title: Prenyltransferase substrate binding pocket flexibility and its application in isoprenoid profiling.
abstract: This communication explores prenyltransferase substrate binding pocket flexibility to tag and enrich isoprenoids using affinity-based purification for metabolomic studies.
authors: Department of Chemistry, Boston University, MA 02215, USA.
authors: Youli
authors: Y
authors: Xiao
authors: Miranda
authors: M
authors: Machacek
authors: Kent
authors: K
authors: Lee
authors: Tomohisha
authors: T
authors: Kuzuyama
authors: Pinghua
authors: P
authors: Liu
mesh_terms: D001426:Bacterial Proteins / Q000378:metabolism; D001665:Binding Sites; D004122:Dimethylallyltranstransferase / Q000737:chemistry / Q000378:metabolism*; D011756:Diphosphates / Q000378:metabolism; D004224:Diterpenes / Q000378:metabolism; D007700:Kinetics; D055432:Metabolomics / Q000379:methods*; D009285:Naphthoquinones / Q000378:metabolism; D018583:Pliability; D054876:Prenylation; D011485:Protein Binding; D015203:Reproducibility of Results; D013302:Streptomyces / Q000201:enzymology; D013729:Terpenes / Q000378:metabolism*
chemical_list: D001426:Bacterial Proteins; D011756:Diphosphates; D004224:Diterpenes; D009285:Naphthoquinones; D013729:Terpenes; C511282:geranyl diphosphate; C502105:naphterpin B; D004122:Dimethylallyltranstransferase