5960-12-3 Usage
Description
Cylohexanecarboxyl-coenzyme A, also known as cyclohexane-1-carboxyl-CoA, is an acyl-CoA compound that is formed through the formal condensation of the thiol group of coenzyme A with the carboxy group of cyclohexane-1-carboxylic acid. It plays a crucial role in various biochemical processes and serves as an intermediate in the metabolism of certain compounds.
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.
Check Digit Verification of cas no
The CAS Registry Mumber 5960-12-3 includes 7 digits separated into 3 groups by hyphens. The first part of the number,starting from the left, has 4 digits, 5,9,6 and 0 respectively; the second part has 2 digits, 1 and 2 respectively.
Calculate Digit Verification of CAS Registry Number 5960-12:
(6*5)+(5*9)+(4*6)+(3*0)+(2*1)+(1*2)=103
103 % 10 = 3
So 5960-12-3 is a valid CAS Registry Number.
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
5960-12-3Relevant articles and documents
Reversible biological birch reduction at an extremely low redox potential
Kung, Johannes W.,Baumann, Sven,Von Bergen, Martin,Mueller, Michael,Hagedoorn, Peter-Leon,Hagen, Wilfred R.,Boll, Matthias
scheme or table, p. 9850 - 9856 (2010/09/06)
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.
