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C3019

Sigma-Aldrich

Coenzyme A trilithium salt

≥93%

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Synonym(s):
CoA Li3
Empirical Formula (Hill Notation):
C21H33Li3N7O16P3S
CAS Number:
18439-24-2
Molecular Weight:
785.33
EC Number:
242-317-9
MDL number:
MFCD00075848
PubChem Substance ID:
24892557
NACRES:
NA.51

Quality Level

200

Assay

≥93%

form

powder

storage temp.

−20°C

SMILES string

[Li+].[Li+].[Li+].CC(C)(COP([O-])(=O)OP([O-])(=O)OC[C@H]1O[C@H]([C@H](O)[C@@H]1OP(O)([O-])=O)n2cnc3c(N)ncnc23)C(O)C(=O)NCCC(=O)NCCS

InChI

1S/C21H36N7O16P3S.3Li/c1-21(2,16(31)19(32)24-4-3-12(29)23-5-6-48)8-41-47(38,39)44-46(36,37)40-7-11-15(43-45(33,34)35)14(30)20(42-11)28-10-27-13-17(22)25-9-26-18(13)28;;;/h9-11,14-16,20,30-31,48H,3-8H2,1-2H3,(H,23,29)(H,24,32)(H,36,37)(H,38,39)(H2,22,25,26)(H2,33,34,35);;;/q;3*+1/p-3/t11-,14-,15-,16?,20-;;;/m1.../s1

InChI key

QSCBPHBAFBVXRK-HJKJOZROSA-K

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General description

Coenzyme A (CoA) is synthesized from phosphopantothenate by the action of enzyme pantothenate kinase and is the master regulator.

Application

Coenzyme A trilithium salt has been used:
  • in standard curve generation in the kinetic assay of acetyltransferase Gcn5 acylation
  • as a cofactor in JNADH and JNADPH production assay
  • in the labeling of Alexa647 (AF647) probe

Biochem/physiol Actions

Coenzyme A (CoA, CoASH, HSCoA) is a coenzyme that facilitates enzymatic acyl-group transfer reactions and supports the synthesis and oxidation of fatty acids. CoA is involved in the mechanisms of a wide variety of enzymes. Acyl CoA accumulation is implicated in metabolic disorders and may indirectly lead to the pathogenesis associated with carbon-induced mitochondrial stress heart failure, diabetes and obesity.

Other Notes

For more more technical information and a complete list of Coenzyme A deriviatives visit the Acyl Transfer Reagents Resource.

Storage Class Code

11 - Combustible Solids

WGK

WGK 3

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable

Personal Protective Equipment

dust mask type N95 (US), Eyeshields, Gloves

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Jessica P Kuppan et al.
eLife, 10 (2021-09-30)
The complement system is a critical host defense against infection, playing a protective role that can also enhance disease if dysregulated. Although many consequences of complement activation during viral infection are well established, mechanisms that determine the extent to which
Characterization of Fluorescein Arsenical Hairpin (FlAsH) as a Probe for Single-Molecule Fluorescence Spectroscopy
Fernandes DD, et al.
Scientific reports, 7(1), 13063-13063 (2017)
Respiratory phenomics across multiple models of protein hyperacylation in cardiac mitochondria reveals a marginal impact on bioenergetics
Fisher-Wellman KH, et al.
Cell Reports, 26(6), 1557-1572 (2019)
Devin T Edwards et al.
Proceedings of the National Academy of Sciences of the United States of America, 118(12) (2021-03-17)
Single-molecule force spectroscopy is a powerful tool for studying protein folding. Over the last decade, a key question has emerged: how are changes in intrinsic biomolecular dynamics altered by attachment to μm-scale force probes via flexible linkers? Here, we studied
Pantothenate kinase regulation of the intracellular concentration of coenzyme A
Rock CO, et al.
The Journal of biological chemistry, 275(2), 1377-1383 (2000)
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