P5397
n-Propionyl coenzyme A lithium salt
≥85%
Synonym(s):
n-Propionyl CoA lithium salt
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About This Item
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Assay
≥85%
form
powder
storage temp.
−20°C
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
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.
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).
Signal Word
Warning
Hazard Statements
Precautionary Statements
Hazard Classifications
Eye Irrit. 2 - Skin Irrit. 2 - STOT SE 3
Target Organs
Respiratory system
Storage Class Code
11 - Combustible Solids
WGK
WGK 3
Personal Protective Equipment
dust mask type N95 (US), Eyeshields, Gloves
Certificates of Analysis (COA)
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Propionyl coenzyme A (propionyl-CoA) carboxylase in Haloferax mediterranei: indispensability for propionyl-CoA assimilation and impacts on global metabolism
Applied and Environmental Microbiology, 81(2), 794-804 (2015)
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
TetR family transcriptional regulator PccD negatively controls propionyl coenzyme A assimilation in Saccharopolyspora erythraea
Journal of Bacteriology, 199(20), e00281-e00217 (2017)
Production of 3-Hydroxypropionic Acid via the Propionyl-CoA Pathway Using Recombinant Escherichia coli Strains
Testing, 11(5), e0156286-e0156286 (2016)
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
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