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Inside Cover: The Catalytic Mechanism of the Class C Radical S ‐Adenosylmethionine Methyltransferase NosN (Angew. Chem. Int. Ed. 14/2017)
Author(s) -
Ding Wei,
Li Yongzhen,
Zhao Junfeng,
Ji Xinjian,
Mo Tianlu,
Qianzhu Haocheng,
Tu Tao,
Deng Zixin,
Yu Yi,
Chen Fener,
Zhang Qi
Publication year - 2017
Publication title -
angewandte chemie international edition
Language(s) - English
Resource type - Reports
SCImago Journal Rank - 5.831
H-Index - 550
eISSN - 1521-3773
pISSN - 1433-7851
DOI - 10.1002/anie.201701989
Subject(s) - methyltransferase , methylation , chemistry , int , catalysis , stereochemistry , mechanism (biology) , zhàng , cover (algebra) , coproduct , enzyme , medicinal chemistry , biochemistry , computer science , philosophy , political science , mathematics , dna , mechanical engineering , engineering , operating system , epistemology , law , pure mathematics , china
A powerful methylating agent :In contrast to all other known S ‐adenosylmethionine (SAM) dependent methyltransferases, the enzyme NosN does not produce S ‐adenosylhomocysteine (SAH) as a coproduct, as shown by Q. Zhang and co‐workers in their Communication on page 3857 ff. Instead, NosN converts SAM into 5′‐methylthioadenosine as a direct methyl donor, by employing a radical‐based mechanism for the methylation and release of 5′‐thioadenosine as a coproduct.
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