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{"work":{"id":27845765,"created_at":"2016-08-17T16:34:16.708-07:00","from_world_paper_id":156665373,"updated_at":"2025-01-10T13:10:44.092-08:00","_data":{"ai_abstract":"The phosphoenolpyruvate carboxykinase (PEPCK) enzyme from the epimastigote form of Trypanosoma cruzi was purified and characterized. The enzyme exhibits strict specificity for adenine nucleotides and requires Mn2+ ions for activity, indicating its regulatory role in the amino acid catabolism of the parasite. Kinetic analyses revealed hyperbolic kinetics for carboxylation reactions and biphasic responses to Mg-ATP in decarboxylation reactions, suggesting complex regulatory mechanisms. These findings deepen the understanding of carbohydrate metabolism in T. cruzi, which utilizes an incomplete catabolism process even in aerobic conditions.","publication_date":"1987,,","publication_name":"Archives of Biochemistry and Biophysics"},"document_type":"paper","pre_hit_view_count_baseline":null,"quality":"high","language":"en","title":"The phosphoenolpyruvate carboxykinase of Trypanosoma (Schizotrypanum) cruzi epimastigotes: Molecular, kinetic, and regulatory properties","broadcastable":false,"draft":null,"has_indexable_attachment":true,"indexable":true}}["work"]; window.loswp.workCoauthors = [52140311]; window.loswp.locale = "en"; window.loswp.countryCode = "SG"; window.loswp.cwvAbTestBucket = ""; window.loswp.designVariant = "ds_vanilla"; window.loswp.fullPageMobileSutdModalVariant = "full_page_mobile_sutd_modal"; window.loswp.useOptimizedScribd4genScript = false; window.loginModal = {}; window.loginModal.appleClientId = 'edu.academia.applesignon';</script><script defer="" src="https://accounts.google.com/gsi/client"></script><div class="ds-loswp-container"><div class="ds-work-card--grid-container"><div class="ds-work-card--container js-loswp-work-card"><div class="ds-work-card--cover"><div class="ds-work-cover--wrapper"><div class="ds-work-cover--container"><button class="ds-work-cover--clickable js-swp-download-button" data-signup-modal="{"location":"swp-splash-paper-cover","attachmentId":48130344,"attachmentType":"pdf"}"><img alt="First page of “The phosphoenolpyruvate carboxykinase of Trypanosoma (Schizotrypanum) cruzi epimastigotes: Molecular, kinetic, and regulatory properties”" class="ds-work-cover--cover-thumbnail" src="https://0.academia-photos.com/attachment_thumbnails/48130344/mini_magick20190204-28517-1ncye2g.png?1549341919" /><img alt="PDF Icon" class="ds-work-cover--file-icon" src="//a.academia-assets.com/images/single_work_splash/adobe_icon.svg" /><div class="ds-work-cover--hover-container"><span class="material-symbols-outlined" style="font-size: 20px" translate="no">download</span><p>Download Free PDF</p></div><div class="ds-work-cover--ribbon-container">Download Free PDF</div><div class="ds-work-cover--ribbon-triangle"></div></button></div></div></div><div class="ds-work-card--work-information"><h1 class="ds-work-card--work-title">The phosphoenolpyruvate carboxykinase of Trypanosoma (Schizotrypanum) cruzi epimastigotes: Molecular, kinetic, and regulatory properties</h1><div class="ds-work-card--work-authors ds-work-card--detail"><a class="ds-work-card--author js-wsj-grid-card-author ds2-5-body-md ds2-5-body-link" data-author-id="52140311" href="https://independent.academia.edu/JulioUrbina7"><img alt="Profile image of Julio Urbina" class="ds-work-card--author-avatar" src="https://0.academia-photos.com/52140311/170891052/160878954/s65_julio.urbina.png" />Julio Urbina</a></div><div class="ds-work-card--detail"><p class="ds-work-card--detail ds2-5-body-sm">1987, Archives of Biochemistry and Biophysics</p><div class="ds-work-card--work-metadata"><div class="ds-work-card--work-metadata__stat"><span class="material-symbols-outlined" style="font-size: 20px" translate="no">visibility</span><p class="ds2-5-body-sm" id="work-metadata-view-count">…</p></div><div class="ds-work-card--work-metadata__stat"><span class="material-symbols-outlined" style="font-size: 20px" translate="no">description</span><p class="ds2-5-body-sm">10 pages</p></div><div class="ds-work-card--work-metadata__stat"><span class="material-symbols-outlined" style="font-size: 20px" translate="no">link</span><p class="ds2-5-body-sm">1 file</p></div></div><script>(async () => { const workId = 27845765; const worksViewsPath = "/v0/works/views?subdomain_param=api&work_ids%5B%5D=27845765"; const getWorkViews = async (workId) => { const response = await fetch(worksViewsPath); if (!response.ok) { throw new Error('Failed to load work views'); } const data = await response.json(); return data.views[workId]; }; // Get the view count for the work - we send this immediately rather than waiting for // the DOM to load, so it can be available as soon as possible (but without holding up // the backend or other resource requests, because it's a bit expensive and not critical). const viewCount = await getWorkViews(workId); const updateViewCount = (viewCount) => { try { const viewCountNumber = parseInt(viewCount, 10); if (viewCountNumber === 0) { // Remove the whole views element if there are zero views. document.getElementById('work-metadata-view-count')?.parentNode?.remove(); return; } const commaizedViewCount = viewCountNumber.toLocaleString(); const viewCountBody = document.getElementById('work-metadata-view-count'); if (!viewCountBody) { throw new Error('Failed to find work views element'); } viewCountBody.textContent = `${commaizedViewCount} views`; } catch (error) { // Remove the whole views element if there was some issue parsing. document.getElementById('work-metadata-view-count')?.parentNode?.remove(); throw new Error(`Failed to parse view count: ${viewCount}`, error); } }; // If the DOM is still loading, wait for it to be ready before updating the view count. if (document.readyState === "loading") { document.addEventListener('DOMContentLoaded', () => { updateViewCount(viewCount); }); // Otherwise, just update it immediately. } else { updateViewCount(viewCount); } })();</script></div><p class="ds-work-card--detail ds2-5-body-md">AI-generated Abstract</p><p class="ds-work-card--work-abstract ds-work-card--detail ds2-5-body-md">The phosphoenolpyruvate carboxykinase (PEPCK) enzyme from the epimastigote form of Trypanosoma cruzi was purified and characterized. The enzyme exhibits strict specificity for adenine nucleotides and requires Mn2+ ions for activity, indicating its regulatory role in the amino acid catabolism of the parasite. Kinetic analyses revealed hyperbolic kinetics for carboxylation reactions and biphasic responses to Mg-ATP in decarboxylation reactions, suggesting complex regulatory mechanisms. These findings deepen the understanding of carbohydrate metabolism in T. cruzi, which utilizes an incomplete catabolism process even in aerobic conditions.</p><div class="ds-work-card--button-container"><button class="ds2-5-button js-swp-download-button" data-signup-modal="{"location":"continue-reading-button--work-card","attachmentId":48130344,"attachmentType":"pdf","workUrl":"https://www.academia.edu/27845765/The_phosphoenolpyruvate_carboxykinase_of_Trypanosoma_Schizotrypanum_cruzi_epimastigotes_Molecular_kinetic_and_regulatory_properties"}">See full PDF</button><button class="ds2-5-button ds2-5-button--secondary js-swp-download-button" data-signup-modal="{"location":"download-pdf-button--work-card","attachmentId":48130344,"attachmentType":"pdf","workUrl":"https://www.academia.edu/27845765/The_phosphoenolpyruvate_carboxykinase_of_Trypanosoma_Schizotrypanum_cruzi_epimastigotes_Molecular_kinetic_and_regulatory_properties"}"><span class="material-symbols-outlined" style="font-size: 20px" translate="no">download</span>Download PDF</button></div></div></div></div><div data-auto_select="false" data-client_id="331998490334-rsn3chp12mbkiqhl6e7lu2q0mlbu0f1b" data-doc_id="48130344" data-landing_url="https://www.academia.edu/27845765/The_phosphoenolpyruvate_carboxykinase_of_Trypanosoma_Schizotrypanum_cruzi_epimastigotes_Molecular_kinetic_and_regulatory_properties" data-login_uri="https://www.academia.edu/registrations/google_one_tap" data-moment_callback="onGoogleOneTapEvent" id="g_id_onload"></div><div class="ds-top-related-works--grid-container"><div class="ds-related-content--container ds-top-related-works--container"><h2 class="ds-related-content--heading">Related papers</h2><div class="ds-related-work--container js-wsj-grid-card" data-collection-position="0" data-entity-id="27845820" data-sort-order="default"><a class="ds-related-work--title js-wsj-grid-card-title ds2-5-body-md ds2-5-body-link" href="https://www.academia.edu/27845820/Regulation_of_energy_metabolism_in_Trypanosoma_schizotrypanum_cruzi_epimastigotes_I_Hexokinase_and_phosphofructokinase">Regulation of energy metabolism in Trypanosoma (schizotrypanum) cruzi epimastigotes, I. Hexokinase and phosphofructokinase</a><div class="ds-related-work--metadata"><a class="js-wsj-grid-card-author ds2-5-body-sm ds2-5-body-link" data-author-id="52140311" href="https://independent.academia.edu/JulioUrbina7">Julio Urbina</a></div><p class="ds-related-work--metadata ds2-5-body-xs">Molecular and Biochemical Parasitology, 1984</p><p class="ds-related-work--abstract ds2-5-body-sm">Hexokinase (ATP: hexose 6-phosphotransferase, E.C. 2.7.1.1) and phosphofructokinase (ATP: fructose-6-phosphate 1-phosphotransferase, E.C.2.7.1.11), two key regulatory enzymes of the glycolytic pathway in vertebrate cells, have been isolated and partially purified from Trypanosoma (Schizotrypanum) cruzi epimastigotes. Both enzymes are associated with particles sedimentable at 105 000 X gay for 1 h and have a high degree of latency; they can be solubilized by sonication. Hexokinase catalyses the phosphorylation of a series of monosaccharides at the following relative rates: D-glucose (100) =, D-fructose . Very little or no phosphorylating activity was found for D-galactose, N-acetyl-2-amino-v-glucose or l-a-methyl-v-glucose. D-Glucose phosphorylation at fixed ATP concentration follows simple Michaelis-Menten kinetics with Krn = 40 laM and Vma x = 440 nmol rain-' mg -1 protein. D-Mannose, 2-deoxy-D-glucose and N-acetyl-2amino-D-glucose act as competitive inhibitors of glucose phophorylation, suggesting a single kinase.</p><div class="ds-related-work--ctas"><button class="ds2-5-text-link ds2-5-text-link--inline js-swp-download-button" data-signup-modal="{"location":"wsj-grid-card-download-pdf-modal","work_title":"Regulation of energy metabolism in Trypanosoma (schizotrypanum) cruzi epimastigotes, I. Hexokinase and phosphofructokinase","attachmentId":48130382,"attachmentType":"pdf","work_url":"https://www.academia.edu/27845820/Regulation_of_energy_metabolism_in_Trypanosoma_schizotrypanum_cruzi_epimastigotes_I_Hexokinase_and_phosphofructokinase","alternativeTracking":true}"><span class="material-symbols-outlined" style="font-size: 18px" translate="no">download</span><span class="ds2-5-text-link__content">Download free PDF</span></button><a class="ds2-5-text-link ds2-5-text-link--inline js-wsj-grid-card-view-pdf" href="https://www.academia.edu/27845820/Regulation_of_energy_metabolism_in_Trypanosoma_schizotrypanum_cruzi_epimastigotes_I_Hexokinase_and_phosphofructokinase"><span class="ds2-5-text-link__content">View PDF</span><span class="material-symbols-outlined" style="font-size: 18px" translate="no">chevron_right</span></a></div></div><div