Obiamaka Obianyo

TL;DR: Inhibition studies suggest that potent and selective bisubstrate analogue inhibitor(s) for PRMT1 can be developed by linking a histone based peptide substrate to homocysteine or sinefungin, and evidence is presented thatPRMT1 utilizes a partially processive mechanism to dimethylate its substrates.

TL;DR: It is shown that 7,8-DHF and BDNF exhibit different TrkB activation kinetics in which TrkB maturation may be implicated, and its agonistic effect may be mediated by neuronal development and maturation.

TL;DR: An analysis of the kinetic mechanism of human PRMT1 using both an unmethylated and a monomethylated substrate peptide based on the N-terminus of histone H4 indicates thatPRMT1 utilizes a rapid equilibrium random mechanism with the formation of dead-end EAP and EBQ complexes, gratifyingly consistent with previous results demonstrating that PR MT1 catalyzes substrate dimethylation in a partially processive manner.

TL;DR: Initial velocity, product inhibition, and dead-end analog inhibition studies with the AcH4-21 and R1 peptides, as well as their monomethylated versions, indicate that PRMT6 utilizes a rapid equilibrium random mechanism with dead- end EAP and EBQ complexes.

TL;DR: This compound, denoted C21, is a chloroacetamidine-containing peptide that is able to irreversibly bind and inactivate the enzyme selectively and it is shown that the coactivator activity of PRMT1 is selectively inhibited by the compound in cellulo.