5960-12-3

Usage

Uses

Used in Pharmaceutical Industry:
Cylohexanecarboxyl-coenzyme A is used as an intermediate in the synthesis of various pharmaceutical compounds, particularly those related to the treatment of certain diseases. Its unique structure allows for the development of novel drugs with potential therapeutic applications.
Used in Biochemical Research:
In the field of biochemistry, cyclohexanecarboxyl-coenzyme A is used as a research tool to study the mechanisms of enzyme-catalyzed reactions and the role of coenzyme A in cellular metabolism. This helps researchers understand the complex interactions between different biomolecules and their functions within the cell.
Used in Chemical Synthesis:
Cylohexanecarboxyl-coenzyme A is also utilized in chemical synthesis, particularly in the production of specialty chemicals and materials. Its unique properties make it a valuable building block for the creation of new compounds with specific applications in various industries.
Used in Environmental Applications:
In the environmental sector, cyclohexanecarboxyl-coenzyme A can be employed in the biodegradation of certain pollutants and contaminants. Its ability to act as an intermediate in metabolic pathways makes it a potential candidate for the development of bioremediation strategies to clean up contaminated sites.
Used in Analytical Chemistry:
As an analytical reagent, cyclohexanecarboxyl-coenzyme A can be used to develop new methods for the detection and quantification of specific compounds in complex samples. Its unique chemical properties make it a valuable tool for researchers in the field of analytical chemistry.

InChI:InChI=1/C28H46N7O17P3S/c1-28(2,22(38)25(39)31-9-8-18(36)30-10-11-56-27(40)16-6-4-3-5-7-16)13-49-55(46,47)52-54(44,45)48-12-17-21(51-53(41,42)43)20(37)26(50-17)35-15-34-19-23(29)32-14-33-24(19)35/h14-17,20-22,26,37-38H,3-13H2,1-2H3,(H,30,36)(H,31,39)(H,44,45)(H,46,47)(H2,29,32,33)(H2,41,42,43)/t17-,20-,21-,22+,26-/m1/s1

Upstream product

• 6420-00-4 cyclohex-1-ene-1-carboxyl-CoA 
• 6756-74-7 S-benzoyl coenzyme A 

Relevant academic research and scientific papers

Reversible biological birch reduction at an extremely low redox potential

The Birch reduction of aromatic rings to cyclohexadiene compounds is widely used in chemical synthesis and requires solvated electrons, the most potent reductants known in organic chemistry. Benzoyl-coenzyme A (CoA) reductases (BCR) are key enzymes in the anaerobic bacterial degradation of aromatic compounds and catalyze an analogous reaction under physiological conditions. Class I BCRs are FeS enzymes and couple the reductive dearomatization of benzoyl-CoA to cyclohexa-1,5-diene-1-carboxyl-CoA (dienoyl-CoA) to a stoichiometric ATP hydrolysis. Here, we report on a tungsten-containing class II BCR from Geobacter metallireducens that catalyzed the fully reversible, ATP-independent dearomatization of benzoyl-CoA to dienoyl-CoA. BCR additionally catalyzed the disproportionation of dienoyl-CoA to benzoyl-CoA/monoenoyl-CoA and the four- and six-electron reduction of benzoyl-CoA in the presence of a reduced low-potential bridged 2,2′-bipyridyl redox dye. Reversible redox titration experiments in the presence of this redox dye revealed a midpoint potential of E0′= -622 mV for the benzoyl-CoA/dienoyl-CoA couple, which is far below the values of other known reversible substrate/product redox couples in enzymology. This work demonstrates the efficiency of reversible metalloenzyme catalysis, which in chemical synthesis can only be achieved under essentially irreversible conditions.

Point mutations (Q19P and N23K) increase the operational solubility of a 2α-o-benzoyltransferase that conveys various acyl groups from CoA to a taxane acceptor

Two site-directed mutations within the wild-type 2-o-benzoyltransferase (tbf) cDNA, from Taxus cuspidata plants, yielded an encoded protein containing replacement amino acids at Q19P and N23K that map to a solvent-exposed loop region. The likely significant changes in the biophysical, properties invoked by these mutations caused the overexpressed, modified TBT (mTBT) to partition into the soluble enzyme fraction about 5-fold greater than the wild-type enzyme. Sufficient protein could now be acquired to examine the scope of the substrate specificity of mTBT by incubation with 7,13-O,O-diacetyl-2-Odebenzoylbaccatin III that was mixed individually with various substituted benzoyls, alkanoyls, and (E)-butenoyl CoA donors. The mTBT catalyzed the conversion of each 7,13-O,O-diacetyl-2-O-debenzoylbaccatin III to several 7,13-O,O-diacetyl-2O- acyl-2-O-debenzoylbaeeatin III analogues. The relative catalytic efficiency of mTBT with the 7,13-O,O-diacetyl-2-Odebenzoyl surrogate substrate and heterole carbonyl CoA substrates was slightly greater than with the natural aroyl substrate benzoyl CoA, while substituted benzoyl CoA thioesters were less productive. Short-chain hydrocarbon carbonyl and cyclohexanoyl CoA thioesters were also productive, where C4 substrates were transferred by mTBT with ～10- to 17-fold greater catalytic efficiency compared to the transfer of benzoyl. The described broad specificity of mTBT suggests that a plethora of 2-O-acyl variants of the antimitotic paclitaxel can be assembled through biocatalytic sequences.