117411-09-3

Basic information

• Product Name: phenylpropionyl-coenzyme A
• Synonyms: phenylpropionyl-coenzyme A;3-phenylpropanoyl-CoA
• CAS NO: 117411-09-3
• Molecular Formula: C₃₀H₄₄N₇O₁₇P₃S
• Molecular Weight: 899.693343
• Mol File: 117411-09-3.mol
• Article Data: 9

Chemical Properties

• Appearance: /
• Density: 1.76g/cm³
• Refractive Index: 1.702
• CAS DataBase Reference: phenylpropionyl-coenzyme A(CAS DataBase Reference)
• NIST Chemistry Reference: phenylpropionyl-coenzyme A(117411-09-3)
• EPA Substance Registry System: phenylpropionyl-coenzyme A(117411-09-3)

Safety Data

• Hazardous Substances Data: 117411-09-3(Hazardous Substances Data)

Usage

Description

Phenylpropionyl-coenzyme A, also known as 3-phenylpropanoyl-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 3-phenylpropanoic acid. This molecule plays a crucial role in various biochemical processes and has potential applications in different industries.

Uses

Used in Pharmaceutical Industry:
Phenylpropionyl-coenzyme A is used as an intermediate in the synthesis of various pharmaceutical compounds, particularly those related to the treatment of neurological disorders and other conditions. Its unique structure allows for the development of novel drugs with potential therapeutic benefits.
Used in Chemical Synthesis:
In the chemical industry, phenylpropionyl-coenzyme A serves as a key building block for the synthesis of a wide range of organic compounds, including specialty chemicals, agrochemicals, and advanced materials. Its versatility in chemical reactions makes it a valuable asset in the development of new products and technologies.
Used in Research and Development:
Phenylpropionyl-coenzyme A is utilized as a research tool in the study of various biological processes and pathways. Its involvement in cellular metabolism and energy production makes it an important molecule for understanding the underlying mechanisms of various diseases and conditions. Additionally, it can be used to develop new diagnostic tools and methods for monitoring disease progression.
Used in Drug Delivery Systems:
Similar to gallotannin, phenylpropionyl-coenzyme A can be incorporated into drug delivery systems to improve the bioavailability and therapeutic outcomes of various pharmaceutical compounds. Its unique properties allow for the development of novel drug carriers and targeted delivery methods, enhancing the efficacy of existing treatments and potentially reducing side effects.

InChI:InChI=1/C30H44N7O17P3S/c1-30(2,25(41)28(42)33-11-10-20(38)32-12-13-58-21(39)9-8-18-6-4-3-5-7-18)15-51-57(48,49)54-56(46,47)50-14-19-24(53-55(43,44)45)23(40)29(52-19)37-17-36-22-26(31)34-16-35-27(22)37/h3-7,16-17,19,23-25,29,40-41H,8-15H2,1-2H3,(H,32,38)(H,33,42)(H,46,47)(H,48,49)(H2,31,34,35)(H2,43,44,45)/t19-,23-,24-,25+,29-/m1/s1

Upstream product

• 501-52-0 3-Phenylpropionic acid 
• 85-61-0 coenzyme A 
• 29679-58-1 Fenoprofen 
• 229171-29-3 L-phenylalanoyl-CoA 
• 621-82-9 Cinnamic acid 
• 57830-63-4 S-(4-Methylphenyl)-thiocinnamat 
• 30801-99-1 cinnamoyl-CoA 
• 124-38-9 carbon dioxide 
• 108761-28-0 (carbonic acid ethyl ester)-cinnamic acid-anhydride 

Relevant articles and documents

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.

METHOD FOR SYNTHESISING AMIDES

The present invention relates to a method for synthesising amides that is of general applicability. The method may be performed in vitro or in vivo. Cell lines for use in the in vivo methods also form aspects of the invention. The method for synthesising a non-natural amide comprises: a. reaction of a carboxylic acid with a naturally occurring CoA ligase or a variant thereof; and b. reaction of the product of step a with an amine in the presence of a naturally occurring acyltransferase or a variant thereof; with the proviso that where the CoA ligase and acyltransferase are both naturally occurring, they are not derived from the same source species and do not act sequentially in a metabolic pathway; and with the proviso that the non-natural product is not N-(E)-p-coumaroyl-3-hydroxyanthranilic acid or N-(E)-p-caffeoyl-3-hydroxyanthranilic acid. Further, a method for producing an active pharmaceutical ingredient by the aforementioned method and host cells for carrying out said methods are envisaged.

Screening and Engineering the Synthetic Potential of Carboxylating Reductases from Central Metabolism and Polyketide Biosynthesis

Carboxylating enoyl-thioester reductases (ECRs) are a recently discovered class of enzymes. They catalyze the highly efficient addition of CO2 to the double bond of α,β-unsaturated CoA-thioesters and serve two biological functions. In primary metabolism of many bacteria they produce ethylmalonyl-CoA during assimilation of the central metabolite acetyl-CoA. In secondary metabolism they provide distinct α-carboxyl-acyl-thioesters to vary the backbone of numerous polyketide natural products. Different ECRs were systematically assessed with a diverse library of potential substrates. We identified three active site residues that distinguish ECRs restricted to C4 and C5-enoyl-CoAs from highly promiscuous ECRs and successfully engineered a selected ECR as proof-of-principle. This study defines the molecular basis of ECR reactivity, allowing for predicting and manipulating a key reaction in natural product diversification.