Design strategy for serine hydroxymethyltransferase probes based on retro-aldol-type reaction View Full Text


Ontology type: schema:ScholarlyArticle      Open Access: True


Article Info

DATE

2019-12

AUTHORS

Hiroshi Nonaka, Yuki Nakanishi, Satoshi Kuno, Tomoki Ota, Kentaro Mochidome, Yutaro Saito, Fuminori Sugihara, Yoichi Takakusagi, Ichio Aoki, Satoru Nagatoishi, Kouhei Tsumoto, Shinsuke Sando

ABSTRACT

Serine hydroxymethyltransferase (SHMT) is an enzyme that catalyzes the reaction that converts serine to glycine. It plays an important role in one-carbon metabolism. Recently, SHMT has been shown to be associated with various diseases. Therefore, SHMT has attracted attention as a biomarker and drug target. However, the development of molecular probes responsive to SHMT has not yet been realized. This is because SHMT catalyzes an essential yet simple reaction; thus, the substrates that can be accepted into the active site of SHMT are limited. Here, we focus on the SHMT-catalyzed retro-aldol reaction rather than the canonical serine-glycine conversion and succeed in developing fluorescent and 19F NMR molecular probes. Taking advantage of the facile and direct detection of SHMT, the developed fluorescent probe is used in the high-throughput screening for human SHMT inhibitors, and two hit compounds are obtained. More... »

PAGES

876

Identifiers

URI

http://scigraph.springernature.com/pub.10.1038/s41467-019-08833-7

DOI

http://dx.doi.org/10.1038/s41467-019-08833-7

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1112222589

PUBMED

https://www.ncbi.nlm.nih.gov/pubmed/30787298


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