class="ds-related-work--container js-wsj-grid-card" data-collection-position="1" data-entity-id="18378557" data-sort-order="default"><a class="ds-related-work--title js-wsj-grid-card-title ds2-5-body-md ds2-5-body-link" href="https://www.academia.edu/18378557/Phosphoenolpyruvate_carboxykinase_from_Trypanosoma_cruzi_Purification_and_physicochemical_and_kinetic_properties">Phosphoenolpyruvate carboxykinase from Trypanosoma cruzi. Purification and physicochemical and kinetic properties</a><div class="ds-related-work--metadata"><a class="js-wsj-grid-card-author ds2-5-body-sm ds2-5-body-link" data-author-id="38713547" href="https://independent.academia.edu/Joaqu%C3%ADnCannata">Joaquín Cannata</a><span>, </span><a class="js-wsj-grid-card-author ds2-5-body-sm ds2-5-body-link" data-author-id="38375749" href="https://independent.academia.edu/CoraCymeryng">Cora Cymeryng</a></div><p class="ds-related-work--metadata ds2-5-body-xs">Molecular and Biochemical Parasitology, 1995</p><p class="ds-related-work--abstract ds2-5-body-sm">Phospho enolpyruvate carboxykinase (PEPCK) has been purified to homogeneity from epimastigotes of the Tul 0 strain of Trypanosoma cruzi. The physicochemical parameters determined allowed the calculation of an average molecular mass of 120 kDa; the subunit molecular mass, about 61 kDa, is in good agreement with the value of 58.6 kDa recently determined from the sequence by Sommer et al. (FEBS Lett. 359 (1994) 125-129). The PEPCK from T. cruzi presented, in addition to its molecular mass, typical properties of other ATP-linked PEPCKs, namely strict specificity for ADP in the carboxylation reaction and lower specificity in the decarboxylation and exchange reactions, and synergistic activation by CdCl2 or MgCl2 when added in addition to MnCl2. The enzyme presented hysteretic behaviour, shown by a lag period in the carboxylation reaction, which was affected by dilution and preincubation. The decarboxylation reaction catalyzed by the T. cruzi PEPCK was not inhibited by excess of ATP-Mn. The apparent Km values for the carboxylation reaction, including the low value for PEP (0.035 mM) are compatible with an important role of PEPCK, as suggested by previous NMR experiments, on the CO2 fixation in vivo which leads to succinate excretion during aerobic fermentation of glucose.</p><div class="ds-related-work--ctas"><button class="ds2-5-text-link ds2-5-text-link--inline js-swp-download-button" data-signup-modal="{"location":"wsj-grid-card-download-pdf-modal","work_title":"Phosphoenolpyruvate carboxykinase from Trypanosoma cruzi. Purification and physicochemical and kinetic properties","attachmentId":42173633,"attachmentType":"pdf","work_url":"https://www.academia.edu/18378557/Phosphoenolpyruvate_carboxykinase_from_Trypanosoma_cruzi_Purification_and_physicochemical_and_kinetic_properties","alternativeTracking":true}"><span class="material-symbols-outlined" style="font-size: 18px" translate="no">download</span><span class="ds2-5-text-link__content">Download free PDF</span></button><a class="ds2-5-text-link ds2-5-text-link--inline js-wsj-grid-card-view-pdf" href="https://www.academia.edu/18378557/Phosphoenolpyruvate_carboxykinase_from_Trypanosoma_cruzi_Purification_and_physicochemical_and_kinetic_properties"><span class="ds2-5-text-link__content">View PDF</span><span class="material-symbols-outlined" style="font-size: 18px" translate="no">chevron_right</span></a></div></div><div class="ds-related-work--container js-wsj-grid-card" data-collection-position="2" data-entity-id="27845768" data-sort-order="default"><a class="ds-related-work--title js-wsj-grid-card-title ds2-5-body-md ds2-5-body-link" href="https://www.academia.edu/27845768/Trypanosoma_cruzi_phospho_enol_pyruvate_carboxykinase_ATP_dependent_transition_metal_ion_requirement_for_activity_and_sulfhydryl_group_reactivity">Trypanosoma cruzi phospho enol pyruvate carboxykinase (ATP-dependent) : transition metal ion requirement for activity and sulfhydryl group reactivity</a><div class="ds-related-work--metadata"><a class="js-wsj-grid-card-author ds2-5-body-sm ds2-5-body-link" data-author-id="52140311" href="https://independent.academia.edu/JulioUrbina7">Julio Urbina</a></div><p class="ds-related-work--metadata ds2-5-body-xs">Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology, 1996</p><p class="ds-related-work--abstract ds2-5-body-sm">We studied the transition metal ion requirements for activity and sulfhydryl group reactivity in phosphoenolpyruvate carboxykinase (PEP-carboxykinase; ATP:oxaloacetate carboxylase (transphosphorylating), EC 4.1.1.49), a key enzyme in the energy metabolism of the protozoan parasite Trypanosoma (Schizotrypanum) cruzi. As for other PEP-carboxykinases this enzyme has a strict requirement of transition metal ions for activity, even in the presence of excess Mg 2+ ions for the carboxylation reaction; the order of effectiveness of these ions as enzyme activators was: Co2+> Mn2+> Cd2+> Ni 2+ >> Fe2+> VO 2+, while Zn 2+ and Ca 2+ had no activating effects. When we investigated the effect of varying the type or concentration of the transition metal ions on the kinetic parameters of the enzyme the results suggested that the stimulatory effects of the transition metal center were mostly associated with the activation of the relatively inert CO 2 substrate. The inhibitory effects of 3-mercaptopicolinic acid (3MP) on the enzyme were found to depend on the transition metal ion activator: for the Mn 2 +-activated enzyme the inhibition was purely non-competitive (Kii = Kis) towards all substrates, while for the CoZ+-activated enzyme the inhibitor was much less effective, produced a mixed-type inhibition and affected differentially the interaction of the enzyme with