Výsledky vyhledávání - "Mabel Cristina Aleanzi"

On the simultaneous activation of Agrobacterium tumefaciens ADP-glucose pyrophosphorylase by pyruvate and fructose 6-phosphate

Autor: Romila Mascarenhas, Mabel Cristina Aleanzi, Carlos Maria Figueroa, María Cecilia Esper, Dali Liu, Miguel A. Ballicora, Matías Damián Asención Diez, Alberto A. Iglesias

Publikováno v: Biochimie.

Bacterial ADP-glucose pyrophosphorylases are allosterically regulated by metabolites that are key intermediates of central pathways in the respective microorganism. Pyruvate (Pyr) and fructose 6-phosphate (Fru6P) activate the enzyme from Agrobacteriu

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::5a8bab6ad6394a5f27cc66a629a00262
https://pubmed.ncbi.nlm.nih.gov/32014504

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A Chimeric UDP-Glucose Pyrophosphorylase Produced by Protein Engineering Exhibits Sensitivity to Allosteric Regulators

Autor: Ana Cristina Ebrecht, Sergio Adrian Guerrero, Lucila Inés Martínez, Miguel A. Ballicora, Alberto A. Iglesias, Mabel Cristina Aleanzi, Matías Damián Asención Diez

Publikováno v: International Journal of Molecular Sciences, Vol 14, Iss 5, Pp 9703-9721 (2013)
International Journal of Molecular Sciences; Volume 14; Issue 5; Pages: 9703-9721
International Journal of Molecular Sciences
CONICET Digital (CONICET)
Consejo Nacional de Investigaciones Científicas y Técnicas
instacron:CONICET

In bacteria, glycogen or oligosaccharide accumulation involves glucose-1-phosphate partitioning into either ADP-glucose (ADP-Glc) or UDP-Glc. Their respective synthesis is catalyzed by allosterically regulated ADP-Glc pyrophosphorylase (EC 2.7.7.27,

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ed5d9b8a00e89af8eff105172caab92e
http://www.mdpi.com/1422-0067/14/5/9703

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UDPglucose pyrophosphorylase from Xanthomonas spp. Characterization of the enzyme kinetics, structure and inactivation related to oligomeric dissociation

Autor: Mabel Cristina Aleanzi, M.B. Bosco, Matías Machtey, Alberto A. Iglesias

Publikováno v: Biochimie. 91:204-213

The genes encoding for UDPglucose pyrophosphorylase in two Xanthomonas spp. were cloned and overexpressed in Escherichia coli. After purification to electrophoretic homogeneity, the recombinant proteins were characterized, and both exhibited similar

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a64ac336c963e3b4665fc3c009385cf8
https://doi.org/10.1016/j.biochi.2008.09.001

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Identification of Regions Critically Affecting Kinetics and Allosteric Regulation of the Escherichia coli ADP-Glucose Pyrophosphorylase by Modeling and Pentapeptide-Scanning Mutagenesis

Autor: Esteban Erben, Ana L. Bertolo, Corina M. Fusari, Carlos Maria Figueroa, Alberto A. Iglesias, Jennifer R. Schmidt, Jack Preiss, Terutaka Yazaki, Mabel Cristina Aleanzi, Clarisa M. Bejar, Miguel A. Ballicora, Ana María Magdalena Demonte

Publikováno v: Journal of Bacteriology. 189:5325-5333

ADP-glucose pyrophosphorylase (ADP-Glc PPase) is the enzyme responsible for the regulation of bacterial glycogen synthesis. To perform a structure-function relationship study of the Escherichia coli ADP-Glc PPase enzyme, we studied the effects of pen

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::92362275dfebc99321ea2f079bd26109
https://doi.org/10.1128/jb.00481-07

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A novel dual allosteric activation mechanism of Escherichia coli ADP-glucose pyrophosphorylase: the role of pyruvate

Autor: Mabel Cristina Aleanzi, Miguel A. Ballicora, Alberto A. Iglesias, Matías Damián Asención Diez

