Literature DB >> 16054248

Characterization of O-methyltransferase ScOMT1 cloned from Streptomyces coelicolor A3(2).

Youngdae Yoon1, Yong Sub Yi, Youngshim Lee, Seunghyun Kim, Bong Gyu Kim, Joong-Hoon Ahn, Yoongho Lim.   

Abstract

The roles of O-methyltransferases (OMTs) in microorganisms are not well understood, and are suggested to increase antimicrobial activity. Studies on OMTs cloned from microorganisms may help elucidate their roles. Streptomyces coelicolor A3(2) produces many useful natural antibiotics such as actinorhodin. Based on sequence information from S. coelicolor A3(2) genome, it was possible to clone several methyltransferases. An OMT cloned from Streptomyces coelicolor A3(2), ScOMT1 was characterized by in vivo and in vitro assays. Of 23 compounds tested, 13 were found to serve as its substrates. Of the 13 substrates, the methylated positions of 7 compounds were determined by HPLC, NMR, and MS analyses. This OMT favored ortho-dihydroxyflavones. Among the compounds tested here, the best substrate is 6,7-dihydroxyflavone.

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Year:  2005        PMID: 16054248     DOI: 10.1016/j.bbaexp.2005.06.005

Source DB:  PubMed          Journal:  Biochim Biophys Acta        ISSN: 0006-3002


  2 in total

1.  Cation dependent O-methyltransferases from rice.

Authors:  Yoon Jung Lee; Bong Gyu Kim; Youhoon Chong; Yoongho Lim; Joong-Hoon Ahn
Journal:  Planta       Date:  2007-10-18       Impact factor: 4.116

2.  Regiospecific O-methylation of naphthoic acids catalyzed by NcsB1, an O-methyltransferase involved in the biosynthesis of the enediyne antitumor antibiotic neocarzinostatin.

Authors:  Yinggang Luo; Shuangjun Lin; Jian Zhang; Heather A Cooke; Steven D Bruner; Ben Shen
Journal:  J Biol Chem       Date:  2008-04-03       Impact factor: 5.157

  2 in total

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