8-Br-GTP, an analog of GTP, functions as both a competitive inhibitor of FtsZ polymerization and GTPase activity (with a K i value of 31.8 μM). Moreover, it is capable of facilitating nucleic acid modification.
Using specific antisera raised against synthetic peptides, we find that three distinct GTP-binding protein alpha subunits remain bound to the plasma membrane even after activation with nonhydrolyzable GTP analog. Trypsin cleaves each alpha subunit at a si
Mant-GTPγS, an effective GTP analog, displays strong competitive inhibition of adenylyl cyclase (AC). Additionally, it acts as a potent inhibitor of YdeH.
5'-GTP trisodium salt hydrate, an activator of the signal-transducing G proteins, serves as a precursor of mononucleotide units in the enzymatic biosynthesis of DNA and RNA.