RESA peptide is a substrate peptide of β-adrenergic receptor kinase (βARK). RESA peptide serves as a substrate for βARK-mediated phosphorylation, and its N-terminal acidic residues enhance phosphorylation efficiency and substrate binding capacity [1].
In Vitro, The RESA peptide (RRREEEEESAAA) (0.05-7 mM; 60 min) acts as a substrate for purified βARK1 with a Vmax/Km ratio of 39, which is 240-fold higher than the basic peptide RRRASAAASAA and ~4000-fold lower than activated rhodopsin[1]. The RESA peptide (RRREEEEESAAA) (0.05-3 mM; 60 min) had its βARK1-mediated phosphorylation slightly inhibited by light-activated rhodopsin (Rho'), reducing the Vmax/Km ratio to 0.6-fold of the value measured in the absence of Rho'[1].
References:
[1]. Chen CY, et al. Beta-adrenergic receptor kinase. Agonist-dependent receptor binding promotes kinase activation. J Biol Chem. 1993 Apr 15;268(11):7825-31.
In Vitro, The RESA peptide (RRREEEEESAAA) (0.05-7 mM; 60 min) acts as a substrate for purified βARK1 with a Vmax/Km ratio of 39, which is 240-fold higher than the basic peptide RRRASAAASAA and ~4000-fold lower than activated rhodopsin[1]. The RESA peptide (RRREEEEESAAA) (0.05-3 mM; 60 min) had its βARK1-mediated phosphorylation slightly inhibited by light-activated rhodopsin (Rho'), reducing the Vmax/Km ratio to 0.6-fold of the value measured in the absence of Rho'[1].
References:
[1]. Chen CY, et al. Beta-adrenergic receptor kinase. Agonist-dependent receptor binding promotes kinase activation. J Biol Chem. 1993 Apr 15;268(11):7825-31.