M4414
Myristoyl coenzyme A lithium salt
≥80.0% (HPLC), powder, protein myristoylation substrate
Synonym(s):
n-Tetradecanoyl Coenzyme A lithium salt
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About This Item
Empirical Formula (Hill Notation):
C35H62N7O17P3S · xLi+
CAS Number:
Molecular Weight:
977.89 (free acid basis)
UNSPSC Code:
12352202
NACRES:
NA.77
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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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Substrates
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.
Storage Class Code
11 - Combustible Solids
WGK
WGK 3
Flash Point(F)
Not applicable
Flash Point(C)
Not applicable
Personal Protective Equipment
dust mask type N95 (US), Eyeshields, Gloves
Certificates of Analysis (COA)
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Functional significance of myristoyl moiety in N-myristoyl proteins.
L J Knoll et al.
Methods in enzymology, 250, 405-435 (1995-01-01)
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
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.
C M D Swarbrick et al.
Acta crystallographica. Section D, Biological crystallography, 71(Pt 4), 986-995 (2015-04-08)
Acyl-CoA thioesterases catalyse the hydrolysis of the thioester bonds present within a wide range of acyl-CoA substrates, releasing free CoASH and the corresponding fatty-acyl conjugate. The TesB-type thioesterases are members of the TE4 thioesterase family, one of 25 thioesterase enzyme
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