Chemoenzymatic Approach to Enantiopure Streptogramin B Variants: Characterization of Stereoselective Pristinamycin I Cyclase from Streptomyces pristinaespiralis was written by Mahlert, Christoph;Sieber, Stephan A.;Gruenewald, Jan;Marahiel, Mohamed A.. And the article was included in Journal of the American Chemical Society in 2005.Quality Control of (S)-1-(((9H-Fluoren-9-yl)methoxy)carbonyl)piperidine-2-carboxylic acid The following contents are mentioned in the article:
Streptogramin B antibiotics are cyclic peptide natural products produced by Streptomyces species. In combination with the synergistic group A component, they are last line of defense antimicrobial agents against multi-resistant cocci. The racemization sensitivity of the phenylglycine (Phg7) ester is a complex challenge in total chem. synthesis of streptogramin B mols. To provide fast and easy access to novel streptogramin antibiotics, we introduce a novel chemoenzymic strategy in which diversity is generated by standard solid phase protocols and stereoselectivity by subsequent enzymic cyclization. For this approach, we cloned, over-produced, and biochem. characterized the recombinant thioesterase domain SnbDE TE of the pristinamycin I nonribosomal peptide synthetase from Streptomyces pristinaespiralis. SnbDE TE catalyzes regioselective ring closure of linear peptide thioester analogs of pristinamycin I as well as stereoselective cyclization out of complex in situ racemizing substrate mixtures, enabling synthesis of Streptogramin B variants via a dynamic kinetic resolution assay. A remarkable substrate tolerance was detected for the enzymic cyclization including all the seven positions of the peptide backbone. Interestingly, SnbDE TE was observed to be the first cyclase from a macrolactone forming NRPS which is addnl. able to catalyze macrolactamization of peptide thioester substrates. An N-methylated peptide bond between positions 4 and 5 is mandatory for a high substrate turnover. The presented strategy is potent to screen for analogs with improved activity and guides our understanding of structure-activity relationships in the important class of streptogramin antibiotics. This study involved multiple reactions and reactants, such as (S)-1-(((9H-Fluoren-9-yl)methoxy)carbonyl)piperidine-2-carboxylic acid (cas: 86069-86-5Quality Control of (S)-1-(((9H-Fluoren-9-yl)methoxy)carbonyl)piperidine-2-carboxylic acid).
(S)-1-(((9H-Fluoren-9-yl)methoxy)carbonyl)piperidine-2-carboxylic acid (cas: 86069-86-5) belongs to piperidine derivatives. Piperidine is a metabolite of cadaverine, a polyamine found in the human intestine. Piperidine derivatives bearing a masked aldehyde function in the ε-position are easily transformed into quinolizidine compounds through intramolecular reductive amination.Quality Control of (S)-1-(((9H-Fluoren-9-yl)methoxy)carbonyl)piperidine-2-carboxylic acid
Referemce:
Piperidine – Wikipedia,
Piperidine | C5H11N – PubChem