70858-14-9Relevant academic research and scientific papers
Intriguing cellular processing of a fluorinated amino acid during protein biosynthesis in: Escherichia coli
Vaughan, Mark D.,Su, Zhengding,Daub, Elisabeth,Honek
supporting information, p. 8942 - 8946 (2016/10/07)
Bioincorporation of the methionine analogue S-(2-fluoroethyl)-l-homocysteine (l-MFE) into bacteriophage lysozyme overproduced in Escherichia coli results not only in the expected l-MFE incorporation but surprisingly substantial l-vinthionine incorporation into the labeled lysozymes. Synthetic l-vinthionine itself however is not activated by purified Escherichia coli methionyl-tRNA synthetase. The indirect preparation of vinthionine-containing proteins has the potential to be an alternate strategy to prepare vinyl thioether moieties for click chemistry applications on proteins.
Capturing Unknown Substrates via in Situ Formation of Tightly Bound Bisubstrate Adducts: S-Adenosyl-vinthionine as a Functional Probe for AdoMet-Dependent Methyltransferases
Qu, Wanlu,Catcott, Kalli C.,Zhang, Kun,Liu, Shanshan,Guo, Jason J.,Ma, Jisheng,Pablo, Michael,Glick, James,Xiu, Yuan,Kenton, Nathaniel,Ma, Xiaoyu,Duclos, Richard I.,Zhou, Zhaohui Sunny
supporting information, p. 2877 - 2880 (2016/03/19)
Identifying an enzyme's substrates is essential to understand its function, yet it remains challenging. A fundamental impediment is the transient interactions between an enzyme and its substrates. In contrast, tight binding is often observed for multisubstrate-adduct inhibitors due to synergistic interactions. Extending this venerable concept to enzyme-catalyzed in situ adduct formation, unknown substrates were affinity-captured by an S-adenosyl-methionine (AdoMet, SAM)-dependent methyltransferase (MTase). Specifically, the electrophilic methyl sulfonium (alkyl donor) in AdoMet is replaced with a vinyl sulfonium (Michael acceptor) in S-adenosyl-vinthionine (AdoVin). Via an addition reaction, AdoVin and the nucleophilic substrate form a covalent bisubstrate-adduct tightly complexed with thiopurine MTase (2.1.1.67). As such, an unknown substrate was readily identified from crude cell lysates. Moreover, this approach is applicable to other systems, even if the enzyme is unknown.
Compositions and Methods for the Inhibition of Methyltransferases
-
Paragraph 0214, (2015/03/04)
Methods and compositions disclosed herein relate to detecting, analyzing, isolating and inhibiting methyltransferases, methyltransferase substrates, S-adenosyl-methionine-binding proteins and RNA, including for the treatment of disease.
