4752-33-4

Basic information

• Product Name: valeryl-coenzyme A
• Synonyms: valeryl-coenzyme A;Adenosine 3'-phosphoric acid 5'-[diphosphoric acid P2-[2,2-dimethyl-3-hydroxy-3-[[2-[[2-(valerylthio)ethyl]aminocarbonyl]ethyl]aminocarbonyl]propyl]] ester;Valeryl CoA;pentanoyl-CoA
• CAS NO: 4752-33-4
• Molecular Formula: C₂₆H₄₄N₇O₁₇P₃S
• Molecular Weight: 851.65
• Mol File: 4752-33-4.mol
• Article Data: 10

Chemical Properties

• Appearance: /
• CAS DataBase Reference: valeryl-coenzyme A(CAS DataBase Reference)
• NIST Chemistry Reference: valeryl-coenzyme A(4752-33-4)
• EPA Substance Registry System: valeryl-coenzyme A(4752-33-4)

Safety Data

• Hazardous Substances Data: 4752-33-4(Hazardous Substances Data)

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.

Upstream product

• 52580-14-0 pentenoyl-CoA 
• 626-98-2 pent-2-enoic acid 
• 110-62-3 pentanal 
• 85-61-0 coenzyme A 
• 109-52-4 valeric acid 
• 2082-59-9 pentanoic anhydride 

Downstream Products

• 85-61-0 coenzyme A 

Relevant articles and documents

Identification of an α-Oxoamine Synthase and a One-Pot Two-Step Enzymatic Synthesis of α-Amino Ketones

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.

Structural Mechanism of Regioselectivity in an Unusual Bacterial Acyl-CoA Dehydrogenase

Terminal alkenes are easily derivatized, making them desirable functional group targets for polyketide synthase (PKS) engineering. However, they are rarely encountered in natural PKS systems. One mechanism for terminal alkene formation in PKSs is through the activity of an acyl-CoA dehydrogenase (ACAD). Herein, we use biochemical and structural analysis to understand the mechanism of terminal alkene formation catalyzed by an ?,?-ACAD from the biosynthesis of the polyketide natural product FK506, TcsD. While TcsD is homologous to canonical α,β-ACADs, it acts regioselectively at the ?,?-position and only on α,β-unsaturated substrates. Furthermore, this regioselectivity is controlled by a combination of bulky residues in the active site and a lateral shift in the positioning of the FAD cofactor within the enzyme. Substrate modeling suggests that TcsD utilizes a novel set of hydrogen bond donors for substrate activation and positioning, preventing dehydrogenation at the α,β position of substrates. From the structural and biochemical characterization of TcsD, key residues that contribute to regioselectivity and are unique to the protein family were determined and used to identify other putative ?,?-ACADs that belong to diverse natural product biosynthetic gene clusters. These predictions are supported by the demonstration that a phylogenetically distant homologue of TcsD also regioselectively oxidizes α,β-unsaturated substrates. This work exemplifies a powerful approach to understand unique enzymatic reactions and will facilitate future enzyme discovery, inform enzyme engineering, and aid natural product characterization efforts.

A HOST CELL MODIFIED TO PRODUCE LACTAMS

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.