Publikováno v: PLoS ONE, Vol 9, Iss 8, p e103888 (2014)
CONICET Digital (CONICET)
Consejo Nacional de Investigaciones Científicas y Técnicas
instacron:CONICET
PLoS ONE

Fructose-1,6-bisphosphate activates ADP-glucose pyrophosphorylase and the synthesis of glycogen in Escherichia coli. Here, we show that although pyruvate is a weak activator by itself, it synergically enhances the fructose-1,6-bisphosphate activation

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::2cc7a9a0f9f1146029d59396ac6d1c78
http://europepmc.org/articles/PMC4125136?pdf=render

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Celiac Disease

Autor: Silvia Garcilazo, Marta Waggener, Mabel Cristina Aleanzi, Cecilia Esper, Ana María Magdalena Demonte

Publikováno v: Clinical Chemistry. 47:2023-2028

Background: Selective deamidation of glutamine residues by tissue transglutaminase (tTG) turns gliadin peptides into stronger activators of T cells from celiac disease (CD) patients. We examined the possibility that these modified peptides could be m

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::a3de289ef95a39b2746ccc721dbe224a
https://doi.org/10.1093/clinchem/47.11.2023

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Epitope contiguous chains and antibody recognition in HIV-1 synthetic peptide antigens

Autor: Mabel Cristina Aleanzi, Georgina Tonarelli, Alejandro Montaner, Norma Perotti, Javier Lottersberger, Alberto J. Marcipar

Publikováno v: Journal of Molecular Recognition. 9:631-638

Five peptides derived from human immuno deficiency virus (HIV-1) gp41 transmembrane protein have been synthesized: M9 (610-618), M12 (598-609), M15 (600-614), M21 (584-604) and M23 (587-609). These sequences partially overlap in the region vicinal to

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::2f52e3da83a20b0b16c9658642423806
https://doi.org/10.1002/(sici)1099-1352(199634/12)9:5/6<631::aid-jmr312>3.0.co

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Insights into Glycogen Metabolism in Chemolithoautotrophic Bacteria from Distinctive Kinetic and Regulatory Properties of ADP-Glucose Pyrophosphorylase from Nitrosomonas europaea

Autor: Miguel A. Ballicora, Misty L. Kuhn, Matías Machtey, Diane A. Flasch, Alberto A. Iglesias, Mabel Cristina Aleanzi

Nitrosomonas europaea is a chemolithoautotroph that obtains energy by oxidizing ammonia in the presence of oxygen and fixes CO2 via the Benson-Calvin cycle. Despite its environmental and evolutionary importance, very little is known about the regulat

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e8badd9468fdf62b5ab3e18a0af0a64b
https://europepmc.org/articles/PMC3486394/

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Understanding the allosteric trigger for the fructose-1,6-bisphosphate regulation of the ADP-glucose pyrophosphorylase from Escherichia coli

Autor: Ana L. Bertolo, Ana María Magdalena Demonte, Carlos Maria Figueroa, Miguel A. Ballicora, Mabel Cristina Aleanzi, María Cecilia Esper, Alberto A. Iglesias

Publikováno v: Biochimie. 93(10)

ADP-glucose pyrophosphorylase is the enzyme responsible for the regulation of glycogen synthesis in bacteria. The enzyme N-terminal domain has a Rossmann-like fold with three neighbor loops facing the substrate ATP. In the Escherichia coli enzyme, on

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::580ca36afe5145183b19eebfefd58509
https://pubmed.ncbi.nlm.nih.gov/21741429

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Plastidic phosphoglycerate kinase from Phaeodactylum tricornutum: on the critical role of cysteine residues for the enzyme function

Autor: Mabel Cristina Aleanzi, María Belén Bosco, Alberto A. Iglesias

Publikováno v: Protist. 163(2)

Chloroplastidic phosphoglycerate kinase (PGKase) plays a key role in photosynthetic organisms, catalyzing a key step in the Calvin cycle. We performed the molecular cloning of the gene encoding chloroplastidic PGKase-1 in the diatom Phaeodactylum tri

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::2aa248a361d14e420773f14b85e3b6c1
https://pubmed.ncbi.nlm.nih.gov/21816671

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