Ontology highlight
ABSTRACT:
SUBMITTER: Zhu Y
PROVIDER: S-EPMC4796655 | biostudies-literature | 2016 Mar
REPOSITORIES: biostudies-literature
Zhu Yuwei Y Jiang Xuguang X Wang Chongyuan C Liu Yang Y Fan Xiaojiao X Zhang Linjuan L Niu Liwen L Teng Maikun M Li Xu X
Scientific reports 20160315
UbiG is a SAM-dependent O-methyltransferase, catalyzing two O-methyl transfer steps for ubiquinone biosynthesis in Escherichia coli. UbiG possesses a unique sequence insertion between β4 and α10, which is used for membrane lipid interaction. Interestingly, this sequence insertion also covers the methyl donor binding pocket. Thus, the relationship between membrane binding and entrance of the methyl donor of UbiG during the O-methyl transfer process is a question that deserves further exploration. ...[more]