its substrates. The modification of a single, highly reactive, cysteine per enzyme molecule by 5,5'-dithiobis(2-nitrobenzoate) (DTNB) lead to an almost complete inhibition of MnZ+-activated T. cruzi PEP-carboxykinase; however, in contrast with the results of previous studies in vertebrate and yeast enzymes, the substrate ADP slowed the chemical modification and enzyme inactivation but did not prevent it. PEP and HCO 3 had no significant effect on the rate or extent of the enzyme inactivation. The kinetics of the enzyme inactivation by DTNB was also dependent on the transition metal activator, being much slower for the C02+-activated enzyme than for its Mn 2+-activated counterpart. When the bulkier but more hydrophobic reagent N-(7-dimethylamino-4methylcoumarinyl)maleimide (DACM) was used the enzyme was slowly and incompletely inactivated in the presence of Mn 2+ and ADP afforded almost complete protection from inactivation; in the presence of Co 2+ the enzyme was completely resistant to inactivation. Taken together, our results indicate that the parasite enzyme has a specific requirement of transition metal ions for activity and that they modulate the reactivity of a single, essential thiol group, different from the hyperreactive cysteines present in vertebrate or yeast enzymes.</p><div class="ds-related-work--ctas"><button class="ds2-5-text-link ds2-5-text-link--inline js-swp-download-button" data-signup-modal="{"location":"wsj-grid-card-download-pdf-modal","work_title":"Trypanosoma cruzi phospho enol pyruvate carboxykinase (ATP-dependent) : transition metal ion requirement for activity and sulfhydryl group reactivity","attachmentId":48130319,"attachmentType":"pdf","work_url":"https://www.academia.edu/27845768/Trypanosoma_cruzi_phospho_enol_pyruvate_carboxykinase_ATP_dependent_transition_metal_ion_requirement_for_activity_and_sulfhydryl_group_reactivity","alternativeTracking":true}"><span class="material-symbols-outlined" style="font-size: 18px" translate="no">download</span><span class="ds2-5-text-link__content">Download free PDF</span></button><a class="ds2-5-text-link ds2-5-text-link--inline js-wsj-grid-card-view-pdf" href="https://www.academia.edu/27845768/Trypanosoma_cruzi_phospho_enol_pyruvate_carboxykinase_ATP_dependent_transition_metal_ion_requirement_for_activity_and_sulfhydryl_group_reactivity"><span class="ds2-5-text-link__content">View PDF</span><span class="material-symbols-outlined" style="font-size: 18px" translate="no">chevron_right</span></a></div></div><div class="ds-related-work--container js-wsj-grid-card" data-collection-position="3" data-entity-id="26018649" data-sort-order="default"><a class="ds-related-work--title js-wsj-grid-card-title ds2-5-body-md ds2-5-body-link" href="https://www.academia.edu/26018649/Differential_energetic_metabolism_during_Trypanosoma_cruzi_differentiation_II_Hexokinase_phosphofructokinase_and_pyruvate_kinase">Differential energetic metabolism during Trypanosoma cruzi differentiation. II. Hexokinase, phosphofructokinase and pyruvate kinase</a><div class="ds-related-work--metadata"><a class="js-wsj-grid-card-author ds2-5-body-sm ds2-5-body-link" data-author-id="37557624" href="https://granada.academia.edu/FranciscoJavierAdroher">Francisco Javier Adroher</a><span>, </span><a class="js-wsj-grid-card-author ds2-5-body-sm ds2-5-body-link" data-author-id="32240805" href="https://granada.academia.edu/AntonioOsuna">Antonio Osuna</a></div><p class="ds-related-work--metadata ds2-5-body-xs">Molecular and Cellular Biochemistry, 1990</p><p class="ds-related-work--abstract ds2-5-body-sm">Adroher, F.J., Osuna, A., Lupiáñez, J.A., 1990. Mol. Cell. Biochem. 94, 71–82. https://doi.org/10.1007/BF00223564 The activities of hexokinase (ATP:hexose-6-phosphate transferase, E.C. 2.7.1.1), phosphofructokinase (ATP:fructose-6-phosphate 1-phosphotransferase, E.C. 2.7.1.11) and pyruvate kinase (ATP:pyruvate trans-ferase, E.C. 2.7.1.40), and their kinetic behaviour in two morphological forms of Trypanosoma cruzi (epimastigotes and metacyclic trypomastigotes) have been studied. The kinetic responses of the three enzymes to their respective substrates were normalized to hyperbolic forms on a velocity versus substrate concentration plots. Hexokinase and phosphofructokinase showed a higher activity in epimastigotes than in metacyclics, whereas pyruvate kinase had similar activity in both forms of the parasite. The specific activity of hexokinase from epimastigotes was 102.00 mUnits/mg of protein and the apparent Km value for glucose was 35.4 microM. Metacyclic forms showed a specific activity of 55.25 mUnits/mg and a Km value of 46.3 microM. The kinetic parameters (specific activity and Km for fructose 6-phosphate) of phosphofructokinase for epimastigotes were 42.60mUnits/mg and 0.31mM and for metacyclics 13.97 mUnits/mg and 0.16 mM, respectively. On the contrary, pyruvate kinase in both forms of T. cruzi did not show significant differences in its kinetic parameters. The specific activity in epimastigotes was 37.00 mUnits/mg and the Km for phosphoe-nolpyruvate was 0.47 mM, whereas in metacyclics these values were 42.94 mUnits/mg and 0.46 mM, respectively. The results presented in this work, clearly demonstrate a quantitative change in the glycolytic pathway of both culture forms of T. cruzi.