Ac-QPKK(Ac)-AMC acetate is a p53-derived peptide conjugated with a fluorophore, which serves as a fluorescent peptide substrate for detecting the deacylase activity of zinc-dependent HDACs and sirtuins (Ex = 360 nm; Em = 460 nm) [1].
In Vitro, Ac-QPKK(Ac)-AMC (4a) (50 μM; 60 min) acetate is acted upon by recombinant human HDAC1, HDAC2, and HDAC3/NCoR2 which exhibit potent deacetylase activity toward the peptide substrate in vitro, with HDAC3/NCoR2 being the most potent[1]. Ac-QPKK(Ac)-AMC (2a) acetate is deacetylated by recombinant SIRT1, SIRT2 and SIRT3 in vitro with distinct catalytic efficiencies, whereas SIRT6 shows negligible deacetylase activity toward this substrate[2].
References:
[1]. Moreno-Yruela C, et al. Class I histone deacetylases (HDAC1–3) are histone lysine delactylases. Sci Adv. 2022 Jan 19;8(3):eabi6696.
[2]. Galleano I, et al. A Continuous, Fluorogenic Sirtuin 2 Deacylase Assay: Substrate Screening and Inhibitor Evaluation. J Med Chem. 2016;59(3):1021-1031.
In Vitro, Ac-QPKK(Ac)-AMC (4a) (50 μM; 60 min) acetate is acted upon by recombinant human HDAC1, HDAC2, and HDAC3/NCoR2 which exhibit potent deacetylase activity toward the peptide substrate in vitro, with HDAC3/NCoR2 being the most potent[1]. Ac-QPKK(Ac)-AMC (2a) acetate is deacetylated by recombinant SIRT1, SIRT2 and SIRT3 in vitro with distinct catalytic efficiencies, whereas SIRT6 shows negligible deacetylase activity toward this substrate[2].
References:
[1]. Moreno-Yruela C, et al. Class I histone deacetylases (HDAC1–3) are histone lysine delactylases. Sci Adv. 2022 Jan 19;8(3):eabi6696.
[2]. Galleano I, et al. A Continuous, Fluorogenic Sirtuin 2 Deacylase Assay: Substrate Screening and Inhibitor Evaluation. J Med Chem. 2016;59(3):1021-1031.