{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"omics_type":["Unknown"],"volume":["59(40)"],"submitter":["Bi D"],"funding":["Howard Hughes Medical Institute","Osteopathic Heritage Foundation"],"pubmed_abstract":["Sirtuin isoform 2 (SIRT2) is an enzyme that catalyzes the removal of acyl groups from lysine residues. SIRT2's catalytic domain has a hydrophobic tunnel where its substrate acyl groups bind. Here, we report that the fluorescent probe 1-aminoanthracene (AMA) binds within SIRT2's hydrophobic tunnel in a substrate-dependent manner. AMA's interaction with SIRT2 was characterized by its enhanced fluorescence upon protein binding (>10-fold). AMA interacted weakly with SIRT2 alone in solution (<i>K</i><sub>d</sub> = 37 μM). However, when SIRT2 was equilibrated with a decanoylated peptide substrate, AMA's affinity for SIRT2 was enhanced ∼10-fold (<i>K</i><sub>d</sub> = 4 μM). The peptide's decanoyl chain and AMA co-occupied SIRT2's hydrophobic tunnel when bound to the protein. In contrast, binding"],"journal":["Biochemistry"],"pagination":["3869-3878"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC7880049"],"repository":["biostudies-literature"],"pubmed_title":["Substrate-Dependent Modulation of SIRT2 by a Fluorescent Probe, 1-Aminoanthracene."],"pmcid":["PMC7880049"],"pubmed_authors":["Hinds N","Yang J","Bi D","Infanti J","Hong JY","Parikh P","Lin H","Weiser BP"],"additional_accession":[]},"is_claimable":false,"name":"Substrate-Dependent Modulation of SIRT2 by a Fluorescent Probe, 1-Aminoanthracene.","description":"Sirtuin isoform 2 (SIRT2) is an enzyme that catalyzes the removal of acyl groups from lysine residues. SIRT2's catalytic domain has a hydrophobic tunnel where its substrate acyl groups bind. Here, we report that the fluorescent probe 1-aminoanthracene (AMA) binds within SIRT2's hydrophobic tunnel in a substrate-dependent manner. AMA's interaction with SIRT2 was characterized by its enhanced fluorescence upon protein binding (>10-fold). AMA interacted weakly with SIRT2 alone in solution (<i>K</i><sub>d</sub> = 37 μM). However, when SIRT2 was equilibrated with a decanoylated peptide substrate, AMA's affinity for SIRT2 was enhanced ∼10-fold (<i>K</i><sub>d</sub> = 4 μM). The peptide's decanoyl chain and AMA co-occupied SIRT2's hydrophobic tunnel when bound to the protein. In contrast, binding","dates":{"release":"2020-01-01T00:00:00Z","publication":"2020 Oct","modification":"2025-04-19T09:42:25.755Z","creation":"2022-02-11T12:06:04.36Z"},"accession":"S-EPMC7880049","cross_references":{"pubmed":["32941003"],"doi":["10.1021/acs.biochem.0c00564"]}}