{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"omics_type":["Unknown"],"volume":["19(1)"],"submitter":["Ma Y"],"pubmed_abstract":["In this paper, we present a novel, \"single experiment\" methodology based on genetic engineering of metabolic pathways for direct intracellular production of non-canonical amino acids from simple precursors, coupled with expanded genetic code. In particular, we engineered the intracellular biosynthesis of L-azidohomoalanine from O-acetyl-L-homoserine and NaN3, and achieved its direct incorporation into recombinant target proteins by AUG codon reassignment in a methionine-auxotroph E. coli strain. In our system, the host's methionine biosynthetic pathway was first diverted towards the production of the desired non-canonical amino acid by exploiting the broad reaction specificity of recombinant pyridoxal phosphate-dependent O-acetylhomoserine sulfhydrylase from Corynebacterium glutamicum. The"],"journal":["Molecules (Basel, Switzerland)"],"pagination":["1004-22"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC6271081"],"repository":["biostudies-literature"],"pubmed_title":["Coupling bioorthogonal chemistries with artificial metabolism: intracellular biosynthesis of azidohomoalanine and its incorporation into recombinant proteins."],"pmcid":["PMC6271081"],"pubmed_authors":["Ma Y","Biava H","Contestabile R","Budisa N","di Salvo ML"],"additional_accession":[]},"is_claimable":false,"name":"Coupling bioorthogonal chemistries with artificial metabolism: intracellular biosynthesis of azidohomoalanine and its incorporation into recombinant proteins.","description":"In this paper, we present a novel, \"single experiment\" methodology based on genetic engineering of metabolic pathways for direct intracellular production of non-canonical amino acids from simple precursors, coupled with expanded genetic code. In particular, we engineered the intracellular biosynthesis of L-azidohomoalanine from O-acetyl-L-homoserine and NaN3, and achieved its direct incorporation into recombinant target proteins by AUG codon reassignment in a methionine-auxotroph E. coli strain. In our system, the host's methionine biosynthetic pathway was first diverted towards the production of the desired non-canonical amino acid by exploiting the broad reaction specificity of recombinant pyridoxal phosphate-dependent O-acetylhomoserine sulfhydrylase from Corynebacterium glutamicum. The","dates":{"release":"2014-01-01T00:00:00Z","publication":"2014 Jan","modification":"2026-05-06T05:54:09.021Z","creation":"2025-05-18T13:31:25.862Z"},"accession":"S-EPMC6271081","cross_references":{"pubmed":["24434673"],"doi":["10.3390/molecules19011004"]}}