31664-36-5

Basic information

• Product Name: coenzyme A disulfide
• Synonyms: coenzyme A disulfide;CoA-disulfide
• CAS NO: 31664-36-5
• Molecular Formula: C₄₂H₇₀N₁₄O₃₂P₆S₂
• Molecular Weight: 1533.052366
• Mol File: 31664-36-5.mol
• Article Data: 3

Chemical Properties

• Boiling Point: °Cat760mmHg
• Flash Point: °C
• Appearance: /
• Density: 2.02g/cm³
• Refractive Index: 1.763
• Storage Temp.: ?20°C
• CAS DataBase Reference: coenzyme A disulfide(CAS DataBase Reference)
• NIST Chemistry Reference: coenzyme A disulfide(31664-36-5)
• EPA Substance Registry System: coenzyme A disulfide(31664-36-5)

Safety Data

• WGK Germany: 3
• Hazardous Substances Data: 31664-36-5(Hazardous Substances Data)

Usage

Description

Coenzyme A disulfide is an organic disulfide compound that is formed through the oxidative dimerization of Coenzyme A (CoA). It plays a significant role in the study of reduction systems, specifically Coenzyme A disulfide reductase (CoADR) systems, which are responsible for regenerating reduced CoA in vivo. This molecule also has unique functions within the body that can be explored through its oxidized form.

Uses

Used in Biochemical Research:
Coenzyme A disulfide is used as a research tool for studying reduction systems, specifically Coenzyme A disulfide reductase (CoADR) systems. It helps in understanding the mechanisms involved in the regeneration of reduced CoA in vivo, which is crucial for enzymatic acyl-group transfer reactions and the synthesis and oxidation of fatty acids.
Used in Pharmaceutical Development:
Coenzyme A disulfide can be utilized in the development of pharmaceuticals targeting the unique functions of CoA in the body. By studying the oxidized form of CoA, researchers can gain insights into its potential therapeutic applications and develop drugs that modulate its activity for the treatment of various diseases.
Used in Analytical Chemistry:
Coenzyme A disulfide can be employed as an analytical reagent in the detection and quantification of CoA and its related compounds. Its unique chemical properties make it a valuable tool for the development of assays and other analytical techniques in the field of chemistry and biochemistry.

InChI:InChI=1/C42H70N14O32P6S2/c1-41(2,15-81-93(75,76)87-91(71,72)79-13-21-29(85-89(65,66)67)27(59)39(83-21)55-19-53-25-33(43)49-17-51-35(25)55)31(61)37(63)47-7-5-23(57)45-9-11-95-96-12-10-46-24(58)6-8-48-38(64)32(62)42(3,4)16-82-94(77,78)88-92(73,74)80-14-22-30(86-90(68,69)70)28(60)40(84-22)56-20-54-26-34(44)50-18-52-36(26)56/h17-22,27-32,39-40,59-62H,5-16H2,1-4H3,(H,45,57)(H,46,58)(H,47,63)(H,48,64)(H,71,72)(H,73,74)(H,75,76)(H,77,78)(H2,43,49,51)(H2,44,50,52)(H2,65,66,67)(H2,68,69,70)/t21-,22-,27-,28-,29-,30-,31+,32+,39-,40-/m1/s1

Upstream product

• 85-61-0 coenzyme A 
• 6477-52-7 coenzyme A-glutathione mixed disulfide 

Downstream Products

• 85-61-0 coenzyme A 
• 6477-52-7 coenzyme A-glutathione mixed disulfide 

Relevant articles and documents

Michael acceptor-containing coenzyme a analogues as inhibitors of the atypical coenzyme a disulfide reductase from staphylococcus aureus

Coenzyme A (CoA) analogues containing α,β-unsaturated ester, ketone, and sulfone moieties were prepared by chemo-enzymatic synthesis as inhibitors of coenzyme A disulfide reductase (CoADR), a proven and as yet unexploited drug target in Staphylococcus aureus. Among these Michael acceptor-containing CoA analogues, which were designed to target CoADR's single essential active site cysteine for conjugate addition, a phenyl vinyl sulfone-containing analogue showed the most potent inhibition with a competitive Ki of ～40 nM, and time-dependent inactivation with a second-order rate of inactivation constant of ～40 000 s -1?M-1. Our results suggest that electrophilic substrate analogues should be considered as potential inhibitors of other medicinally relevant disulfide reductase enzymes.

N6-[N-(6-Aminohexyl)carbamoylmethyl]-coenzyme A. Synthesis and application in affinity chromatography and as an immobilized active coenzyme.

The synthesis of a new coenzyme A analogue, N6-[N-(6-aminohexyl)carbamoylmethyl]-CoA, suitable for immobilisation through its terminal amino group to support matrices, is described. The synthetic route starts with bis(CoA) and involves the following steps: alkylation with iodoacetic acid and rearrangement yielding bis(N6-carboxymethyl-CoA), elongation of the carboxymethyl terminal with 1,6-diaminohexane using carbodiimide to yield bis(N6-[N-(6-aminohexyl)-carbamoylmethyl]-CoA) and finally the splitting of this bis[CoA analogue) through reduction with dithiothreitol to give the final product in approximately 10% overall yield. This CoA analogue showed 'coenzymic activity' with the enzymes acetyl-CoA synthetase, phosphotransacetylase and succinic thiokinase. Covalent binding of the CoA analogue to Sepharose 4B was normally carried out using its S-(5-thio-2-nitrobenzoic acid) derivative as this allows a convenient way for determining the amount of ligand coupled, based on the amount of 5-thio-2-nitrobenzoic acid liberated from the gel after reduction with dithiothreitol. After covalent binding of the CoA analogue to water-soluble activated dextran 70, the analogue was recycled while present in an ultrafiltration cell using the enzymes phosphotransacetylase and citrate synthase. The reaction was followed by measuring the citrate formed on addition of acetylphosphate and oxaloacetate. In affinity chromatographic studies it was shown that the CoA-Sepharose preparation could bind the CoA-dependent enzymes citrate synthase and succinic thiokinase and these could be biospecifically eluted using soluble CoA.