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Coenzyme A

Catalog No. Name Structure M.W. Purity
In stock BPG-3099 20:5 Coenzyme A ammonium salt
1246522-05-3 - Chemical Structure
1103.06 >99%
In stock BPG-3098 18:1 Ether Coenzyme A Ammonium salt
2260670-62-8 - Chemical Structure
1068.46 >99%
In stock BPG-3097 17:1 (n7) Coenzyme A ammonium salt
1246304-40-4 - Chemical Structure
1068.43 >99%
In stock BPG-3096 18:2 (n6) Coenzyme A ammonium salt
1246304-39-1 - Chemical Structure
1081.06 >99%
In stock BPG-3095 18:3 (n6) Coenzyme A
27843-61-4 - Chemical Structure
1078.41 >99%
In stock BPG-3094 18:3 (n3) Coenzyme A ammonium salt
13673-87-5 - Chemical Structure
1078.41 >99%
In stock BPG-3093 18:1 (n12) Coenzyme A (ammonium salt)
70954-87-9 - Chemical Structure
1083.07 >99%

Background

BOC Sciences offers our customers a wide range of coenzyme A products, you can find the right product for your project development in our list. Coenzyme A can activate the metabolism of substances, enhance the oxidation of substances in the body and supply energy. Coenzyme A is the main active form of pantothenic acid in living organisms and is formed by 3',5'-ADP linked to 4-phosphopantothenyl-β-mercaptoethylamine by a phosphoric anhydride bond. Coenzyme A contains active sulfhydryl groups that can combine with acyl groups to form sulfolipids, and thus can serve as a coenzyme for acyltransferases, which play a role in transferring acyl groups in the metabolism of sugars, proteins, lipids, and other metabolic processes.

Schematic diagram of the CoA biosynthetic pathway Fig. 1. Schematic diagram of the CoA biosynthetic pathway (BBA advances. 2023, 3: 100075).

Coenzyme A Structure

Adenosine diphosphate - Adenosine diphosphate is the nucleotide portion of coenzyme A and consists of adenine and diphosphate groups. It is attached to the nucleotide structure of coenzyme A to provide energy and stability.

Pantothenic acid (PA) - PA is the truncated portion of coenzyme A, also known as bitartrate. It consists of a chain containing five carbon atoms and an acyl group (thiol group). The acyl group is the active part of coenzyme A and is involved in metabolic reactions by being attached to other molecules through ester bonds.

Choline - Choline is the choline ester portion of coenzyme A and is attached to PA by a phosphodiester bond. Choline plays a supporting and stabilizing role in the structure of coenzyme A.

Biosynthesis of Coenzyme A

As an important cofactor in various fields, coenzyme A has a wide range of applications with the reconstruction of the coenzyme A biosynthetic pathway and the resolution of the structure and function of key enzymes in the synthetic pathway.

Coenzyme A Function

As a cofactor, coenzyme A participates in several enzymatic reactions, regulates cellular metabolic processes, and maintains normal cellular function and energy supply.

Formation of Acetyl Coenzyme A

Coenzyme A combines with acetylase to form acetyl coenzyme A. Through the acetylation reaction, acetyl coenzyme A is able to transfer acetyl groups to other molecules, thus affecting metabolic processes.

Tricarboxylic Acid Cycle

Coenzyme A participates in the tricarboxylic acid cycle (also known as the Krebs cycle or the citric acid cycle) by translocating acetyl coenzyme A into the cycle reactions that produce energy and provide intermediates.

Lipid Metabolism

Coenzyme A is involved in the synthesis of fatty acids by transferring the acetyl group to the carboxyl group of long-chain fatty acids to form fatty acyl coenzyme A. Coenzyme A is also involved in the beta-oxidation of fatty acids, which breaks down fatty acyl coenzyme A into acetyl coenzyme A and generates energy.

BOC Sciences plays a vital role in providing high-quality coenzyme A to support cutting edge research and development in the biotechnology and pharmaceutical industries, if you are interested in our lipid synthesis and lipid analysis, please get in touch with us.

Reference

  1. Filonenko, V. et al. Discovery and functional characterisation of protein CoAlation and the antioxidant function of coenzyme A. BBA advances. 2023, 3: 100075.

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