Biotechnology Bulletin ›› 2023, Vol. 39 ›› Issue (12): 56-70.doi: 10.13560/j.cnki.biotech.bull.1985.2023-0220

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Research Progress in S-adenosyl-L-methionine Dependent 3-amino-3-carboxypropyl Utilizing Enzymes

HE Jia-le(), DONG Min()   

  1. Key Laboratory of Systems Bioengineering(Ministry of Education),School of Chemical Engineering and Technology,Tianjin University,Tianjin 300072
  • Received:2023-03-14 Online:2023-12-26 Published:2024-01-11
  • Contact: DONG Min E-mail:hejiale@tju.edu.cn;mindong@tju.edu.cn

Abstract:

S-adenosyl-L-methionine(SAM)is a very important cofactor in biology. It possesses three unstable C-S bonds, which can be selectively cleaved by various SAM-dependent enzymes, catalyzing a wide range of biochemical reactions. Methyltransferases and radical SAM enzymes, which cleave C-S bonds and use methyl and 5'-dexoyadenosine of SAM respectively, have been intensively studied. Over 1.8 million protein sequences of methyltransferases have been deposited in the UniProt database. Radical SAM enzymes have grown into one of the largest enzyme superfamilies, consisting of over 700 000 members. However, enzymes utilizing the 3-amino-3-carboxypropyl(ACP)group of SAM are relatively rarely reported. This paper aims to classify and introduce these enzymes while also provide a prospective research direction for the future.

Key words: S-adenosyl-L-methionine, 3-amino-3-carboxypropyl, reaction mechanism, methyltransferase, non-canonical radical SAM enzyme