91133-15-2

Usage

Uses

Used in Pharmaceutical Industry:
N-(2-Mercaptoethyl)-acetamide benzoate is used as a chelating agent for metal ions, which can be beneficial in treating metal poisoning or managing metal-related health conditions. Its ability to bind with metal ions can help in detoxification processes and prevent metal-induced cellular damage.
N-(2-Mercaptoethyl)-acetamide benzoate is also used as a potential protective agent against oxidative stress. The thiol group in its structure can act as an antioxidant, neutralizing free radicals and reducing oxidative damage to cells and tissues. This property can be valuable in the development of drugs targeting various diseases associated with oxidative stress, such as neurodegenerative disorders and aging.
Used in Organic Synthesis:
Due to its thiol and amide functional groups, N-(2-Mercaptoethyl)-acetamide benzoate may have applications in the synthesis of organic compounds. These functional groups can participate in various chemical reactions, such as nucleophilic substitution, addition, and condensation reactions, making it a versatile building block for the creation of new organic molecules with potential applications in different industries.
However, it is important to note that further research is needed to fully understand the potential uses and properties of N-(2-Mercaptoethyl)-acetamide benzoate, as well as to optimize its synthesis and application methods for various industries.

InChI:InChI=1/C11H13NO2S/c1-9(13)12-7-8-15-11(14)10-5-3-2-4-6-10/h2-6H,7-8H2,1H3,(H,12,13)

Upstream product

• 1190-73-4 2-(acetylamino)ethanethiol 
• 98-88-4 benzoyl chloride 
• 2722-34-1 2-phenylthiazoline 
• 108-24-7 acetic anhydride 
• 65-85-0 benzoic acid 

Downstream Products

• 20851-38-1 4-hydroxy-6-(2-oxo-2-phenylethyl)-2H-pyran-2-one 
• 5526-38-5 4-hydroxy-6-phenyl-2H-pyran-2-one 
• 1443502-35-9 urauchimycin B 

Relevant academic research and scientific papers

Characterization of AntB, a promiscuous acyltransferase involved in antimycin biosynthesis

The in vivo and in vitro characterization of AntB, a dedicated acyltransferase encoded in the antimycin biosynthetic gene cluster, which catalyzes the C-8 acyloxy formation is reported. It is demonstrated that AntB has broad substrate specificity toward both the acyl substrate and the acyl carrier and produces more antimycin analogues with varying C-8 acyloxy moieties.

A mechanism-based fluorescence transfer assay for examining ketosynthase selectivity

Since their discovery, polyketide synthases have received massive attention from researchers hoping to harness their potential as a platform for generating new and improved therapeutics. Despite significant strides toward this end, inherent specificities within the enzymes responsible for polyketide production have severely limited these efforts. We have developed a mechanism-based, fluorescence transfer assay for a key enzyme component of all polyketide synthases, the ketosynthase domain. As demonstrated, this method can be used with both ketosynthase-containing didomains and full modules. As proof of principle, the ketosynthase domain from module 6 of the 6-deoxyerythronolide synthase is examined for its ability to accept a variety of simple thioester substrates. Consistent with its natural hexaketide substrate, we find that this ketosynthase prefers longer, α-branched thioesters and its ability to distinguish these structural features is quite remarkable. Substrate electronics are also tested via a variety of p-substituted aromatic groups. In all, we expect this technique to find considerable use in the field of polyketide biosynthesis and engineering due to its extraordinary simplicity and very distinct visible readout.

Unnatural polyketide analogues selectively target the her signaling pathway in human breast cancer cells

Receptor tyrosine kinases are critical targets for the regulation of cell survival. Cancer patients with abnormal receptor tyrosine kinases (RTK) tend to have more aggressive disease with poor clinical outcomes. As a result, human epidermal growth factor

In vitro precursor-directed synthesis of polyketide analogues with coenzyme a regeneration for the development of antiangiogenic agents

Polyketide analogues are produced via in vitro reconstruction of a precursor-directed polyketide biosynthetic pathway. Malonyl-CoA synthetase (MCS) was used in conjunction with chalcone synthase (CHS), thereby allowing efficient use of synthetic starter molecules and malonate as extender. Coenzyme-A was recycled up to 50 times. The use of a simple immobilization procedure resulted in up to a 30-fold higher yield of pyrone CHS products than that obtained with the free enzyme solutions.

Antiparasitic agents

Antiparasitic compound of formula (I): STR1 The broken line at the 22-23 position representing an optional double bond and either R1 is a H or OH and the double bond is absent or the double bond is present and R1 is absent; R2 is optionally substituted phenyl, or a group of formula (II): STR2 wherein X is O, S or --CH2 --, abc and d are 0-2 and a+b+c+d≤5 R3 is H or Me R4 is H, OH or 4'-(alpha-L-oleandrosyl)-alpha-L-oleandrosyloxy. The compounds are prepared by fermentation of Streptomyces avermitilis in the presence of an N-alkanoyl cysteamine thioester containing R2.