35161-20-7

Usage

Uses

Used in Fragrance Industry:
4-isopropyl-4-methylcyclohexanone is used as a fragrance ingredient for its distinctive scent, contributing to the formulation of various personal care products and perfumes.
Used in Pharmaceutical Industry:
4-isopropyl-4-Methylcyclohexanone serves as a building block in the production of pharmaceuticals, playing a crucial role in the synthesis of diverse medicinal agents.
Used in Agrochemical Industry:
4-isopropyl-4-methylcyclohexanone is utilized in the development of agrochemicals, which are essential for enhancing crop protection and yield.
Used as a Solvent in Chemical Reactions:
It is employed as a solvent in various chemical processes, facilitating reactions that require a suitable dissolving medium.
Used in Organic Synthesis:
4-isopropyl-4-methylcyclohexanone has potential applications in the synthesis of organic compounds, which can be further utilized in different chemical and industrial applications.
Used in Food Industry:
It also functions as a flavoring agent in the food industry, enhancing the taste and aroma of various food products.
However, it is important to handle 4-isopropyl-4-methylcyclohexanone with caution due to its potential harmful effects if ingested or inhaled, and its ability to cause skin and eye irritation.

Upstream product

• 35161-12-7 4-Isopropyl-4-methyl-cyclohex-2-enone 

Relevant academic research and scientific papers

Investigating: Saccharomyces cerevisiae alkene reductase OYE 3 by substrate profiling, X-ray crystallography and computational methods

Saccharomyces cerevisiae OYE 3 shares 80% sequence identity with the well-studied Saccharomyces pastorianus OYE 1; however, wild-type OYE 3 shows different stereoselectivities toward some alkene substrates. Site-saturation mutagenesis of Trp 116 in OYE 3 followed by substrate profiling showed that the mutations had relatively little effect, opposite to that observed previously for OYE 1. The X-ray crystal structures of unliganded and phenol-bound OYE 3 were solved to 1.8 and 1.9 ? resolution, respectively. Both structures were nearly identical to that of OYE 1, with only a single amino acid difference in the active site region (Ser 296 versus Phe 296, part of loop 6). Despite their essentially identical static X-ray structures, molecular dynamics (MD) simulations revealed that loop 6 conformations differed significantly in solution between OYE 3 and OYE 1. In OYE 3, loop 6 remained nearly as open as observed in the crystal structure; by contrast, loop 6 closed over the active site of OYE 1 by ca. 4 ?. Loop closure likely generates a greater number of active site protein contacts for substrate bound to OYE 1 as compared to OYE 3. These differences provide an explanation for the differing stereoselectivities of OYE 3 and OYE 1, despite their nearly identical X-ray crystal structures.