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At least 865 records · Page 48Linked to original sources
PubMed1977

Effect of some glycolytic intermediates and palmitoyl-CoA on alpha-glycerophosphate dehydrogenase in mitochondria isolated from liver of triiodothyronine-treated rats.

alpha-Glycerophosphate dehydrogenase (EC 1.1.99.5) in mitochondria from liver of the triiodothyronine-treated rats is competitively inhibited by phosphoenolpyruvate, glyceraldehyde 3-phosphate and 3-phosphoglycerate, the apparent Ki values for phosphoenolpyruvate being 0.76 mM at pH 7.0, 1.7 mM at pH 7.4 and 3.5 mM at pH 7.7. The apparent Ki values for glyceraldehyde 3-phosphate and 3-phosphoglycerate are also pH-dependent. Other glycolytic intermediates, such as 2-phosphoglycerate, 2,3-diphosphoglycerate, pyruvate, glucose 6-phosphate, fructose 6-phosphate and fructose 1,6-diphosphate did not alter significantly alpha-glycerophosphate dehydrogenase activity. Palmitoyl-CoA is a competitive inhibitor of this enzyme, with Ki value of about 30 micron.

Acyl Coenzyme A↗
PubMed1993

Arrangement of substrates at the active site of yeast phosphoglycerate kinase. Effect of sulfate ion.

beta, gamma-Bidentate CrATP, a stable exchange-inert metal-nucleotide analog, was used as a probe of the conformation of the substrates at the active site of yeast phosphoglycerate kinase (PGK). The paramagnetic effects of Cr3+ on the longitudinal relaxation rates (1/T1p) of the 1H, 31P, and 13C nuclei of 3-phospho-D-glycerate (3PGA) were examined to determine the distances between enzyme-bound CrATP and the nuclei of 3PGA in the ternary PGK.CrATP.3PGA complex. Kinetic studies indicated that Ki(CrATP) was dependent on the concentration of 3PGA that was abolished in the presence of activator sulfate ion. Similarly, NMR studies showed that the environment of CrATP bound at the active site was altered by the presence of sulfate ion. The determined metal-to-nucleus distances show the close proximity of the substrates at the active site of PGK, which is consistent with a hinge-bending mechanism of the enzyme for bringing the two substrates together. Additionally, the presence of an activating concentration of sulfate was observed to cause significant changes in both the relative Cr(3+)-to-3PGA distances and the overall conformation of 3PGA when compared to the findings in the absence of sulfate. This is consistent with the active site being in a "less closed" configuration when sulfate is present. Under both conditions, models can be constructed that allow for direct transfer of a phosphoryl group between the bound substrates.

Adenosine Triphosphate↗
PubMed1993

Kinetic mechanism and regulation of ADP-glucose pyrophosphorylase from barley (Hordeum vulgare) leaves.

Barley (Hordeum vulgare, cv. Bomi) leaf ADP-glucose pyrophosphorylase (AGP) was purified to near-homogeneity, using ammonium sulfate fractionation and heat treatment as well as ion exchange, hydrophobic, and dye-ligand chromatography. The enzyme was found to be composed of two subunit types of 51 and 54 kDa, which were recognized by the respective rabbit antibodies against the small and/or large subunit of spinach leaf AGP. Substrate kinetics and product inhibition studies, carried out in the direction of ADP-glucose synthesis, suggested a sequential Iso Ordered Bi Bi kinetic mechanism for the enzyme. In addition, inhibition patterns with CrATP, a dead-end inhibitor of ATP-utilizing enzymes, were consistent with ATP (synthesis reaction) and ADP-glucose (pyrophosphorolysis reaction) binding first to different free forms of the enzyme. The AGP was potently activated by 3-phosphoglycerate (PGA) (K alpha of 5 microM) and inhibited by orthophosphate (P(i)), with the ratio of the two effectors playing a major role in modulating AGP activity. At low [PGA]/[P(i)] ratios, P(i) could reverse the activating effect of PGA. However, at the [PGA]/[Pi] ratios of 1.4, or higher, some activating effect of P(i) in the presence of PGA was observed. PGA decreased the Km values for all substrates of AGP (in both the synthesis and pyrophosphorolysis directions). Properties of the barley leaf AGP are compared to those of AGP from barley seed endosperm, which is insensitive to PGA/P(i) regulation.

Adenosine Triphosphate↗
PubMed1995

Detection of primary hyperoxaluria type 2 (L-glyceric aciduria) in patients with maintained renal function or end-stage renal failure.

Primary hyperoxaluria (PH) type 1 and type 2 are autosomal recessive defects of oxalate metabolism resulting from glyoxylate accumulation which occurs by two distinct pathways. PH1 is associated to glycolic aciduria; PH2 to L-glyceric aciduria. Because hyperoxaluria leads to nephrolithiasis or nephrocalcinosis in both, they can be differentiated only through detection of the associated acidurias. However, glycolate and L-glycerate assays are not widely available and, in the setting of ESRF, diagnosis is hampered by a number of misleading events. At any stage of the disease diagnosis is crucial because there are differences between the two forms in clinical behaviour, long-term prognosis, and treatment. In this paper we outline diagnostic criteria for identification of PH2 in two patients, one with maintained renal function and one with ESRF on CPD, based on the use of a novel HPLC assay of L-glycerate in different body fluids. With the routine application of this procedure PH2 has been identified in two of 23 patients fulfilling criteria for diagnosis of PH. This suggests that the type 2 variant of PH may occur more frequently than so far suspected, and should be tested for even in the setting of ESRF.

Child, Preschool↗
PubMedDate not supplied

[Study of yeast phosphoglycerate kinase by electron paramagnetic resonance. 1. Modification of protein SH-group by spin labels. Conformational changes of enzyme].

The conditions for modifications of a single SH-group of phosphoglycerate kinase from yeast by maleimid spin label and the mercury-containing spin labels were defined. The time course of immobilization of mercury containing paramagnetic radicals was obtained. Based on changes in EPR spectra we calculated dissociation constants for complexes of phosphoglycerate kinase with 3-phosphoglycerate and sulfate ions. Distinct substances were shown to induce different changes in enzyme conformation. It was concluded that approach of enzyme domains is caused by the binding of 3-phosphoglycerate-a specific substrate of this enzyme.

Electron Spin Resonance Spectroscopy↗