82317-75-7Relevant academic research and scientific papers
Tailored Peptide Phenyl Esters Block ClpXP Proteolysis by an Unusual Breakdown into a Heptamer–Hexamer Assembly
Lakemeyer, Markus,Bertosin, Eva,M?ller, Friederike,Balogh, Dóra,Strasser, Ralf,Dietz, Hendrik,Sieber, Stephan A.
supporting information, p. 7127 - 7132 (2019/04/27)
The proteolytic complex ClpXP is fundamental to bacterial homeostasis and pathogenesis. Because of its conformational flexibility, the development of potent ClpXP inhibitors is challenging, and novel tools to decipher its intricate regulation are urgently needed. Herein, we present amino acid based phenyl esters as molecular probes to study the activity and oligomerization of the ClpXP complex of S. aureus. Systematic screening of (R)- and (S)-amino acids led to compounds showing potent inhibition, as well as stimulation of ClpXP-mediated proteolysis. Substoichiometric binding of probes arrested ClpXP in an unprecedented heptamer–hexamer assembly, in which the two heptameric ClpP rings are dissociated from each other. At the same time, the affinity between ClpX and ClpP increased, leading to inhibition of both enzymes. This conformational arrest is beneficial for the consolidated shutdown of ClpXP, as well as for the study of the oligomeric state during its catalytic cycle.
Synthesis of (S)-3,4-dihydroxyphenylalanine (L-DOPA) and unnatural α-amino acids via enzymatic resolution using alcalase
Tyagi, O D,Boll, P M,Parmar, V S,Taneja, Poonam,Singh, S K
, p. 851 - 854 (2007/10/02)
Enzymatic resolution has been used for the synthesis of L-DOPA with high optical purity.N-Acetyl-(R,S)-3,4-methylenedioxyphenylalanine methyl ester (2b) on enzymatic resolution by alcalase (Subtilisin Carlsberg) yields N-acetyl-(S)-3,4-methylenedioxyphenylalanine (3b) which upon acid treatment affords (S)-3,4-dihydroxyphenylalanine (L-DOPA) (4).Several optically active unnatural N-acetylated and N-benzoylated α-amino acids have been prepared by similar enzymatic resolution.
