M4414
Myristoyl coenzyme A lithium salt
≥80.0% (HPLC), powder, protein myristoylation substrate
Synonyme(s) :
n-Tetradecanoyl Coenzyme A lithium salt
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A propos de cet article
Formule empirique (notation de Hill) :
C35H62N7O17P3S · xLi+
Numéro CAS:
Poids moléculaire :
977.89 (free acid basis)
UNSPSC Code:
12352202
NACRES:
NA.77
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Laissez-nous vous aiderNom du produit
Myristoyl coenzyme A lithium salt, ≥80.0%
assay
≥80.0%
storage temp.
−20°C
Quality Level
Catégories apparentées
General description
Long chain fatty acid (C14) covalently linked to Coenzyme A. Substrate for de novo fatty acid synthesis. Fatty acylation has been shown to block G protein-associated calcium release by a direct allosteric modification of a component of the GTP-activated process.
Biochem/physiol Actions
Myristoyl coenzyme A is a combination of coenzyme A and myristate. It serves as a substrate in protein myristoylation, catalyzed by the enzyme N-myristoyl transferase. Myristyolation involves the transfer of the myristoyl group to the glycine residue at the amino-terminal of the protein.
Features and Benefits
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Classe de stockage
11 - Combustible Solids
wgk
WGK 3
flash_point_f
Not applicable
flash_point_c
Not applicable
ppe
Eyeshields, Gloves, type N95 (US)
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K E Rys-Sikora et al.
The Journal of biological chemistry, 269(50), 31607-31613 (1994-12-16)
A sensitive and specific GTP-activated Ca2+ translocation process induces rapid Ca2+ movements within cells and appears to reflect G protein-induced membrane fusion or junctional communication between discrete subpopulations of Ca(2+)-pumping organelles (Ghosh, T. K., Mullaney, J. M., Tarazi, F. I.
Signal Transduction - Single Cell Techniques, 327-327 (2008)
F Dittrich et al.
European journal of biochemistry, 252(3), 477-485 (1998-04-18)
Elongation of long-chain fatty acids was investigated in yeast mutants lacking endogenous de novo fatty acid synthesis. In this background, in vitro fatty acid elongation was dependent strictly on the substrates malonyl-CoA, NADPH and a medium-chain or long-chain acyl-CoA primer
Functional significance of myristoyl moiety in N-myristoyl proteins.
L J Knoll et al.
Methods in enzymology, 250, 405-435 (1995-01-01)
Yasmin ElMaghloob et al.
eLife, 10 (2021-01-14)
The ADP-ribosylation factor-like 3 (ARL3) is a ciliopathy G-protein which regulates the ciliary trafficking of several lipid-modified proteins. ARL3 is activated by its guanine exchange factor (GEF) ARL13B via an unresolved mechanism. BART is described as an ARL3 effector which
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