276682-02-1

Basic information

• Product Name: methyl (2R)-S-tritylthiolactate
• Synonyms: methyl (2R)-S-tritylthiolactate
• CAS NO: 276682-02-1
• Molecular Weight: 362.492
• Mol File: 276682-02-1.mol
• Article Data: 3

Chemical Properties

• CAS DataBase Reference: methyl (2R)-S-tritylthiolactate(CAS DataBase Reference)
• NIST Chemistry Reference: methyl (2R)-S-tritylthiolactate(276682-02-1)
• EPA Substance Registry System: methyl (2R)-S-tritylthiolactate(276682-02-1)

Safety Data

• Hazardous Substances Data: 276682-02-1(Hazardous Substances Data)

Upstream product

• 3695-77-0 triphenylmethanethiol 
• 67-56-1 methanol 
• 42411-39-2 (R)-ethyl 2-chloropropanoate 

Downstream Products

• 480995-84-4 N-propyl-(2S)-S-tritylthiolactamide 
• 276682-05-4 S-trityl-2S-thiolactyl-2R-alanine amide 
• 276682-03-2 (2S)-S-tritylthiolactic acid 

Relevant articles and documents

Use of trityl thiol for stereoselective thioester synthesis: A new preparation of (S)-thiolactic acid

Trityl thiol is found to be a convenient reagent for the enantioselective preparation of (S)-thiolactic acid and a muramic acid thioester. (C) 2000 Elsevier Science Ltd.

Thioester analogues of peptidoglycan fragment MurNAc-L-Ala-γ-D-Glu as substrates for peptidoglycan hydrolase MurNAc-L-Ala amidase

MurNAc-L-amidase is one of a family of peptidoglycan hydrolases which catalyses the breakdown of bacterial peptidoglycan. Analogues of the peptidoglycan fragment MurNAc-L-Ala-γ-D-Glu containing S-thiolactic acid in place of L-alanine were synthesised as thioester substrates for this enzyme. Triphenylmethanethiol was used to develop a stereoselective synthesis of S-thiolactic acid, which was elaborated synthetically into MurNAc-dipeptide analogues. MurNAc-S-thioacetyl-N-propylamide 13 and MurNAc-S-thiolactyl-2R-alaninamide 16 were found not to be substrates for recombinant MurNAc-L-Ala amidases CwlA from Bacillus subtilis and Ply21 from bacteriophage TP21, however, turnover of tripeptide thioester S-propionylthiolactyl-γ-D-Glu-L-Lys-OMe 21 was observed using amidase Ply21. Therefore, recognition of the amino acid at position 3 of the pentapeptide sidechain appears to be important for enzymatic turnover.