</p><div class="ds-related-work--ctas"><button class="ds2-5-text-link ds2-5-text-link--inline js-swp-download-button" data-signup-modal="{"location":"wsj-grid-card-download-pdf-modal","work_title":"Differential energetic metabolism during Trypanosoma cruzi differentiation. II. Hexokinase, phosphofructokinase and pyruvate kinase","attachmentId":46362208,"attachmentType":"pdf","work_url":"https://www.academia.edu/26018649/Differential_energetic_metabolism_during_Trypanosoma_cruzi_differentiation_II_Hexokinase_phosphofructokinase_and_pyruvate_kinase","alternativeTracking":true}"><span class="material-symbols-outlined" style="font-size: 18px" translate="no">download</span><span class="ds2-5-text-link__content">Download free PDF</span></button><a class="ds2-5-text-link ds2-5-text-link--inline js-wsj-grid-card-view-pdf" href="https://www.academia.edu/26018649/Differential_energetic_metabolism_during_Trypanosoma_cruzi_differentiation_II_Hexokinase_phosphofructokinase_and_pyruvate_kinase"><span class="ds2-5-text-link__content">View PDF</span><span class="material-symbols-outlined" style="font-size: 18px" translate="no">chevron_right</span></a></div></div><div class="ds-related-work--container js-wsj-grid-card" data-collection-position="4" data-entity-id="81932706" data-sort-order="default"><a class="ds-related-work--title js-wsj-grid-card-title ds2-5-body-md ds2-5-body-link" href="https://www.academia.edu/81932706/Kinetic_and_molecular_characterization_of_the_pyruvate_phosphate_dikinase_from_Trypanosoma_cruzi">Kinetic and molecular characterization of the pyruvate phosphate dikinase from Trypanosoma cruzi</a><div class="ds-related-work--metadata"><a class="js-wsj-grid-card-author ds2-5-body-sm ds2-5-body-link" data-author-id="59124190" href="https://independent.academia.edu/JuanLuisConcepci%C3%B3n">Juan Luis Concepción</a></div><p class="ds-related-work--metadata ds2-5-body-xs">Experimental Parasitology, 2016</p><p class="ds-related-work--abstract ds2-5-body-sm">Trypanosoma cruzi, like other trypanosomatids analyzed so far, can use both glucose and amino acids as carbon and energy source. In these parasites, glycolysis is compartmentalized in glycosomes, authentic but specialized peroxisomes. The major part of this pathway, as well as a two-branched glycolytic auxiliary system, are present in these organelles. The first enzyme of one branch of this auxiliary system is the PPidependent pyruvate phosphate dikinase (PPDK) that converts phosphoenolpyruvate (PEP), inorganic pyrophosphate (PPi) and AMP into pyruvate, inorganic phosphate (Pi) and ATP, thus contributing to the ATP/ADP balance within the glycosomes. In this work we cloned, expressed and purified the T. cruzi PPDK. It kinetic parameters were determined, finding K M values for PEP, PPi and AMP of 320, 70 and 17 µM, respectively. Using molecular exclusion chromatography, two native forms of the enzyme were found with estimated molecular weights of 200 and 100 kDa, corresponding to a homodimer and monomer, respectively. It was established that T. cruzi PPDK's specific activity can be enhanced up to 2.6 times by the presence of ammonium in the assay mixture. During growth of epimastigotes in batch culture an apparent decrease in the specific activity of PPDK was observed. However, when its activity is normalized for the presence of ammonium in the medium, no significant modification of the enzyme activity per cell in time was found.</p><div class="ds-related-work--ctas"><button class="ds2-5-text-link ds2-5-text-link--inline js-swp-download-button" data-signup-modal="{"location":"wsj-grid-card-download-pdf-modal","work_title":"Kinetic and molecular characterization of the pyruvate phosphate dikinase from Trypanosoma cruzi","attachmentId":87803416,"attachmentType":"pdf","work_url":"https://www.academia.edu/81932706/Kinetic_and_molecular_characterization_of_the_pyruvate_phosphate_dikinase_from_Trypanosoma_cruzi","alternativeTracking":true}"><span class="material-symbols-outlined" style="font-size: 18px" translate="no">download</span><span class="ds2-5-text-link__content">Download free PDF</span></button><a class="ds2-5-text-link ds2-5-text-link--inline js-wsj-grid-card-view-pdf" href="https://www.academia.edu/81932706/Kinetic_and_molecular_characterization_of_the_pyruvate_phosphate_dikinase_from_Trypanosoma_cruzi"><span class="ds2-5-text-link__content">View PDF</span><span class="material-symbols-outlined" style="font-size: 18px" translate="no">chevron_right</span></a></div></div><div class="ds-related-work--container js-wsj-grid-card" data-collection-position="5" data-entity-id="12982094" data-sort-order="default"><a class="ds-related-work--title js-wsj-grid-card-title ds2-5-body-md ds2-5-body-link" href="https://www.academia.edu/12982094/Subcellular_localization_of_phosphoenolpyruvate_carboxykinase_in_the_trypanosomatids_Trypanosoma_cruzi_and_Crithidia_fasciculata">Subcellular localization of phosphoenolpyruvate carboxykinase in the trypanosomatids Trypanosoma cruzi and Crithidia fasciculata</a><div class="ds-related-work--metadata"><a class="js-wsj-grid-card-author ds2-5-body-sm ds2-5-body-link" data-author-id="32287176" href="https://unsam.academia.edu/JCazzulo">J. Cazzulo</a><span>, </span><a class="js-wsj-grid-card-author ds2-5-body-sm ds2-5-body-link" data-author-id="32190958" href="https://uga.academia.edu/RobertoDocampo">Roberto Docampo</a></div><p class="ds-related-work--metadata ds2-5-body-xs">Molecular and Biochemical Parasitology, 1982</p><p class="ds-related-work--abstract ds2-5-body-sm">Particulate fractions obtained from Trypanosoma cruzi and Crithidia fasciculata by different procedures were subjected to isopycnic centrifugation in sucrose gradients, in order to determine the subceUular localization of phosphoenolpyruvate carboxykinase (PEPCK) in both organisms, and of malic enzyme (ME) I in T. cruzi. The more clear-cut results were obtained with T. cruzi by breaking the cells by grinding in a mortar with silicon carbide and using a gradient from 0.4 to 2.0 M sucrose, whereas with C. fasciculata, the best procedure was disruption of the cells by digitonin treatment and potter homogenization and use of a gradient from 1.1 to 2.0 M sucrose. PEPCK banded together with the glycosomal marker hexokinase in both organisms; there was a clear separation from the mitochondrial markers, oligomycin-sensitive Mg2÷-APTase and citrate synthase. PEPCK showed a latency of 24% in the enriched 'glycosoma' fraction of T. cruzi. ME I from T. cruzi, on the other hand, banded together with the mitochondrial markers. These results indicate that PEPCK and ME are present in different subcellular compartments, a fact significant for the prevention of a futile cycle between C,dicarboxylic acids and C 3 -monocarboxylic acids, which might take place ff both enzymes functioned in the same compartment.