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Background  Pterostilbene, a structural analog of resveratrol, has higher oral bioavailability and bioactivity than that of the parent compound; but is far less abundant in natural sources. Thus, to efficiently obtain this bioactive resveratrol analog, it is necessary to develop new bioproduction systems.    Results  We identified a resveratrol O-methyltransferase (ROMT) function from a multifunctional caffeic acid O-methyltransferase (COMT) originating from  Arabidopsis , which catalyzes the transfer of a methyl group to resveratrol resulting in pterostilbene production. In addition, we constructed a biological platform to produce pterostilbene with this ROMT gene. Pterostilbene can be synthesized from intracellular  l -tyrosine, which requires the activities of four enzymes: tyrosine ammonia lyase (TAL),  p -coumarate:CoA ligase (CCL), stilbene synthase (STS) and resveratrol O-methyltransferase (ROMT). For the efficient production of pterostilbene in  E. coli , we used an engineered  E. coli  strain to increase the intracellular pool of  l -tyrosine, which is the initial precursor of pterostilbene. Next, we tried to produce pterostilbene in the engineered  E. coli  strain using  l -methionine containing media, which is used to increase the intracellular pool of S-adenosyl- l -methionine (SAM). According to this result, pterostilbene production as high as 33.6 ± 4.1 mg/L was achieved, which was about 3.6-fold higher compared with that in the parental  E. coli  strain harboring a plasmid for pterostilbene biosynthesis.    Conclusion  As a potential phytonutrient, pterostilbene was successfully produced in  E. coli  from a glucose medium using a single vector system, and its production titer was also significantly increased using a  l -methionine containing medium in combination with a strain that had an engineered metabolic pathway for  l -tyrosine. Additionally, we provide insights into the dual functions of COMT from  A. thaliana  which was characterized as a ROMT enzyme.    Electronic supplementary material  The online version of this article (doi:10.1186/s12934-017-0644-6) contains supplementary material, which is available to authorized users.

De novo biosynthesis of pterostilbene in an Escherichia coli strain using a new resveratrol O-methyltransferase from Arabidopsis