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B1508

Sigma-Aldrich

Butyryl coenzyme A lithium salt hydrate

≥90%

Synonyme(s) :

Butyryl-CoA lithium salt hydrate

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About This Item

Formule empirique (notation de Hill):
C25H42N7O17P3S · xLi+ · yH2O
Poids moléculaire :
837.62 (free acid basis)
Numéro MDL:
MFCD00038616
Code UNSPSC :
41106305
ID de substance PubChem :
329773188
Nomenclature NACRES :
NA.51

Niveau de qualité

200

Pureté

≥90%

Forme

powder

Température de stockage

−20°C

Chaîne SMILES 

[Li+].[Li+].[Li+].[Li+].CCCC(=O)Nc1ncnc2n(cnc12)[C@@H]3O[C@H](COP([O-])(=O)OP([O-])(=O)OCC(C)(C)C(O)C(=O)NCCC(=O)NCCS)[C@@H](OP([O-])([O-])=O)[C@H]3O

InChI

1S/C25H42N7O17P3S.4Li/c1-4-5-16(34)31-21-17-22(29-12-28-21)32(13-30-17)24-18(35)19(48-50(38,39)40)14(47-24)10-45-51(41,42)49-52(43,44)46-11-25(2,3)20(36)23(37)27-7-6-15(33)26-8-9-53;;;;/h12-14,18-20,24,35-36,53H,4-11H2,1-3H3,(H,26,33)(H,27,37)(H,41,42)(H,43,44)(H2,38,39,40)(H,28,29,31,34);;;;/q;4*+1/p-4/t14-,18-,19-,20?,24-;;;;/m1..../s1

Clé InChI

FKMUWGIOOMBTED-VLFKLNKMSA-J

Application

Butyryl CoA is a substrate for Butyryl CoA Dehydrogenase. Butyryl CoA is involved in both lipid and butanoate metabolism. Butyryl-CoA may be used as a substrate of various lipases and as an alternate substrate for 4-hydroxybutyrate CoA-transferase. Butyryl CoA may be used to study the newly discovered process of post-translational histone modification by butyrylation.

Actions biochimiques/physiologiques

Butyryl CoA is a substrate for Butyryl CoA Dehydrogenase. Butyryl CoA is involved in both lipid and butanoate metabolism.

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

Point d'éclair (°F)

Not applicable

Point d'éclair (°C)

Not applicable

Équipement de protection individuelle

dust mask type N95 (US), Eyeshields, Gloves

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Consulter la Bibliothèque de documents

C Biben et al.
Molecular and cellular biology, 14(5), 3504-3513 (1994-05-01)
A DNase I-hypersensitive site analysis of the 5'-flanking region of the mouse alpha-cardiac actin gene with muscle cell lines derived from C3H mice shows the presence of two such sites, at about -5 and -7 kb. When tested for activity
Sofia Macieira et al.
Archives of microbiology, 194(3), 157-166 (2011-08-13)
Clostridium aminobutyricum ferments 4-aminobutyrate (γ-aminobutyrate, GABA) to ammonia, acetate and butyrate via 4-hydroxybutyrate that is activated to the CoA-thioester catalyzed by 4-hydroxybutyrate CoA-transferase. Then, 4-hydroxybutyryl-CoA is dehydrated to crotonyl-CoA, which disproportionates to butyryl-CoA and acetyl-CoA. Cocrystallization of the CoA-transferase with
Li-Chiun Lee et al.
Journal of agricultural and food chemistry, 59(19), 10693-10698 (2011-08-23)
Recombinant Candida rugosa lipase 5 (LIP5) has been functionally expressed along with other isoforms in our laboratory. However, the characterization and codon optimization of LIP5 have not been done. In this work, we characterized, codon-optimized and compared LIP5 with commercial
Yue Chen et al.
Molecular & cellular proteomics : MCP, 6(5), 812-819 (2007-02-03)
The positively charged lysine residue plays an important role in protein folding and functions. Neutralization of the charge often has a profound impact on the substrate proteins. Accordingly all the known post-translational modifications at lysine have pivotal roles in cell
Alison E Ringel et al.
Acta crystallographica. Section D, Structural biology, 72(Pt 7), 841-848 (2016-07-06)
Gcn5 is a conserved acetyltransferase that regulates transcription by acetylating the N-terminal tails of histones. Motivated by recent studies identifying a chemically diverse array of lysine acyl modifications in vivo, the acyl-chain specificity of the acetyltransferase human Gcn5 (Gcn5L2) was
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