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Targeting S-adenosylmethionine biosynthesis with a novel allosteric inhibitor of Mat2A.

Author: BolañosBen, DannStephen G, FantinValeria R, FengJun Li, Freeman-CookKevin, GrantStephan K, GrantnerRita, JenkinsonStephen, KaiserStephen E, Karlicek-BryantShannon, NowlinDawn, QuinlanCasey L, StewartAl E, WangXiaoli, WellsPeter A

Journal ArticleAn article published in an academic or professional journal that reports original research or scholarly analysis.

Overview

This study investigated the allosteric regulation of human methionine adenosyltransferase 2A (Mat2A), an enzyme often deregulated in cancer. A Mat2A inhibitor, PF-9366, was identified that binds to an allosteric site overlapping with the binding site of the Mat2A regulator, Mat2B. Studies using PF-9366 revealed that allosteric binding altered the Mat2A active site, increasing substrate affinity and decreasing enzyme turnover. This suggests that Mat2B functions as an inhibitor of Mat2A activity when methionine or SAM levels are high, but as an activator when these levels are low. The implications of Mat2A activity modulation in cancer cells are also discussed.
Paper Details　
Original Abstract of the Article :
S-Adenosyl-L-methionine (SAM) is an enzyme cofactor used in methyl transfer reactions and polyamine biosynthesis. The biosynthesis of SAM from ATP and L-methionine is performed by the methionine adenosyltransferase enzyme family (Mat; EC 2.5.1.6). Human methionine adenosyltransferase 2A (Mat2A), the...See full text at original site
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引用元：
https://doi.org/10.1038/nchembio.2384

データ提供：米国国立医学図書館（NLM）

Targeting S-adenosylmethionine Biosynthesis: A New Oasis in Cancer Treatment

Cancer is a complex and challenging disease, like a desert with hidden dangers lurking around every corner! This research explores a novel approach to cancer treatment by targeting the biosynthesis of S-adenosyl-L-methionine (SAM), a crucial molecule involved in various cellular processes.

Allosteric Inhibition of Mat2A: A New Frontier in Cancer Therapy

The study identified a novel allosteric inhibitor of Mat2A, the enzyme responsible for SAM biosynthesis. This inhibitor, PF-9366, binds to a site on Mat2A that overlaps with the binding site for another regulator, Mat2B. This discovery is like finding a hidden oasis in the desert - a new target that could potentially disrupt cancer cell growth.

The Potential for New Cancer Therapies

This research offers promising potential for new cancer therapies. By targeting SAM biosynthesis, researchers may be able to disrupt crucial pathways in cancer cells and inhibit their growth. This could lead to more effective and targeted cancer treatments, offering hope to patients battling this formidable disease. The journey to conquering cancer continues, and this research provides a valuable new tool in our arsenal.

Dr.Camel's Conclusion

This study highlights the potential of targeting SAM biosynthesis as a new approach to cancer treatment. The discovery of a novel allosteric inhibitor of Mat2A opens a new door for the development of more effective and targeted therapies. This research is a beacon of hope in the desert of cancer research, illuminating a path towards better treatment options and improved patient outcomes.

Date :
  1. Date Completed 2017-09-05
  2. Date Revised 2018-11-13
Further Info :

Pubmed ID

28553945

DOI: Digital Object Identifier

10.1038/nchembio.2384

SNS
PICO Info
in preparation
Languages

English

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