35155-49-8

Upstream product

• 85997-72-4 4-ethyl-4-methyl-heptanedioic acid 
• 17429-32-2 4-ethyl-4-methyl-2-cyclohexene-1-one 
• 676560-15-9 Ethyl (cis/trans)-4-<(tert-butyldimethylsilyl)oxy>cyclohexanecarboxylate 
• 1557246-87-3 8-ethyl-8-methyl-1,4-dioxaspiro[4.5]decane 
• 1557246-84-0 (8-ethyl-1,4-dioxaspiro[4.5]decan-8-yl)methyl-4-methylbenzenesulfonate 
• 1207111-65-6 (8-ethyl-1,4-dioxaspiro[4.5]decan-8-yl)methanol 
• 1557246-79-3 methyl 8-ethyl-1,4-dioxaspiro[4.5]decane-8-carboxylate 
• 26845-47-6 methyl 1,4-dioxaspiro[4.5]decane-8-carboxylate 
• 96-17-3 2-Methylbutyraldehyde 
• 4111-01-7 4-methyl-4-vinylcyclohexan-1-one 
• 105519-85-5 5-ethyl-5-methyl-2-oxo-cyclohexanecarboxylic acid ethyl ester 
• 19830-09-2 4-acetyl-4-methyl-heptanedioic acid 

Downstream Products

• 1393645-38-9 C₁₁H₂₀O₂ 
• 1393645-34-5 C₁₁H₁₈O₂ 
• 1393645-35-6 C₁₀H₁₆O 
• 1393645-33-4 C₁₀H₁₆O₂ 
• 49576-83-2 Bis-2-(4-methyl-4-ethylcyclohexa-2,5-dienyl)-diselenid 
• 51319-09-6 4-Ethyl-4-methyl-2,5-cyclohexadien-1-on 
• 15509-58-7 1,1-Difluor-4-methyl-4-ethyl-cyclohexan 
• 108153-30-6 4-ethyl-2,6-dibromo-4-methyl-cyclohexanone 

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.

OXYSTEROLS AND METHODS OF USE THEREOF

Compounds are provided according to Formula (I): and pharmaceutically acceptable salts thereof, and pharmaceutical compositions thereof; wherein R2, R3, R4, R5, and and R6 are as defined herein. Compounds of the present invention are contemplated useful for the prevention and treatment of a variety of conditions.

Pichia stipitis OYE 2.6 variants with improved catalytic efficiencies from site-saturation mutagenesis libraries

An earlier directed evolution project using alkene reductase OYE 2.6 from Pichia stipitis yielded 13 active site variants with improved properties toward three homologous Baylis-Hillman adducts. Here, we probed the generality of these improvements by testing the wild-type and all 13 variants against a panel of 16 structurally-diverse electron-deficient alkenes. Several substrates were sterically demanding, and as hoped, creating additional active site volume yielded better conversions for these alkenes. The most impressive improvement was found for 2-butylidenecyclohexanone. The wild-type provided less than 20% conversion after 24 h; a triple mutant afforded more than 60% conversion in the same time period. Moreover, even wild-type OYE 2.6 can reduce cyclohexenones with very bulky 4-substituents efficiently.

PYRAZOLE CARBOXAMIDE COMPOUNDS, COMPOSITIONS AND METHODS OF USE

Provided herein are compounds of formula (AA): N N H HN O N N R R 6 A (R a ) p, (AA) stereoisomers or a pharmaceutically acceptable salt thereof, wherein A, R a, p, R and R 6 are defined herein, compositions including the compounds and methods of manufacturing and using the compounds for the treatment of diseases.

Asymmetric Baeyer - Villiger oxidations of 4-mono- and 4,4-disubstituted cyclohexanones by whole cells of engineered Escherichia coli

Whole cells of an Escherichia coli strain that overexpresses Acinetobacter sp. NCIB 9871 cyclohexanone monooxygenase have been used for the Baeyer-Villiger oxidations of a variety of 4-mono- and 4,4-disubstituted cyclohexanones. In cases where comparisons were possible, this new biocatalytic reagent provided lactones with chemical yields and optical purities that were comparable to those obtained from the purified enzyme or a strain of bakers' yeast that expresses the same enzyme. The efficient production of cyclohexanone monooxygenase in the E. coli expression system (ca. 30% of total soluble protein) allowed these oxidations to reach completion in approximately half the time required for the engineered bakers' yeast strain. Surprisingly, 4,4-disubstituted cyclohexanones were also accepted by the enzyme, and the enantioselectivities of these oxidations could be rationalized by considering the conformational energies of bound substrates along with the enzyme's intrinsic enantioselectivity. The enzyme expressed in E. coli cells also oxidized several 4-substituted cyclohexanones bearing polar substituents, often with high enantioselectivities. In the case of 4-iodocyclohexanone, the lactone was obtained in > 98% ee and its absolute configuration was assigned by X-ray crystallography. The crystal belongs to the monoclinic P21 space group with a = 5.7400(10), b = 6.1650(10), c = 11.377(2) A, b = 99.98(2)°, and Z = 2. Taken together, these results demonstrate the utility of an engineered bacterial strain in delivering useful chiral building blocks in an experimentally simple manner.