118546-67-1

Basic information

• Product Name: Carbamic acid, [(1R)-1-formyl-2-[(phenylmethyl)thio]ethyl]-, 1,1-dimethylethyl ester
• CAS NO: 118546-67-1
• Molecular Formula: C15H21NO3S
• Molecular Weight: 295.403
• Mol File: 118546-67-1.mol
• Article Data: 6

Chemical Properties

• CAS DataBase Reference: Carbamic acid, [(1R)-1-formyl-2-[(phenylmethyl)thio]ethyl]-, 1,1-dimethylethyl ester(CAS DataBase Reference)
• NIST Chemistry Reference: Carbamic acid, [(1R)-1-formyl-2-[(phenylmethyl)thio]ethyl]-, 1,1-dimethylethyl ester(118546-67-1)
• EPA Substance Registry System: Carbamic acid, [(1R)-1-formyl-2-[(phenylmethyl)thio]ethyl]-, 1,1-dimethylethyl ester(118546-67-1)

Safety Data

• Hazardous Substances Data: 118546-67-1(Hazardous Substances Data)

Upstream product

• 100-39-0 benzyl bromide 
• 3054-01-1 S-benzyl-L-cysteine 
• 5068-28-0 (2R)-3-benzylsulfanyl-2-tert-butoxycarbonylamino-propionic acid 
• 208521-21-5 S-Benzyl-N_α-(tert-butyloxycarbonyl)-cysteine-N-methoxy-N-methylamide 
• 139428-96-9 N-tert-butoxycarbonyl-S-benzyl-(R)-cysteinol 

Downstream Products

• 619328-41-5 (3R)-4-benzylthio-3-(N-tert-butyloxycarbonyl)amino-1-butene 
• 879219-18-8 [1-benzylsulfanylmethyl-2-(5-fluoro-2,3-dihydro-indol-1-yl)-ethyl]-carbamic acid tert-butyl ester 

Relevant articles and documents

Design and Synthesis of Activity-Based Probes and Inhibitors for Bleomycin Hydrolase

Summary Bleomycin hydrolase (BLMH) is a neutral cysteine aminopeptidase that has been ascribed roles in many physiological and pathological processes, yet its primary biological function remains enigmatic. In this work, we describe the results of screening of a library of fluorogenic substrates to identify non-natural amino acids that are optimally recognized by BLMH. This screen identified several substrates with kcat/KM values that are substantially improved over the previously reported fluorogenic substrates for this enzyme. The substrate sequences were used to design activity-based probes that showed potent labeling of recombinant BLMH as well as endogenously expressed BLMH in cell extracts, and in intact cells. Importantly, we identify potent BLMH inhibitors that are able to fully inhibit endogenous BLMH activity in intact cells. These probes and inhibitors will be valuable new reagents to study BLMH function in cellular and animal models of human diseases where BLMH is likely to be involved.

Arylaminoethyl amides as noncovalent inhibitors of cathepsin S. Part 2: Optimization of P1 and N-aryl

A systematic study of anilines led to the discovery of a metabolically robust fluoroindoline replacement for the alkoxy aniline toxicophore in 1. Investigations of the P1 pocket resulted in the discovery of a wide tolerance of functionality leading to the discovery of 11 as a potent and selective inhibitor of cathepsin S.

Total synthesis and biological evaluation of (+)-kalkitoxin, a cytotoxic metabolite of the cyanobacterium Lyngbya majuscula

(+)-Kalkitoxin, a metabolite of the marine cyanobacterium Lyngbya majuscula, was synthesized from (R)-2-methylbutyric acid, (R)-cysteine, and (3S, 4S, 6S)-3,4,6-trimethyl-8-(methylamino)octanoic acid. A key step in the synthesis was installation of the anti,anti methyl stereotriad by means of a tandem asymmetric conjugate addition of an organocopper species to an α,β-unsaturated N-acyl oxazolidin-2-one followed in situ by α-methylation of the resultant enolate. The thiazoline portion of kalkitoxin was assembled by titanium tetrachloride catalyzed cyclization of a vinyl substituted amido thiol.