</p><div class="ds-related-work--ctas"><button class="ds2-5-text-link ds2-5-text-link--inline js-swp-download-button" data-signup-modal="{"location":"wsj-grid-card-download-pdf-modal","work_title":"Subcellular localization of phosphoenolpyruvate carboxykinase in the trypanosomatids Trypanosoma cruzi and Crithidia fasciculata","attachmentId":45805309,"attachmentType":"pdf","work_url":"https://www.academia.edu/12982094/Subcellular_localization_of_phosphoenolpyruvate_carboxykinase_in_the_trypanosomatids_Trypanosoma_cruzi_and_Crithidia_fasciculata","alternativeTracking":true}"><span class="material-symbols-outlined" style="font-size: 18px" translate="no">download</span><span class="ds2-5-text-link__content">Download free PDF</span></button><a class="ds2-5-text-link ds2-5-text-link--inline js-wsj-grid-card-view-pdf" href="https://www.academia.edu/12982094/Subcellular_localization_of_phosphoenolpyruvate_carboxykinase_in_the_trypanosomatids_Trypanosoma_cruzi_and_Crithidia_fasciculata"><span class="ds2-5-text-link__content">View PDF</span><span class="material-symbols-outlined" style="font-size: 18px" translate="no">chevron_right</span></a></div></div><div class="ds-related-work--container js-wsj-grid-card" data-collection-position="6" data-entity-id="17329260" data-sort-order="default"><a class="ds-related-work--title js-wsj-grid-card-title ds2-5-body-md ds2-5-body-link" href="https://www.academia.edu/17329260/Characterization_of_pyruvate_kinase_of_Trypanosoma_brucei_and_its_role_in_the_regulation_of_carbohydrate_metabolism">Characterization of pyruvate kinase of Trypanosoma brucei and its role in the regulation of carbohydrate metabolism</a><div class="ds-related-work--metadata"><a class="js-wsj-grid-card-author ds2-5-body-sm ds2-5-body-link" data-author-id="32147726" href="https://uclouvain.academia.edu/FredOpperdoes">Fred Opperdoes</a></div><p class="ds-related-work--metadata ds2-5-body-xs">Molecular and Biochemical Parasitology, 1991</p><p class="ds-related-work--abstract ds2-5-body-sm">Pyruvate kinase from Trypanosoma brucei is a labile enzyme, losing its activity within several hours. In mixtures containing 50 mM triethanolamine buffer, pH 7.2, 25% glycerol and 0.5 mM inorganic phosphate the enzyme remained active and could be purified to homogeneity with a specific activity of 417 units mg-1 and a yield of 65%. The enzyme has an activation energy of 31.9 kJ mol-1. Magnesium and potassium ions are essential for activity. Cobalt or manganese ions replace Mg2+ but this leads to a decrease in maximal velocity. Potassium ions can be substituted by ammonium ions, while sodium ions behave as a competitive inhibitor with respect to both K+ and NH4+. All metal ions studied displayed sigmoidal kinetics. The enzyme is activated, with decreasing efficiency by fructose 2-phosphorothioate 6-phosphate, fructose 2,6-bisphosphate, fructose 1,6-bisphosphate and glucose 1,6-bisphosphate. They all display hyperbolic kinetics. Glycerate 2,3-bisphosphate, glyceraldehyde 3-phosphate, CoASAc, oxalate, AMP, ADP, and ATP inhibit the enzyme. At substrate saturation PK was activated by Pi up to a concentration of 0.8 mM. At higher Pi concentrations the enzyme is inhibited. The enzyme is unaffected by most amino acids, only phenylalanine stimulates and tyrosine inhibits.</p><div class="ds-related-work--ctas"><button class="ds2-5-text-link ds2-5-text-link--inline js-swp-download-button" data-signup-modal="{"location":"wsj-grid-card-download-pdf-modal","work_title":"Characterization of pyruvate kinase of Trypanosoma brucei and its role in the regulation of carbohydrate metabolism","attachmentId":42267961,"attachmentType":"pdf","work_url":"https://www.academia.edu/17329260/Characterization_of_pyruvate_kinase_of_Trypanosoma_brucei_and_its_role_in_the_regulation_of_carbohydrate_metabolism","alternativeTracking":true}"><span class="material-symbols-outlined" style="font-size: 18px" translate="no">download</span><span class="ds2-5-text-link__content">Download free PDF</span></button><a class="ds2-5-text-link ds2-5-text-link--inline js-wsj-grid-card-view-pdf" href="https://www.academia.edu/17329260/Characterization_of_pyruvate_kinase_of_Trypanosoma_brucei_and_its_role_in_the_regulation_of_carbohydrate_metabolism"><span class="ds2-5-text-link__content">View PDF</span><span class="material-symbols-outlined" style="font-size: 18px" translate="no">chevron_right</span></a></div></div><div class="ds-related-work--container js-wsj-grid-card" data-collection-position="7" data-entity-id="17558653" data-sort-order="default"><a class="ds-related-work--title js-wsj-grid-card-title ds2-5-body-md ds2-5-body-link" href="https://www.academia.edu/17558653/Differential_energetic_metabolism_during_Trypanosoma_cruzi_differentiation">Differential energetic metabolism during Trypanosoma cruzi differentiation</a><div class="ds-related-work--metadata"><a class="js-wsj-grid-card-author ds2-5-body-sm ds2-5-body-link" data-author-id="37352370" href="https://granada.academia.edu/JoseLupi%C3%A1%C3%B1ez">Jose