Skip to Content
Merck
CN

P5397

n-Propionyl coenzyme A lithium salt

≥85%

Synonym(s):

n-Propionyl CoA lithium salt

Sign In to View Organizational & Contract Pricing.

Select a Size

About This Item

Empirical Formula (Hill Notation):
C24H40N7O17P3S
CAS Number:
108321-21-7
Molecular Weight:
823.60
UNSPSC Code:
41106305
PubChem Substance ID:
24898631
NACRES:
NA.51

Key Documents

View All Documentation
Technical Service
Need help? Our team of experienced scientists is here for you.
Let Us Assist
Technical Service
Need help? Our team of experienced scientists is here for you.
Let Us Assist

Product Name

n-Propionyl coenzyme A lithium salt, ≥85%

InChI key

CXNLEKKSVXVZAF-IEQRABFGSA-N

InChI

1S/C24H40N7O17P3S.Li/c1-4-15(33)52-8-7-26-14(32)5-6-27-22(36)19(35)24(2,3)10-45-51(42,43)48-50(40,41)44-9-13-18(47-49(37,38)39)17(34)23(46-13)31-12-30-16-20(25)28-11-29-21(16)31;/h11-13,17-19,23,34-35H,4-10H2,1-3H3,(H,26,32)(H,27,36)(H,40,41)(H,42,43)(H2,

SMILES string

[Li].[P](=O)(O[P](=O)(OCC([C@@H](O)C(=O)NCCC(=O)NCCSC(=O)CC)(C)C)O)(OC[C@H]1O[C@H]([C@@H]([C@@H]1O[P](=O)(O)O)O)[n]2c3ncnc(c3nc2)N)O

biological source

yeast

assay

≥85%

form

powder

solubility

H2O: soluble-50 mg/mL, clear, colorless

storage temp.

−20°C

Quality Level

200

Related Categories

Biochem/physiol Actions

Coenzyme A functions as an acyl group carrier, acetyl-CoA. Propionyl coenzyme A (Propionyl-CoA) may be used to characterize and study propionyl-coenzyme A carboxylase complexes found in bacteria. Propionyl-CoA may be used to study the specificity and kinetics of methylisocitrate lyase(s).

General description

Propionyl-CoA is obtained as an end product of isoleucine, valine and methionine catabolism. It is an essential component for the methylaspartate cycle. Branched-chain amino acids and cholesterol also give rise to propionyl-CoA. Propionyl coenzyme A (CoA) is the coenzyme A derivative of propionic acid. Propionyl CoA is formed during the β-oxidation of odd-chain fatty acids.

pictograms

Exclamation mark
GHS07

signalword

Warning

Hazard Classifications

Eye Irrit. 2 - Skin Irrit. 2 - STOT SE 3

target_organs

Respiratory system

Storage Class

11 - Combustible Solids

wgk

WGK 3

ppe

dust mask type N95 (US), Eyeshields, Gloves

Choose from one of the most recent versions:

Certificates of Analysis (COA)

Lot/Batch Number
0000414376
0000414376
0000400283
0000399444
0000400282

Don't see the Right Version?

If you require a particular version, you can look up a specific certificate by the Lot or Batch number.

Search for a COA

Already Own This Product?

Find documentation for the products that you have recently purchased in the Document Library.

Visit the Document Library

M A Luttik et al.
Journal of bacteriology, 182(24), 7007-7013 (2000-11-28)
The Saccharomyces cerevisiae ICL1 gene encodes isocitrate lyase, an essential enzyme for growth on ethanol and acetate. Previous studies have demonstrated that the highly homologous ICL2 gene (YPR006c) is transcribed during the growth of wild-type cells on ethanol. However, even
Propionyl coenzyme A (propionyl-CoA) carboxylase in Haloferax mediterranei: indispensability for propionyl-CoA assimilation and impacts on global metabolism
Hou J, et al.
Applied and Environmental Microbiology, 81(2), 794-804 (2015)
Atanas V Demirev et al.
Journal of microbiology (Seoul, Korea), 49(3), 407-412 (2011-07-01)
Acyl-CoA carboxylases (ACC) are involved in important primary or secondary metabolic pathways such as fatty acid and/or polyketides synthesis. In the 62 kb fragment of pccB gene locus of Streptomyces toxytricini producing a pancreatic inhibitor lipstatin, 3 distinct subunit genes
Atanas V Demirev et al.
Applied microbiology and biotechnology, 87(3), 1129-1139 (2010-05-04)
Streptomyces toxytricini produces lipstatin, a specific inhibitor of pancreatic lipase, which is derived from two fatty acid moieties with eight and 14 carbon atoms. The pccB gene locus in 10.6 kb fragment of S. toxytricini chromosomal DNA contains three genes
Sebastian Müller et al.
Environmental microbiology, 13(6), 1534-1548 (2011-04-02)
Gene duplication represents an evolutionary mechanism for expanding metabolic potential. Here we analysed the evolutionary relatedness of isocitrate and methylisocitrate lyases, which are key enzymes of the glyoxylate and methylcitrate cycle respectively. Phylogenetic analyses imply that ancient eukaryotes acquired an
View All Related Papers

Our team of scientists has experience in all areas of research including Life Science, Material Science, Chemical Synthesis, Chromatography, Analytical and many others.

Contact Technical Service