20859-00-1 Usage
Description
2-Methylthio-N6-isopentenyladenosine, a nucleoside analogue, is a modified adenosine derivative characterized by the presence of a methylthio (methylsulfanyl) group at the C-2 position and a Delta2-isopentenyl group attached to the 6-amino nitrogen. This unique structure plays a crucial role in the function of certain transfer RNAs (tRNAs) and has potential applications in various fields.
Uses
Used in Molecular Biology:
2-Methylthio-N6-isopentenyladenosine is used as a tRNA modification for enhancing the efficiency of tRNAs that read codons starting with uridine. Its presence in trpT(Su9) suppressor tRNA increases the efficiency by protecting the tRNA from ribosomal proofreading, which is induced by codon context. This modification is essential for the proper functioning of the translation process in protein synthesis.
Used in Pharmaceutical Industry:
2-Methylthio-N6-isopentenyladenosine may have potential applications in the development of new drugs targeting the translation process in protein synthesis. Its unique structure and function in tRNAs could be exploited to design novel therapeutic agents that modulate protein synthesis, which could be useful in treating various diseases and conditions related to abnormal protein production.
Used in Research and Development:
As a nucleoside analogue with a specific role in tRNA function, 2-Methylthio-N6-isopentenyladenosine can be used as a research tool to study the mechanisms of translation and protein synthesis. This knowledge can contribute to the development of new strategies for targeting these processes in various diseases, including cancer and other genetic disorders.
Check Digit Verification of cas no
The CAS Registry Mumber 20859-00-1 includes 8 digits separated into 3 groups by hyphens. The first part of the number,starting from the left, has 5 digits, 2,0,8,5 and 9 respectively; the second part has 2 digits, 0 and 0 respectively.
Calculate Digit Verification of CAS Registry Number 20859-00:
(7*2)+(6*0)+(5*8)+(4*5)+(3*9)+(2*0)+(1*0)=101
101 % 10 = 1
So 20859-00-1 is a valid CAS Registry Number.
InChI:InChI=1/C16H23N5O4S/c1-8(2)4-5-17-13-10-14(20-16(19-13)26-3)21(7-18-10)15-12(24)11(23)9(6-22)25-15/h4,7,9,11-12,15,22-24H,5-6H2,1-3H3,(H,17,19,20)/t9-,11-,12-,15-/m1/s1
20859-00-1Relevant articles and documents
Burrows et al.
, p. 3071,3072 (1969)
Peroxide-shunt substrate-specificity for the Salmonella typhimurium O 2-dependent tRNA modifying monooxygenase (MiaE)
Corder, Andra L.,Subedi, Bishnu P.,Zhang, Siai,Dark, Amanda M.,Foss Jr., Frank W.,Pierce, Brad S.
, p. 6182 - 6196 (2013/10/01)
Post-transcriptional modifications of tRNA are made to structurally diversify tRNA. These modifications alter noncovalent interactions within the ribosomal machinery, resulting in phenotypic changes related to cell metabolism, growth, and virulence. MiaE is a carboxylate bridged, nonheme diiron monooxygenase, which catalyzes the O2-dependent hydroxylation of a hypermodified-tRNA nucleoside at position 37 (2-methylthio-N6- isopentenyl-adenosine(37)-tRNA) [designated ms2i6A 37]. In this work, recombinant MiaE was cloned from Salmonella typhimurium, purified to homogeneity, and characterized by UV-visible and dual-mode X-band EPR spectroscopy for comparison to other nonheme diiron enzymes. Additionally, three nucleoside substrate-surrogates (i6A, Cl2i6A, and ms2i6A) and their corresponding hydroxylated products (io6A, Cl2io 6A, and ms2io6A) were synthesized to investigate the chemo- and stereospecificity of this enzyme. In the absence of the native electron transport chain, the peroxide-shunt was utilized to monitor the rate of substrate hydroxylation. Remarkably, regardless of the substrate (i6A, Cl2i6A, and ms2i6A) used in peroxide-shunt assays, hydroxylation of the terminal isopentenyl-C4-position was observed with >97% E-stereoselectivity. No other nonspecific hydroxylation products were observed in enzymatic assays. Steady-state kinetic experiments also demonstrate that the initial rate of MiaE hydroxylation is highly influenced by the substituent at the C2-position of the nucleoside base (v0/[E] for ms2i6A > i 6A > Cl2i6A). Indeed, the >3-fold rate enhancement exhibited by MiaE for the hydroxylation of the free ms 2i6A nucleoside relative to i6A is consistent with previous whole cell assays reporting the ms2io6A and io6A product distribution within native tRNA-substrates. This observation suggests that the nucleoside C2-substituent is a key point of interaction regulating MiaE substrate specificity.
