic acid. The dramatic effect of pH on the kinetics of these reactions provided considerable information concerning the nature of these reactions. The reactions with pyruvate and formaldehyde displayed similar pH rate profiles and were significant only at acidic pH. Glyoxylate displayed a pH rate profile that differed markedly from those of pyruvate and formaldehyde as the pH was increased beyond 2.0. The ability of glyoxylate to convert 4-nitrosobiphenyl to the hydroxamic acid increased rapidly in the pH range 2.0-4.0, above which the pH dependency was constant. This biphasic appearance of the pH rate profile was unique to glyoxylate, since the reactions of pyruvate and formaldehyde became extremely slow as solution neutrality was approached. A second substrate, 4-chloronitrosobenzene, displayed similar pH rate profiles in its reactions with these carbonyl substrates. For 4-nitrosobiphenyl, hydroxamic acid formation by glyoxylate was 10(4) times faster than that by pyruvate at neutral pH, but only about 3-fold faster at pH 1.0. The appearance of the pH rate profile for glyoxylate suggested that this alpha-oxo acid reacts with nitrosoarenes at neutrality via a pathway that is insignificant for pyruvate or formaldehyde. Thus, the nitroso-glyoxylate reaction is unique to this alpha-oxo acid under physiological pH conditions.(ABSTRACT TRUNCATED AT 250 WORDS)

Biphenyl Compounds↗

PubMed1972

The subcellular distribution of rat liver L-alanine-glyoxylate aminotransferase in relation to a pathway for glucose formation involving glyoxylate.

1. The distribution of l-alanine-glyoxylate aminotransferase activity between subcellular fractions prepared from rat liver homogenates was investigated. The greater part of the homogenate activity (about 80%) was recovered in the ;total-particles' fraction sedimented by high-speed centrifugation and the remainder in the cytosol fraction. 2. Subfractionation of the particles by differential sedimentation and on sucrose density gradients revealed a specific association between the aminotransferase and the mitochondrial enzymes glutamate dehydrogenase and rhodanese. 3. The aminotransferase activities in the cytosol and the mitochondria are due to isoenzymes. The solubilized mitochondrial enzyme has a pH optimum of 8.6, an apparent K(m) of 0.24mm with respect to glyoxylate and is inhibited by glyoxylate at concentrations above 5mm. The cytosol aminotransferase shows no distinct pH optimum (over the range 7.0-9.0) and has an apparent K(m) of 1.11mm with respect to glyoxylate; there is no evidence of inhibition by glyoxylate. 4. The mitochondrial location of the bulk of the rat liver l-alanine-glyoxylate aminotransferase activity is discussed in relation to a pathway for gluconeogenesis involving glyoxylate.

Acid Phosphatase↗

PubMed1997

Glyoxylate oxidoreductase activity and glyoxylate-like molecules in the motor, somatosensory, cyngulate and olfactory areas of the rat frontoparietal cortex. Histoenzymological and immunohistochemical study.

In the present paper the presence of glyoxylate-oxidoreductase (GOR, GLYO-DH) activity and glyoxylate-like molecules has been investigated in several areas of the rat frontoparietal cortex-motor, somatosensory, cyngulate and olfactory areas-, using the histoenzymological and immunocytochemical methods. Antibodies against glyoxylate-like molecules have been obtained using a glyoxylate-BSA conjugate as immunogen. GOR activity as well as immunostaining for glyoxylate-like molecules were observed in the periphery of the perikaryon and neuronal processes of scattered neurons in the above mentioned cortical areas. At the electron microscopic level positive immunoreaction was found associated to synaptic vesicles in axon terminals, and also within glial cells. These findings reveal both the presence of glyoxylate-like molecules and glyoxylate metabolism in neurons of the motor, somatosensory, cyngulate and olfactory areas of the rat frontoparietal cortex. The presence of such molecules associated to synaptic vesicles within the axon terminals suggest the possible involvement of these molecules in some type of neurotransmission.

Alcohol Oxidoreductases↗

PubMed1986

Purification and characterization of a novel NADPH(NADH)-dependent glyoxylate reductase from spinach leaves. Comparison of immunological properties of leaf glyoxylate reductase and hydroxypyruvate reductase.

