{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Salem SM"],"funding":["NIDDK NIH HHS","NCI NIH HHS","NIGMS NIH HHS"],"pagination":["2529-2534"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC5886728"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["12(10)"],"pubmed_abstract":["Glycosyltransferases are key enzymes involved in the biosynthesis of valuable natural products providing an excellent drug-tailoring tool. Herein, we report the identification of two cooperative glycosyltransferases from the sqn gene cluster directing the biosynthesis of saquayamycins in Streptomyces sp. KY40-1: SqnG1 and SqnG2. Gene inactivation of sqnG1 leads to 50-fold decrease in saquayamycin production, while inactivation of sqnG2 leads to complete production loss, suggesting that SqnG2 acts as dual O- and C-glycosyltransferase. Gene inactivation of a third putative glycosyltransferase-encoding gene, sqnG3, does not affect saquayamycin production in a major way, suggesting that SqnG3 has no or a supportive role in glycosylation. The data indicate that SqnG1 and SqnG2 are solely and possibly cooperatively responsible for the sugar diversity observed in saquayamycins 1-7. This is the first evidence of a glycosyltransferase system showing codependence to achieve dual O- and C-glycosyltransferase activity, utilizing NDP-activated d-olivose, l-rhodinose, as well as an unusual amino sugar, presumably 3,6-dideoxy-l-idosamine."],"journal":["ACS chemical biology"],"pubmed_title":["Two Cooperative Glycosyltransferases Are Responsible for the Sugar Diversity of Saquayamycins Isolated from Streptomyces sp. KY 40-1."],"pmcid":["PMC5886728"],"funding_grant_id":["U24 DK097215","P30 CA177558","R01 GM105977","R01 CA091901"],"pubmed_authors":["Weidenbach S","Rohr J","Salem SM"],"additional_accession":[]},"is_claimable":false,"name":"Two Cooperative Glycosyltransferases Are Responsible for the Sugar Diversity of Saquayamycins Isolated from Streptomyces sp. KY 40-1.","description":"Glycosyltransferases are key enzymes involved in the biosynthesis of valuable natural products providing an excellent drug-tailoring tool. Herein, we report the identification of two cooperative glycosyltransferases from the sqn gene cluster directing the biosynthesis of saquayamycins in Streptomyces sp. KY40-1: SqnG1 and SqnG2. Gene inactivation of sqnG1 leads to 50-fold decrease in saquayamycin production, while inactivation of sqnG2 leads to complete production loss, suggesting that SqnG2 acts as dual O- and C-glycosyltransferase. Gene inactivation of a third putative glycosyltransferase-encoding gene, sqnG3, does not affect saquayamycin production in a major way, suggesting that SqnG3 has no or a supportive role in glycosylation. The data indicate that SqnG1 and SqnG2 are solely and possibly cooperatively responsible for the sugar diversity observed in saquayamycins 1-7. This is the first evidence of a glycosyltransferase system showing codependence to achieve dual O- and C-glycosyltransferase activity, utilizing NDP-activated d-olivose, l-rhodinose, as well as an unusual amino sugar, presumably 3,6-dideoxy-l-idosamine.","dates":{"release":"2017-01-01T00:00:00Z","publication":"2017 Oct","modification":"2020-10-31T08:56:23Z","creation":"2019-03-26T23:29:16Z"},"accession":"S-EPMC5886728","cross_references":{"pubmed":["28892347"],"doi":["10.1021/acschembio.7b00453"]}}