135304-07-3 Usage
Description
N-Acetyl-S-trans,trans-farnesyl-L-cysteine, also known as N-acetyl-S-farnesyl-L-Cysteine, is a synthetic substrate specifically designed for the isoprenylated protein methyltransferase, which is also referred to as S-adenosylmethionine-dependent methyltransferase. N-Acetyl-S-trans,trans-farnesyl-L-cysteine plays a crucial role in the methylation process of endogenous isoprenylated proteins by acting as an effective inhibitor. It is characterized by its yellow-red oil appearance, indicating its油性 (oily) nature.
Uses
Used in Pharmaceutical Industry:
N-Acetyl-S-trans,trans-farnesyl-L-cysteine is used as a research compound for the pharmaceutical industry. Its primary application is to inhibit the methylation of endogenous isoprenylated proteins, which can be beneficial in studying the effects and roles of these proteins in various biological processes and potential therapeutic interventions.
Used in Biochemical Research:
In the field of biochemical research, N-Acetyl-S-trans,trans-farnesyl-L-cysteine is used as a tool to investigate the function and regulation of isoprenylated protein methyltransferase. By inhibiting the methylation process, researchers can gain insights into the consequences of altered methylation patterns on protein function and cellular signaling pathways.
Used in Drug Development:
N-Acetyl-S-trans,trans-farnesyl-L-cysteine may also be utilized in drug development efforts, particularly in the design of novel therapeutics targeting the isoprenylation and methylation of proteins. Its inhibitory properties could be harnessed to develop drugs that modulate protein function, potentially leading to treatments for diseases associated with abnormal protein methylation.
Overall, N-Acetyl-S-trans,trans-farnesyl-L-cysteine is a versatile compound with applications in various scientific and medical fields, primarily due to its ability to inhibit the methylation of isoprenylated proteins.
References
1) Volker?et al.?(1991),?Effects of farnesylcyteine analogs on protein carboxyl methylation and signal transduction; J. Biol. Chem.?266?21515
2) Xu?et al.?(1996),?Inhibition of capacitative Ca2+ entry into cells by farnesyl analogs; Mol. Pharmacol.?50?1495
3) Rosado and Sage (2000),?Farnesylcyteine analogues inhibit store-regulated Ca2+ entry in human platelets: evidence for involvement of small GTP-binding proteins and actin cytoskeleton; Biochem. J.?347?183
4) Gordon?et al.?(2008),?Topical N-acetyl-S-farnesyl-L-cysteine inhibits mouse skin inflammation, and unlike dexamethasone, its effects are restricted to the application site; J. Invest. Dermatol.?128?643
5) Adhami?et al.?(2012),?N-acetyl-S-farnesyl-L-cysteine suppresses chemokine production by human dermal microvascular endothelial cells;?Exp. Dermatol.?21?700
Check Digit Verification of cas no
The CAS Registry Mumber 135304-07-3 includes 9 digits separated into 3 groups by hyphens. The first part of the number,starting from the left, has 6 digits, 1,3,5,3,0 and 4 respectively; the second part has 2 digits, 0 and 7 respectively.
Calculate Digit Verification of CAS Registry Number 135304-07:
(8*1)+(7*3)+(6*5)+(5*3)+(4*0)+(3*4)+(2*0)+(1*7)=93
93 % 10 = 3
So 135304-07-3 is a valid CAS Registry Number.
InChI:InChI=1/C20H33NO3S/c1-15(2)8-6-9-16(3)10-7-11-17(4)12-13-25-14-19(20(23)24)21-18(5)22/h8,10,12,19H,6-7,9,11,13-14H2,1-5H3,(H,21,22)(H,23,24)/b16-10+,17-12+/t19-/m0/s1
135304-07-3Relevant articles and documents
Structure-activity studies on the retinal rod outer segment isoprenylated protein methyltransferase
Gilbert, Bryant A.,Tan, Eng Wui,Pérez-Sala, Dolores,Rando, Robert R.
, p. 3966 - 3973 (1992)
Structure-activity studies were performed on the retinal rod outer segment isoprenylated protein methyltransferase that transfers a methyl group from S-adenosylmethionine (AdoMet) to the carboxyl group of isoprenylated (farnesylated or geranylgeranylated) cysteine residues. This methyltransferase enzyme has been shown to methylate N-acetyl-S-farnesyl-L-cysteine (L-AFC, 1) and S-(farnesyl-3-thio)propionic acid (FTP, 2). It is shown here that the enzyme does not enzymatically process D-AFC (8), although D-AFC (8) is a mixed-type inhibitor of the enzyme. Small modifications in the FTP (2) structural series generally lead to inactive substrates. For example, neither the cis- nor the trans-acrylate derivatives of FTP (2) are substrates of the enzyme, but both are inhibitors of it. Alkyl substitutions at the 3-position of FTP (2), moreover, lead to inhibitors of the methyltransferase. Substituents at the 2-position of FTP (2), as in 2-methyl-S-(farnesyl-3-thio)propionic acid (MFTP, 28) or S-farnesyl-2-(thiomethyl)acrylic acid (FTMA, 31), produce active substrates. Modifications at the carboxyl moiety produce neither substrates nor inhibitors of the enzyme. The conclusion from this and earlier studies is that the methyltransferase is selective for an isoprenylated thiopropionate moiety. Small deviations from this minimally essential structure lead to the abolition of substrate activity.
A photoactivatable prenylated cysteine designed to study isoprenoid recognition
Kale,Raab,Yu,Dean,Distefano
, p. 4373 - 4381 (2007/10/03)
Protein prenylation, involving the alkylation of a specific C-terminal cysteine with a C15 or C20 isoprenoid unit, is an essential posttranslational modification required by most GTP-binding proteins for normal biological activity. Despite the ubiquitous nature of this modification and numerous efforts aimed at inhibiting prenylating enzymes for therapeutic purposes, the function of prenylation remains unclear. To explore the role the isoprenoid plays in mediating protein-protein recognition, we have synthesized a photoactivatable, isoprenoid-containing cysteine analogue (2) designed to act as a mimic of the C-terminus of prenylated proteins. Photolysis experiments with 2 and RhoGDI (GDI), a protein which interacts with prenylated Rho proteins, suggest that the GDI is in direct contact with the isoprenoid moiety. These results, obtained using purified GDI as well as Escherichia coli (E. coli) crude extract containing GDI, suggest that this analogue will be an effective and versatile tool for the investigation of putative isoprenoid binding sites in a variety of systems. Incorporation of this analogue into peptides or proteins should allow for even more specific interactions between the photoactivatable isoprenoid and any number of isoprenoid binding proteins.
