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Biochemical investigations of two 6-DMATS enzymes from streptomyces reveal new features of l -tryptophan prenyltransferases
Two putative prenyltransferase genes, SAML0654 and Strvi8510, were identified in Streptomyces ambofaciens and Streptomyces violaceusniger, respectively. Their deduced products share 63-?% sequence identity. Biochemical investigations with recombinant proteins demonstrated that L-tryptophan and derivatives, including D-tryptophan, 4-, 5-, 6- and 7-methyl-dl-tryptophan, were well accepted by both enzymes in the presence of DMAPP. Structural elucidation of the isolated products revealed regiospecific prenylation at C-6 of the indole ring and proved unequivocally the identification of two very similar 6-dimethylallyltryptophan synthases (6-DMATS). Detailed biochemical investigations with SAML0654 proved L-tryptophan to be the best substrate (Km 18 mum, turnover 0.3 s-1). Incubation with different prenyl donors showed that they also accepted GPP and catalyzed the same specific prenylation. Utilizing GPP as a prenyl donor has not been reported for tryptophan prenyltransferases previously. Both enzymes also catalyzed prenylation of some hydroxynaphthalenes; this has not previously been described for bacterial indole prenyltransferases. Interestingly, SAML0654 transferred prenyl moieties onto the unsubstituted ring of hydroxynaphthalenes. They can do more: L-Tryptophan (1-?a) and derivatives as well as hydroxynaphthalenes like 2,3-dihydroxynaphthalene (10-?a) were accepted by 6-DMATSSa and 6-DMATSSv from Streptomyces strains, in the presence of DMAPP and GPP. C6-prenylated indole derivatives and dihydroxynaphthalenes with prenylation at the unsubstituted ring were identified as enzyme products of 6-DMATSSa.
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Reference:
Metal catalyst and ligand design,
Ligand Template Strategies for Catalyst Encapsulation – NCBI