{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Nigro M"],"funding":["ANPCyT","universidad nacional de Quilmes"],"pagination":["750"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC11274987"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["14(7)"],"pubmed_abstract":["Dihydroxyacetone phosphate (DHAP)-dependent aldolases catalyze the aldol addition of DHAP to a variety of aldehydes and generate compounds with two stereocenters. This reaction is useful to synthesize chiral acyclic nucleosides, which constitute a well-known class of antiviral drugs currently used. In such compounds, the chirality of the aliphatic chain, which mimics the open pentose residue, is crucial for activity. In this work, three DHAP-dependent aldolases: fructose-1,6-biphosphate aldolase from rabbit muscle, rhanmulose-1-phosphate aldolase from <i>Thermotoga maritima</i>, and fuculose-1-phosphate aldolase from <i>Escherichia coli</i>, were used as biocatalysts. Aldehyde derivatives of thymine and cytosine were used as acceptor substrates, generating new acyclic nucleoside analogues "],"journal":["Biomolecules"],"pubmed_title":["Synthesis of Chiral Acyclic Pyrimidine Nucleoside Analogues from DHAP-Dependent Aldolases."],"pmcid":["PMC11274987"],"funding_grant_id":["EXPTE. 2287/22","PICT"],"pubmed_authors":["Iribarren AM","Nigro M","Benito-Arenas R","Lewkowicz ES","Veiga N","Valino AL","Garcia-Junceda E","Sanchez-Moreno I"],"additional_accession":[]},"is_claimable":false,"name":"Synthesis of Chiral Acyclic Pyrimidine Nucleoside Analogues from DHAP-Dependent Aldolases.","description":"Dihydroxyacetone phosphate (DHAP)-dependent aldolases catalyze the aldol addition of DHAP to a variety of aldehydes and generate compounds with two stereocenters. This reaction is useful to synthesize chiral acyclic nucleosides, which constitute a well-known class of antiviral drugs currently used. In such compounds, the chirality of the aliphatic chain, which mimics the open pentose residue, is crucial for activity. In this work, three DHAP-dependent aldolases: fructose-1,6-biphosphate aldolase from rabbit muscle, rhanmulose-1-phosphate aldolase from <i>Thermotoga maritima</i>, and fuculose-1-phosphate aldolase from <i>Escherichia coli</i>, were used as biocatalysts. Aldehyde derivatives of thymine and cytosine were used as acceptor substrates, generating new acyclic nucleoside analogues ","dates":{"release":"2024-01-01T00:00:00Z","publication":"2024 Jun","modification":"2026-04-21T03:29:08.522Z","creation":"2025-04-19T13:12:22.145Z"},"accession":"S-EPMC11274987","cross_references":{"pubmed":["39062466"],"doi":["10.3390/biom14070750"]}}