The G subunit will eventually hydrolyze the attached GTP to GDP by its inherent enzymatic activity, allowing it to re-associate with G and starting a new cycle. A group of proteins called Regulator of G protein signalling (RGSs), act as GTPase-activating proteins (GAPs), are specific for G subunits. These proteins accelerate the hydrolysis of GTP to GDP, thus terminating the transduced signal. In some cases, the effector itself may possess intrinsic GAP activity, which then can help deactivate the pathway. This is true in the case of phospholipase C-beta, which possesses GAP activity within its C-terminal region. This is an alternate form of regulation for the G subunit. Such G GAPs do not have catalytic residues (specific amino acid sequences) to activate the G protein. They work instead by lowering the required activation energy for the reaction to take place.