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Your search keyword '"Martín Alejandro Palazzolo"' showing total 3 results
Start Over Author "Martín Alejandro Palazzolo" Topic aldolase a
3 results on '"Martín Alejandro Palazzolo"'

1. N-Acetylneuraminic acid aldolase-catalyzed synthesis of acyclic nucleoside analogues carrying a 4-hydroxy-2-oxoacid moiety

Author

Mariano J. Nigro, Elizabeth Sandra Lewkowicz, Martín Alejandro Palazzolo, Adolfo M. Iribarren, and Diego Damián Colasurdo

Subjects
Stereochemistry, Butyrate, 010402 general chemistry, 01 natural sciences, Catalysis, Nucleobase, purl.org/becyt/ford/1 [https], chemistry.chemical_compound, Aldol reaction, purl.org/becyt/ford/1.4 [https], Moiety, N-ACETYLNEURAMINIC ACID ALDOLASE, chemistry.chemical_classification, ACYCLIC NUCLEOSIDES, biology, 010405 organic chemistry, Process Chemistry and Technology, Otras Ciencias Químicas, Aldolase A, Ciencias Químicas, General Chemistry, 0104 chemical sciences, Sialic acid, Enzyme, chemistry, Oxoacid, biology.protein, CIENCIAS NATURALES Y EXACTAS, ALDOL ADDITION
Abstract

N-Acetylneuraminic acid aldolase (NeuAcA) (EC 4.1.3.3) is a pyruvate-dependent class I aldolase that catalyzes the reversible aldol cleavage of N-acetylneuraminic acid to form N-acetyl-D-mannosamine and pyruvate. The synthetic activity of this enzyme has been applied to the preparation of many sialic acid analogues. In this report, we demonstrate the ability of NeuAcA from Clostridium perfringens to use 2-oxoethyl substituted nucleobases as unusual acceptor substrates to perform aldol additions. In this way, novel acyclic nucleoside analogues bearing a further derivatizable 4-hydroxy-2-oxo butyrate skeleton were prepared in good yields. Fil: Nigro, Mariano J.. Universidad Nacional de Quilmes; Argentina Fil: Palazzolo, Martín Alejandro. Universidad Nacional de Quilmes; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina Fil: Colasurdo, Diego Damián. Universidad Nacional de La Plata. Facultad de Ciencias Exactas. Departamento de Química. Laboratorio de Estudio de Compuestos Orgánicos; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata; Argentina Fil: Iribarren, Adolfo Marcelo. Universidad Nacional de Quilmes; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina Fil: Lewkowicz, Elizabeth Sandra. Universidad Nacional de Quilmes; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina

Published
2019

2. ChemInform Abstract: A Chemoenzymatic Route to Prepare Acyclic Nucleoside Analogues

Author

Adolfo M. Iribarren, Mariano J. Nigro, Elizabeth Sandra Lewkowicz, and Martín Alejandro Palazzolo

Subjects
biology, Stereochemistry, organic chemicals, Acyclic nucleoside, Aldolase A, Dihydroxyacetone, General Medicine, Condensation reaction, Nucleobase, Catalysis, chemistry.chemical_compound, chemistry, polycyclic compounds, biology.protein, Aldol condensation
Abstract

involving an aldol condensation of aldehydes of various nucleobases catalyzed by a dihydroxyacetone phosphate-dependent aldolase (rabbit muscle aldolase)

Published
2016

3. Selection of a New Whole Cell Biocatalyst for the Synthesis of 2-Deoxyribose 5-Phosphate

Author

Adolfo M. Iribarren, Ana Laura Valino, Elizabeth Sandra Lewkowicz, and Martín Alejandro Palazzolo

Subjects
Deoxyribonucleosides, Bioengineering, Erwinia, Applied Microbiology and Biotechnology, Biochemistry, chemistry.chemical_compound, Aldol reaction, Organic chemistry, Molecular Biology, Aldehyde-Lyases, Bacteria, biology, Chemistry, Aldolase A, Acetaldehyde, Substrate (chemistry), General Medicine, biology.organism_classification, Pectobacterium carotovorum, Biocatalysis, biology.protein, Indicators and Reagents, Ribosemonophosphates, Biotechnology
Abstract

2-deoxyribose 5-phosphate (DR5P) is a key intermediate in the biocatalyzed preparation of deoxyribonucleosides. Therefore, DR5P production by means of simpler, cleaner, and economic pathways becomes highly interesting. One strategy involves the use of bacterial whole cells containing DR5P aldolase as biocatalyst for the aldol addition between acetaldehyde and D: -glyceraldehyde 3-phosphate or glycolytic intermediates that in situ generate the acceptor substrate. In this work, diverse microorganisms capable of synthesizing DR5P were selected by screening several bacteria genera. In particular, Erwinia carotovora ATCC 33260 was identified as a new biocatalyst that afforded 14.1-mM DR5P starting from a cheap raw material like glucose.

Published
2011

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