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Insights into the Branched‐Chain Formation of Mycarose: Methylation Catalyzed by an ( S )‐Adenosylmethionine‐Dependent Methyltransferase
Author(s) -
Chen Huawei,
Zhao Zongbao,
Hallis Tina M.,
Guo Zhihong,
Liu Hungwen
Publication year - 2001
Publication title -
angewandte chemie international edition
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.831
H-Index - 550
eISSN - 1521-3773
pISSN - 1433-7851
DOI - 10.1002/1521-3773(20010202)40:3<607::aid-anie607>3.0.co;2-8
Subject(s) - methyltransferase , methylation , chemistry , tylosin , biochemistry , stereochemistry , enzyme , biosynthesis , catalysis , transferase , sugar , cofactor , derivative (finance) , dna , antibiotics , financial economics , economics
A C‐methyltransferase involved in methyl‐branch formation in sugars has been characterized for the first time. TylC3, an ( S )‐adenosylmethylthionine(AdoMet)‐dependent enzyme, catalyzes the attachment of a methyl branch [Eq. (1)] in the biosynthesis of L ‐mycarose, an unusual sugar found in tylosin and as its O‐3‐methyl derivative in erythromycin. The C‐3 methylation proceeds with inversion of configuration and does not require the assistance of any cofactors. The turnover rate is 1.4±0.1 min −1 . TDP=thymidine‐5′‐dihydrogenphosphate.