{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Bougioukou DJ"],"funding":["NCRR NIH HHS","National Institute of General Medical Sciences","NIGMS NIH HHS"],"pagination":["822-829"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC6344287"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["17(4)"],"pubmed_abstract":["The C-terminal domain of the dehydrophos biosynthetic enzyme DhpH (DhpH-C) catalyzes the condensation of Leu-tRNALeu with (R)-1-aminoethylphosphonate, the aminophosphonate analog of alanine called Ala(P). The product of this reaction, Leu-Ala(P), is a phosphonodipeptide, a class of compounds that have previously been investigated for use as clinical antibiotics. In this study, we show that DhpH-C is highly substrate tolerant and can condense various aminophosphonates (Gly(P), Ser(P), Val(P), 1-amino-propylphosphonate, and phenylglycine(P)) to Leu. Moreover, the enzyme is also tolerant with respect to the amino acid attached to tRNALeu. Using a mutant of leucyl tRNA synthetase that is deficient in its proofreading ability allowed the preparation of a series of aminoacyl-tRNALeu derivatives "],"journal":["Organic & biomolecular chemistry"],"pubmed_title":["Use of the dehydrophos biosynthetic enzymes to prepare antimicrobial analogs of alaphosphin."],"pmcid":["PMC6344287"],"funding_grant_id":["S10-RR028833","S10 RR028833","F32 GM129944","P01 GM077596","GM 077596"],"pubmed_authors":["Bougioukou DJ","Peck SC","Mukherjee S","Ting CP","van der Donk WA"],"additional_accession":[]},"is_claimable":false,"name":"Use of the dehydrophos biosynthetic enzymes to prepare antimicrobial analogs of alaphosphin.","description":"The C-terminal domain of the dehydrophos biosynthetic enzyme DhpH (DhpH-C) catalyzes the condensation of Leu-tRNALeu with (R)-1-aminoethylphosphonate, the aminophosphonate analog of alanine called Ala(P). The product of this reaction, Leu-Ala(P), is a phosphonodipeptide, a class of compounds that have previously been investigated for use as clinical antibiotics. In this study, we show that DhpH-C is highly substrate tolerant and can condense various aminophosphonates (Gly(P), Ser(P), Val(P), 1-amino-propylphosphonate, and phenylglycine(P)) to Leu. Moreover, the enzyme is also tolerant with respect to the amino acid attached to tRNALeu. Using a mutant of leucyl tRNA synthetase that is deficient in its proofreading ability allowed the preparation of a series of aminoacyl-tRNALeu derivatives ","dates":{"release":"2019-01-01T00:00:00Z","publication":"2019 Jan","modification":"2025-04-04T02:39:35.86Z","creation":"2020-10-29T12:52:45Z"},"accession":"S-EPMC6344287","cross_references":{"pubmed":["30608108"],"doi":["10.1039/c8ob02860e"]}}