60668-55-5

Upstream product

• 63-91-2 L-phenylalanine 
• 60687-36-7 (R)-(1-aminoethyl)phosphonic acid 
• 3397-32-8 N-(benzyloxycarbonyl)-phenylalanine-N-hydroxysuccinimide ester 
• 60668-54-4 (1R)-1-[(N-benzyloxycarbonyl-L-phenylalanyl)amino]-ethylphosphonic acid 

Relevant academic research and scientific papers

Investigation of Amide Bond Formation during Dehydrophos Biosynthesis

Dehydrophos is a tripeptide phosphonate antibiotic produced by Streptomyces luridus. Its biosynthetic pathway involves the use of aminoacyl-tRNA (aa-tRNA) for amide bond formation. The first amide bond during biosynthesis is formed by DhpH-C, a peptidyltransferase that utilizes Leu-tRNALeu. DhpH-C is a member of a burgeoning family of natural product biosynthetic enzymes that make use of aa-tRNA outside of canonical translation activities in the cell. Here, we used site-directed mutagenesis of both DhpH-C and tRNALeu to investigate the enzyme mechanism and substrate specificity, respectively, and analyzed the substrate scope for the production of a set of dipeptides. DhpH-C appears to recognize both the amino acyl group on the tRNA and the tRNA acceptor stem, and the enzyme can accept other hydrophobic residues, in addition to leucine. These results contribute to a better understanding of enzyme-aa-tRNA interactions and the growing exploration of aa-tRNA usage beyond translation.

Peptide derivatives of phosphonic and phosphinic acids and intermediates therefor

The present disclosure relates to peptide derivatives. More particularly, the disclosure is concerned with peptide derivatives of phosphonic and phosphinic acids, a process for the manufacture thereof and pharmaceutical preparations containing same.