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G9510

Sigma-Aldrich

Glutaryl coenzyme A lithium salt

≥90%

Synonyme(s) :

Glutaryl CoA

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About This Item

Formule empirique (notation de Hill):
C26H42N7O19P3S
Numéro CAS:
103192-48-9
Poids moléculaire :
881.63
Code UNSPSC :
41106305
ID de substance PubChem :
24895375
Nomenclature NACRES :
NA.51

Niveau de qualité

200

Pureté

≥90%

Température de stockage

−20°C

Chaîne SMILES 

[Li].CC(C)(COP(O)(=O)OP(O)(=O)OCC1OC(C(O)C1OP(O)(O)=O)n2cnc3c(N)ncnc23)C(O)C(=O)NCCC(=O)NCCSC(=O)CCCC(O)=O

InChI

1S/C26H42N7O19P3S/c1-26(2,21(39)24(40)29-7-6-15(34)28-8-9-56-17(37)5-3-4-16(35)36)11-49-55(46,47)52-54(44,45)48-10-14-20(51-53(41,42)43)19(38)25(50-14)33-13-32-18-22(27)30-12-31-23(18)33/h12-14,19-21,25,38-39H,3-11H2,1-2H3,(H,28,34)(H,29,40)(H,35,36)(H,44,45)(H,46,47)(H2,27,30,31)(H2,41,42,43)/t14-,19-,20-,21?,25-/m1/s1

Clé InChI

SYKWLIJQEHRDNH-KRPIADGTSA-N

Description générale

Glutaryl coenzyme A (Glutaryl CoA) is an intermediate in the mitochondrial oxidation of lysine, hydroxylysine and tryptophan.

Application

Glutaryl coenzyme A lithium salt has been used:
  • in comparative study of acylomes of β-Hydroxy β-methylglutaryl-CoA (HMG-CoA) and glutaryl-CoA by quantitative proteomics
  • as a component of the assay buffer for in vitro biosensor activity experiments for FapR-NLuc proteins
  • to test its effect on pyruvate kinase activity inhibition in a549 lysate

Pictogrammes

Exclamation mark
GHS07

Mention d'avertissement

Warning

Mentions de danger

H315,H319,H335

Classification des risques

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

Organes cibles

Respiratory system

Code de la classe de stockage

11 - Combustible Solids

Classe de danger pour l'eau (WGK)

WGK 3

Équipement de protection individuelle

dust mask type N95 (US), Eyeshields, Gloves

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Simon Wischgoll et al.
Biochemistry, 49(25), 5350-5357 (2010-05-22)
Glutaryl-coenzyme A dehydrogenases (GDHs) involved in amino acid degradation were thought to catalyze both the dehydrogenation and decarboxylation of glutaryl-coenzyme A to crotonyl-coenzyme A and CO(2). Recently, a structurally related but nondecarboxylating, glutaconyl-coenzyme A-forming GDH was characterized in the obligately
Rhushikesh A Kulkarni et al.
Cell chemical biology, 24(2), 231-242 (2017-02-07)
Non-enzymatic protein modification driven by thioester reactivity is thought to play a major role in the establishment of cellular lysine acylation. However, the specific protein targets of this process are largely unknown. Here we report an experimental strategy to investigate
Kinetic mechanism of glutaryl-CoA dehydrogenase
Rao K S, et al.
Biochemistry, 45(51), 15853-15861 (2006)
Yipeng Du et al.
Bioconjugate chemistry, 30(3), 826-832 (2019-01-11)
Malonyl-CoA is one of the key metabolic intermediates in fatty acid metabolism as well as a key player in protein post-translational modifications. Detection of malonyl-CoA in live cells is challenging because of the lack of effective measuring tools. Here we
Jörg Schaarschmidt et al.
FEBS letters, 585(9), 1317-1321 (2011-04-12)
Glutaryl-coenzyme A (CoA) dehydrogenases (GDHs) are acyl-CoA dehydrogenases, which usually dehydrogenate and decarboxylate the substrate to crotonyl-CoA. In some anaerobic bacteria, non-decarboxylating GDHs exist that release glutaconyl-CoA (2,3-dehydroglutaryl-CoA) without decarboxylation. The differing mechanisms of decarboxylating and non-decarboxylating GDHs were investigated
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