Abstract：
:The glycolipid synthase MG517 from Mycoplasma genitalium catalyzes the glucosyl transfer from UDPGlc to diacylglycerol producing glycoglycerolipids (GGL) (Andrés et al., 2011). The enzyme was functional in E. coli accumulating GGL in the plasma membrane. A metabolic engineering strategy for GGL production was evaluated using this microorganism. To increase the levels of GGL precursors, UDPGlc and diacylglycerol, GalU and PlsC enzymes involved in their biosynthesis were overexpressed. Seven engineered strains were obtained containing different combinations of the mg517 with galU and plsC genes. Diacylglycerol synthesis showed to be limiting and the strain overexpressing MG517 and PlsC achieved the highest GGL yield. The new lipids were mono, di- and triglucosyldiacylglycerol with different acyl combinations in each compound. It indicates that the successive glucosyl transferase activities of MG517 have different acyl chain specificity for the acceptor substrate. GGL represented up to 6 mg per g of dry weight.
journal_name
Metab Engjournal_title
Metabolic engineeringauthors
Mora-Buyé N,Faijes M,Planas Adoi
10.1016/j.ymben.2012.06.001subject
Has Abstractpub_date
2012-09-01 00:00:00pages
551-9issue
5eissn
1096-7176issn
1096-7184pii
S1096-7176(12)00066-3journal_volume
14pub_type
杂志文章abstract：:There is considerable interest in mining organisms for new natural products (NPs) and in improving methods to overproduce valuable NPs. Because of the rapid development of tools and strategies for metabolic engineering and the markedly increased knowledge of the biosynthetic pathways and genetics of NP-producing organ...
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pub_type： 杂志文章
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pub_type： 杂志文章
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更新日期：2008-09-01 00:00:00
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更新日期：2012-09-01 00:00:00
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