Molecular analysis of a 4-dimethylallyltryptophan synthase from Malbranchea aurantiaca.

ABSTRACT: Prenyltransferases are widely distributed in prokaryotes and eukaryotes and play critical roles in cell signaling, protein trafficking, and elaboration of complex molecules in secondary metabolism. Numerous prenylated natural products have been isolated from diverse microorganisms, including bacteria and fungi. These complex metabolites possess a wide range of biological activities, with some showing promise as medicinal agents. On the other hand, many prenylated secondary metabolites have been described as toxins such as ergot alkaloids that have potent psychotropic activity. We have characterized a new prenyltransferase isolated from genomic DNA of Malbranchea aurentiaca RRC1813. Enzyme specificity was investigated with a series of amino acid substrates revealing its function as a 4-dime

SUBMITTER: Ding Y 

PROVIDER: S-EPMC2414270 | biostudies-literature | 2008 Jun

REPOSITORIES: biostudies-literature