Lupiáñez</a></div><p class="ds-related-work--metadata ds2-5-body-xs">Archives of Biochemistry and Biophysics, 1988</p><p class="ds-related-work--abstract ds2-5-body-sm">The activities of the mitochondrial enzymes citrate synthase (citrate oxaloacetatelyase, EC 4.1.3.7), NADP-linked isocitrate dehydrogenase (three-D,-isocitrate:NADP+ oxidoreductase (decarboxylating), EC 1.1.1.42), and succinate dehydrogenase (succinate: FAD oxidoreductase, EC 1.3.99.1) as well as their kinetic behavior in the two developmental forms of Trypanosma cruzi at insect vector stage, epimastigotes and infective metacyclic trypomastigotes, were studied. The results presented in this work clearly demonstrate a higher mitochondrial metabolism in the metacyclic forms as is shown by the extraordinary enhanced activities of metacyclic citrate synthase, isocitrate dehydrogenase, and succinate dehydrogenase. In epimastigotes, the specific activities of citrate synthase at variable concentrations of oxalacetate and acetyl-CoA were 24.6 and 26.6 mU/mg of protein, respectively, and the Michaelis constants were 7.88 and 6.84 PM for both substrates. The metacyclic enzyme exhibited the following kinetic parameters: a specific activity of 228.4 mU/mg and K, of 3.18 ~.LM for oxalacetate and 248.5 mU/mg and 2.75 PM, respectively, for acetyl-CoA. NADP-linked isocitrate dehydrogenase specific activities for epimastigotes and metacyclics were 110.2 and 210.3 mU/mg, whereas the apparent Km's were 47.9 and 12.5 PM, respectively. No activity for the NAD-dependent isozyme was found in any form of T. cruxi differentiation.</p><div class="ds-related-work--ctas"><button class="ds2-5-text-link ds2-5-text-link--inline js-swp-download-button" data-signup-modal="{"location":"wsj-grid-card-download-pdf-modal","work_title":"Differential energetic metabolism during Trypanosoma cruzi differentiation","attachmentId":39579142,"attachmentType":"pdf","work_url":"https://www.academia.edu/17558653/Differential_energetic_metabolism_during_Trypanosoma_cruzi_differentiation","alternativeTracking":true}"><span class="material-symbols-outlined" style="font-size: 18px" translate="no">download</span><span class="ds2-5-text-link__content">Download free PDF</span></button><a class="ds2-5-text-link ds2-5-text-link--inline js-wsj-grid-card-view-pdf" href="https://www.academia.edu/17558653/Differential_energetic_metabolism_during_Trypanosoma_cruzi_differentiation"><span class="ds2-5-text-link__content">View PDF</span><span class="material-symbols-outlined" style="font-size: 18px" translate="no">chevron_right</span></a></div></div><div class="ds-related-work--container js-wsj-grid-card" data-collection-position="8" data-entity-id="17657047" data-sort-order="default"><a class="ds-related-work--title js-wsj-grid-card-title ds2-5-body-md ds2-5-body-link" href="https://www.academia.edu/17657047/Differential_behaviour_of_glucose_6_phosphate_dehydrogenase_in_two_morphological_forms_of_Trypanosoma_cruzi">Differential behaviour of glucose 6-phosphate dehydrogenase in two morphological forms of Trypanosoma cruzi</a><div class="ds-related-work--metadata"><a class="js-wsj-grid-card-author ds2-5-body-sm ds2-5-body-link" data-author-id="37557624" href="https://granada.academia.edu/FranciscoJavierAdroher">Francisco Javier Adroher</a></div><p class="ds-related-work--metadata ds2-5-body-xs">International Journal of Biochemistry, 1987</p><p class="ds-related-work--abstract ds2-5-body-sm">Lupiáñez, J.A., Adroher, F.J., Vargas, A.M., Osuna, A., 1987. Int. J. Biochem. 19, 1085–1089. https://doi.org/10.1016/0020-711X(87)90310-7 1. Glucose 6-phosphate dehydrogenase activity (EC 1.1.1.49) of two morphological forms of Trypanosoma cruzi, epimastigotes and metacyclics, are reported. 2. The kinetic behaviour and some of the kinetic parameters of the enzyme in both forms were studied. The enzymes showed a simple Michaelis-Menten kinetic. 3. The activity in epimastigote forms was alway higher than the metacyclic ones. At subsaturating concentrations of substrate was almost 10-fold higher, whereas at saturating concentrations was about 2-fold higher, 4. In epimastigote forms, the specific activity and Km, values, at pH 7.5 and 37°C, was found to be 142 mUnits × mg-1 of protein and 0.23 mM, respectively. 5. In the same conditions, the specific activity and Km values in metacyclic forms was 75 mUnits × mg-1 of protein and 1.06mM, respectively. 6. A possible role in the carbohydrate metabolism of glucose 6-phosphate dehydrogenase in both forms of Trypanosoma cruzi is discussed. © 1987.</p><div class="ds-related-work--ctas"><button class="ds2-5-text-link ds2-5-text-link--inline js-swp-download-button" data-signup-modal="{"location":"wsj-grid-card-download-pdf-modal","work_title":"Differential behaviour of glucose 6-phosphate dehydrogenase in two morphological forms of Trypanosoma cruzi","attachmentId":39642033,"attachmentType":"pdf","work_url":"https://www.academia.edu/17657047/Differential_behaviour_of_glucose_6_phosphate_dehydrogenase_in_two_morphological_forms_of_Trypanosoma_cruzi","alternativeTracking":true}"><span class="material-symbols-outlined" style="font-size: 18px" translate="no">download</span><span class="ds2-5-text-link__content">Download free PDF</span></button><a class="ds2-5-text-link ds2-5-text-link--inline js-wsj-grid-card-view-pdf" href="https://www.academia.edu/17657047/Differential_behaviour_of_glucose_6_phosphate_dehydrogenase_in_two_morphological_forms_of_Trypanosoma_cruzi"><span class="ds2-5-text-link__content">View PDF</span><span class="material-symbols-outlined" style="font-size: 18px" translate="no">chevron_right</span></a></div></div><div class="ds-related-work--container