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

Definition

ChEBI: A short-chain fatty acyl-CoA that results from the formal condensation of the thiol group of coenzyme A with the carboxy group of pentanoic acid.

Upstream product

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

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.

ATP Regeneration System in Chemoenzymatic Amide Bond Formation with Thermophilic CoA Ligase

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

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.