4752-33-4 Usage
Description
Valeryl-coenzyme A, also known as pentanoyl-CoA, is a short-chain fatty acyl-CoA that is formed through the formal condensation of the thiol group of coenzyme A with the carboxy group of pentanoic acid. It plays a crucial role in various biochemical processes and serves as an important intermediate in the metabolism of certain compounds.
Uses
Used in Pharmaceutical Industry:
Valeryl-coenzyme A is used as an intermediate in the synthesis of various pharmaceutical compounds, particularly those derived from pentanoic acid. Its unique structure allows for the development of novel drugs with potential applications in treating a range of medical conditions.
Used in Biochemical Research:
In the field of biochemistry, valeryl-coenzyme A is utilized as a research tool to study the mechanisms of fatty acid metabolism and the role of coenzyme A in various enzymatic reactions. This knowledge can contribute to a better understanding of metabolic pathways and the development of targeted therapies for metabolic disorders.
Used in Chemical Synthesis:
Valeryl-coenzyme A can be employed as a building block in the chemical synthesis of complex organic molecules, such as natural products and bioactive compounds. Its unique structure and reactivity make it a valuable starting material for the development of new chemical entities with potential applications in various industries, including pharmaceuticals, agrochemicals, and materials science.
Used in Enzyme Assays:
In the development of enzyme assays, valeryl-coenzyme A can be used as a substrate to study the activity of enzymes involved in fatty acid metabolism, such as acyl-CoA dehydrogenases and acyl-CoA synthetases. These assays can help researchers investigate the function of these enzymes and their role in various metabolic pathways, as well as identify potential targets for therapeutic intervention.
Used in Metabolic Engineering:
Valeryl-coenzyme A can be employed in metabolic engineering efforts to enhance the production of specific compounds in microorganisms or cell cultures. By modifying the expression of genes involved in fatty acid metabolism, researchers can increase the yield of desired products, such as biofuels, pharmaceuticals, or specialty chemicals.
Check Digit Verification of cas no
The CAS Registry Mumber 4752-33-4 includes 7 digits separated into 3 groups by hyphens. The first part of the number,starting from the left, has 4 digits, 4,7,5 and 2 respectively; the second part has 2 digits, 3 and 3 respectively.
Calculate Digit Verification of CAS Registry Number 4752-33:
(6*4)+(5*7)+(4*5)+(3*2)+(2*3)+(1*3)=94
94 % 10 = 4
So 4752-33-4 is a valid CAS Registry Number.
4752-33-4Relevant articles and documents
Identification of an α-Oxoamine Synthase and a One-Pot Two-Step Enzymatic Synthesis of α-Amino Ketones
Zhou, Ting,Gao, Du,Li, Jia-Xin,Xu, Min-Juan,Xu, Jun
supporting information, p. 37 - 41 (2020/12/21)
Alb29, an α-oxoamine synthase involved in albogrisin biosynthesis in Streptomyces albogriseolus MGR072, was characterized and responsible for the incorporation of l-glutamate to acyl-coenzyme A substrates. Combined with Alb29 and Mgr36 (an acyl-coenzyme A ligase), a one-pot enzymatic system was established to synthesize seven α-amino ketones. When these α-amino ketones were fed into the alb29 knockout strain Δalb29, respectively, the albogrisin analogs with different side chains were observed.
ATP Regeneration System in Chemoenzymatic Amide Bond Formation with Thermophilic CoA Ligase
Lelièvre, Chloé M.,Balandras, Mélanie,Petit, Jean-Louis,Vergne-Vaxelaire, Carine,Zaparucha, Anne
, p. 1184 - 1189 (2020/01/22)
CoA ligases are enzymes catalyzing the ATP-dependent addition of coenzyme A to carboxylic acids in two steps through an adenylate intermediate. This intermediate can be diverted by a nucleophilic non enzymatic addition of amine to get the corresponding amide for synthetic purposes. To this end, we selected thermophilic CoA ligases to study the conversion of various carboxylic acids into their amide counterparts. To limit the use of ATP, we implemented an ATP regeneration system combining polyphosphate kinase 2 (PPK2 Class III) and inorganic pyrophosphatase. Suitability of this system was illustrated by the lab-scale chemoenzymatic synthesis of N-methylbutyrylamide in 77 % yield using low enzyme loading and 5 % molar ATP.
A HOST CELL MODIFIED TO PRODUCE LACTAMS
-
Paragraph 0097-0098; 00109, (2018/01/15)
The present invention provides for a genetically modified host cell capable of producing a lactam comprising a 2-pyrrolidone synthase, or an enzymatically active fragment thereof, heterologous to the host cell.