js-wsj-grid-card" data-collection-position="9" data-entity-id="99917756" data-sort-order="default"><a class="ds-related-work--title js-wsj-grid-card-title ds2-5-body-md ds2-5-body-link" href="https://www.academia.edu/99917756/Glucose_metabolism_in_Trypanosoma_cruzi">Glucose metabolism in Trypanosoma cruzi</a><div class="ds-related-work--metadata"><a class="js-wsj-grid-card-author ds2-5-body-sm ds2-5-body-link" data-author-id="265093893" href="https://independent.academia.edu/MaugeriDante">Dante Maugeri</a></div><p class="ds-related-work--metadata ds2-5-body-xs">Essays in biochemistry, 2011</p><p class="ds-related-work--abstract ds2-5-body-sm">The causative agent of Chagas disease, Trypanosoma cruzi, metabolizes glucose through two major pathways: glycolysis and the pentose phosphate pathway. Glucose is taken up via one facilitated transporter and its catabolism by the glycolytic pathway leads to the excretion of reduced products, succinate and l-alanine, even in the presence of oxygen; the first six enzymes are located in a peroxisome-like organelle, the glycosome, and the lack of regulatory controls in hexokinase and phosphofructokinase results in the lack of the Pasteur effect. All of the enzymes of the pentose phosphate pathway are present in the four major stages of the parasite&#39;s life cycle, and some of them are possible targets for chemotherapy. The gluconeogenic enzymes phosphoenolpyruvate carboxykinase and fructose-1,6-bisphosphatase are present, but there is no reserve polysaccharide.</p><div class="ds-related-work--ctas"><button class="ds2-5-text-link ds2-5-text-link--inline js-swp-download-button" data-signup-modal="{"location":"wsj-grid-card-download-pdf-modal","work_title":"Glucose metabolism in Trypanosoma cruzi","attachmentId":100879416,"attachmentType":"pdf","work_url":"https://www.academia.edu/99917756/Glucose_metabolism_in_Trypanosoma_cruzi","alternativeTracking":true}"><span class="material-symbols-outlined" style="font-size: 18px" translate="no">download</span><span class="ds2-5-text-link__content">Download free PDF</span></button><a class="ds2-5-text-link ds2-5-text-link--inline js-wsj-grid-card-view-pdf" href="https://www.academia.edu/99917756/Glucose_metabolism_in_Trypanosoma_cruzi"><span class="ds2-5-text-link__content">View PDF</span><span class="material-symbols-outlined" style="font-size: 18px" translate="no">chevron_right</span></a></div></div></div></div><div class="ds-sticky-ctas--wrapper js-loswp-sticky-ctas hidden"><div class="ds-sticky-ctas--grid-container"><div class="ds-sticky-ctas--container"><button class="ds2-5-button js-swp-download-button" data-signup-modal="{"location":"continue-reading-button--sticky-ctas","attachmentId":48130344,"attachmentType":"pdf","workUrl":null}">See full PDF</button><button class="ds2-5-button ds2-5-button--secondary js-swp-download-button" data-signup-modal="{"location":"download-pdf-button--sticky-ctas","attachmentId":48130344,"attachmentType":"pdf","workUrl":null}"><span class="material-symbols-outlined" style="font-size: 20px" translate="no">download</span>Download PDF</button></div></div></div><div class="ds-below-fold--grid-container"><div class="ds-work--container js-loswp-embedded-document"><div class="attachment_preview" data-attachment="Attachment_48130344" style="display: none"><div class="js-scribd-document-container"><div class="scribd--document-loading js-scribd-document-loader" style="display: block;"><img alt="Loading..." src="//a.academia-assets.com/images/loaders/paper-load.gif" /><p>Loading Preview</p></div></div><div style="text-align: center;"><div class="scribd--no-preview-alert js-preview-unavailable"><p>Sorry, preview is currently unavailable. You can download the paper by clicking the button above.</p></div></div></div></div><div class="ds-sidebar--container js-work-sidebar"><div class="ds-related-content--container"><h2 class="ds-related-content--heading">Related papers</h2><div class="ds-related-work--container js-related-work-sidebar-card" data-collection-position="0" data-entity-id="109548021" data-sort-order="default"><a class="ds-related-work--title js-related-work-grid-card-title ds2-5-body-md ds2-5-body-link" href="https://www.academia.edu/109548021/Two_forms_of_malic_enzyme_with_different_regulatory_properties_in_Trypanosoma_cruzi">Two forms of ‘malic’ enzyme with different regulatory properties in Trypanosoma cruzi</a><div class="ds-related-work--metadata"><a class="js-related-work-grid-card-author ds2-5-body-sm ds2-5-body-link" data-author-id="66964791" href="https://independent.academia.edu/JoaquinJBCannata">Joaquin J B Cannata</a></div><p class="ds-related-work--metadata ds2-5-body-xs">Biochemical journal. Cellular aspects, 1979</p><div class="ds-related-work--ctas"><button class="ds2-5-text-link ds2-5-text-link--inline js-swp-download-button" data-signup-modal="{"location":"wsj-grid-card-download-pdf-modal","work_title":"Two forms of ‘malic’ enzyme with different regulatory properties in Trypanosoma cruzi","attachmentId":107640208,"attachmentType":"pdf","work_url":"https://www.academia.edu/109548021/Two_forms_of_malic_enzyme_with_different_regulatory_properties_in_Trypanosoma_cruzi","alternativeTracking":true}"><span class="material-symbols-outlined" style="font-size: 18px" translate="no">download</span><span class="ds2-5-text-link__content">Download free PDF</span></button><a class="ds2-5-text-link ds2-5-text-link--inline js-related-work-grid-card-view-pdf" href="https://www.academia.edu/109548021/Two_forms_of_malic_enzyme_with_different_regulatory_properties_in_Trypanosoma_cruzi"><span class="ds2-5-text-link__content">View PDF</span><span class="material-symbols-outlined" 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