A novel reductase displaying high specificity for glyoxylate and NADPH was purified 3343-fold from spinach leaves. The enzyme was found to be an oligomer of about 125 kDa, composed of four equal subunits of 33 kDa each. A Km for glyoxylate was about 14-fold lower with NADPH than with NADH (0.085 and 1.10 mM respectively), but the maximal activity, 210 mumol/min per mg of protein, was similar with either cofactor. Km values for NADPH and NADH were 3 and 150 microM respectively. Optimal rates with either NADPH or NADH were found in the pH range 6.5-7.4. The enzyme also showed some reactivity towards hydroxypyruvate with rates less than 2% of those observed for glyoxylate. Results of immunological studies, using antibodies prepared against either glyoxylate reductase or spinach peroxisomal hydroxypyruvate reductase, suggested substantial differences in molecular structure of the two proteins. The high rates of NADPH(NADH)-glyoxylate reductase in crude leaf extracts of spinach, wheat and soya bean (30-45 mumol/h per mg of chlorophyll) and its strong affinity for glyoxylate suggest that the enzyme may be an important side component of photorespiration in vivo. In leaves of nitrogen-fixing legumes, this reductase may also be involved in ureide breakdown, utilizing the glyoxylate produced during allantoate metabolism.

Alcohol Oxidoreductases↗

PubMed1995

Electron transport phosphorylation driven by glyoxylate respiration with hydrogen as electron donor in membrane vesicles of a glyoxylate-fermenting bacterium.

The syntrophically glycolate-fermenting bacterium in the methanogenic binary coculture FlGlyM was isolated in pure culture (strain FlGlyR) with glyoxylate as sole substrate. This strain disproportionated 12 glyoxylate to 7 glycolate, 10 CO2, and 3 hydrogen. Glyoxylate was oxidized via the malyl-CoA pathway. All enzymes of this pathway, i.e. malyl-CoA lyase/malate: CoA ligase, malic enzyme, and pyruvate synthase, were demonstrated in cell-free extracts. Glycolate dehydrogenase, hydrogenase, and ATPase, as well as menaquinones as potential electron carriers, were present in the membranes. Everted membrane vesicles catalyzed hydrogen-dependent glyoxylate reduction to glycolate [86-207 nmol min-1 (mg protein)-1] coupled to ATP synthesis from ADP and Pi [38-82 nmol min-1 (mg protein)-1)]. ATP synthesis was abolished entirely by protonophores or ATPase inhibitors (up to 98 and 94% inhibition, respectively) indicating the involvement of proton-motive force in an electron transport phosphorylation driven by a new glyoxylate respiration with hydrogen as electron donor. Measured reaction rates in vesicle preparations revealed a stoichiometry of ATP formation of 0.2-0.5 ATP per glyoxylate reduced.

Adenosine Triphosphate↗

PubMed1985

Characteristics of alanine: glyoxylate aminotransferase from Saccharomyces cerevisiae, a regulatory enzyme in the glyoxylate pathway of glycine and serine biosynthesis from tricarboxylic acid-cycle intermediates.

Alanine: glyoxylate aminotransferase (EC 2.6.1.44), which is involved in the glyoxylate pathway of glycine and serine biosynthesis from tricarboxylic acid-cycle intermediates in Saccharomyces cerevisiae, was highly purified and characterized. The enzyme had Mr about 80 000, with two identical subunits. It was highly specific for L-alanine and glyoxylate and contained pyridoxal 5'-phosphate as cofactor. The apparent Km values were 2.1 mM and 0.7 mM for L-alanine and glyoxylate respectively. The activity was low (10 nmol/min per mg of protein) with glucose as sole carbon source, but was remarkably high with ethanol or acetate as carbon source (930 and 430 nmol/min per mg respectively). The transamination of glyoxylate is mainly catalysed by this enzyme in ethanol-grown cells. When glucose-grown cells were incubated in medium containing ethanol as sole carbon source, the activity markedly increased, and the increase was completely blocked by cycloheximide, suggesting that the enzyme is synthesized de novo during the incubation period. Similarity in the amino acid composition was observed, but immunological cross-reactivity was not observed among alanine: glyoxylate aminotransferases from yeast and vertebrate liver.

Alanine Transaminase↗

PubMed1992

On the possibility of involvement of glutamate:glyoxylate and serine:glyoxylate aminotransferases from rye (Secale cereale L.) seedlings in the metabolism of tetrapyrrole compounds.

The activity of highly purified L-serine:glyoxylate aminotransferase (SGAT, EC 2.6.1.45) from rye seedlings was inhibited competitively by 5-aminolevulinate (ALA, Ki = 5 mM) SGAT was activated by hematin. Protoporphyrin IX and hematin inhibited irreversibly the activity of highly purified glutamate:glyoxylate aminotransferase (GGAT, EC 2.6.1.2) from rye seedlings. SGAT was found to catalyse transamination between ALA and hydroxypyruvate, whereas GGAT that between ALA and 2-oxoglutarate or pyruvate. It is suggested that SGAT is involved in the process of degradation of the excess ALA which has not been incorporated into porphyrin compounds.

Glyoxylates↗

PubMed1970