Functional and Pathological Roles of AHCY

Pedro Vizán, Luciano Di Croce, Sergi Aranda

Research output: Indexed journal article Reviewpeer-review

48 Citations (Scopus)

Abstract

Adenosylhomocysteinase (AHCY) is a unique enzyme and one of the most conserved proteins in living organisms. AHCY catalyzes the reversible break of S-adenosylhomocysteine (SAH), the by-product and a potent inhibitor of methyltransferases activity. In mammals, AHCY is the only enzyme capable of performing this reaction. Controlled subcellular localization of AHCY is believed to facilitate local transmethylation reactions, by removing excess of SAH. Accordingly, AHCY is recruited to chromatin during replication and active transcription, correlating with increasing demands for DNA, RNA, and histone methylation. AHCY deletion is embryonic lethal in many organisms (from plants to mammals). In humans, AHCY deficiency is associated with an incurable rare recessive disorder in methionine metabolism. In this review, we focus on the AHCY protein from an evolutionary, biochemical, and functional point of view, and we discuss the most recent, relevant, and controversial contributions to the study of this enzyme.

Original languageEnglish
Article number654344
JournalFrontiers in Cell and Developmental Biology
Volume9
DOIs
Publication statusPublished - 31 Mar 2021
Externally publishedYes

Keywords

  • S-adenosylhomocysteine hydrolase
  • S-adenosylmethionine
  • adenosylhomocysteinase
  • chromatin
  • embryo development
  • epigenetics
  • gene regulation

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