Ontology highlight
ABSTRACT:
SUBMITTER: Catcott KC
PROVIDER: S-EPMC6483605 | biostudies-literature | 2017 Apr
REPOSITORIES: biostudies-literature
Catcott Kalli C KC Yan Jing J Qu Wanlu W Wysocki Vicki H VH Zhou Zhaohui Sunny ZS
Chembiochem : a European journal of chemical biology 20170314 7
The enzyme-substrate complex is inherently transient, rendering its detection difficult. In our framework designed for bisubstrate systems-isotope-labeled, activity-based identification and tracking (IsoLAIT)-the common substrate, such as S-adenosyl-l-methionine (AdoMet) for methyltransferases, is replaced by an analogue (e.g., S-adenosyl-l-vinthionine) that, as a probe, creates a tightly bound [enzyme⋅substrate⋅probe] complex upon catalysis by thiopurine-S-methyltransferase (TPMT, EC 2.1.1.67). ...[more]