Proteins > NAD-dependent protein deacetylase sirtuin-3, mitochondrial
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NAD-dependent protein deacetylase sirtuin-3, mitochondrial
An NAD-dependent protein deacetylase sirtuin-3, mitochondrial that is encoded in the genome of human. [PRO:DNx, UniProtKB:Q9NTG7]
Synonyms
hSIRT3;
EC 2.3.1.286;
Regulatory protein SIR2 homolog 3;
SIR2-like protein 3
Research
Bioassay Publications (24)
| Timeframe | Studies on this Protein(%) | All Drugs % |
|---|
| pre-1990 | 0 (0.00) | 18.7374 |
| 1990's | 0 (0.00) | 18.2507 |
| 2000's | 4 (16.67) | 29.6817 |
| 2010's | 15 (62.50) | 24.3611 |
| 2020's | 5 (20.83) | 2.80 |
Compounds (17)
Drugs with Inhibition Measurements
Drugs with Activation Measurements
| Drug | Taxonomy | Measurement | Average (mM) | Bioassay(s) | Publication(s) |
|---|
| amiodarone | Homo sapiens (human) | EC50 | 3.2500 | 1 | 1 |
| honokiol | Homo sapiens (human) | EC50 | 0.1700 | 1 | 1 |
| honokiol | Homo sapiens (human) | Kd | 1.3150 | 4 | 4 |
| resveratrol | Homo sapiens (human) | EC50 | 177.5950 | 2 | 2 |
| srt1460 | Homo sapiens (human) | EC50 | 300.0000 | 1 | 1 |
| srt1720 | Homo sapiens (human) | EC50 | 300.0000 | 1 | 1 |
| srt2183 | Homo sapiens (human) | EC50 | 300.0000 | 1 | 1 |
Novel Lysine-Based Thioureas as Mechanism-Based Inhibitors of Sirtuin 2 (SIRT2) with Anticancer Activity in a Colorectal Cancer Murine Model.Journal of medicinal chemistry, , 04-25, Volume: 62, Issue:8, 2019
Extending Cross Metathesis To Identify Selective HDAC Inhibitors: Synthesis, Biological Activities, and Modeling.ACS medicinal chemistry letters, , Jun-13, Volume: 10, Issue:6, 2019
Development of Peptide-Based Sirtuin Defatty-Acylase Inhibitors Identified by the Fluorescence Probe, SFP3, That Can Efficiently Measure Defatty-Acylase Activity of Sirtuin.Journal of medicinal chemistry, , 06-13, Volume: 62, Issue:11, 2019
Discovery of potent and selective sirtuin 2 (SIRT2) inhibitors using a fragment-based approach.Journal of medicinal chemistry, , Oct-23, Volume: 57, Issue:20, 2014
Identification of a sirtuin 3 inhibitor that displays selectivity over sirtuin 1 and 2.European journal of medicinal chemistry, , Volume: 55, 2012
Inhibitors of the NAD(+)-Dependent Protein Desuccinylase and Demalonylase Sirt5.ACS medicinal chemistry letters, , Dec-13, Volume: 3, Issue:12, 2012
Identification of a cell-active non-peptide sirtuin inhibitor containing N-thioacetyl lysine.Bioorganic & medicinal chemistry letters, , Oct-01, Volume: 19, Issue:19, 2009
[no title available]Journal of medicinal chemistry, , 10-14, Volume: 64, Issue:19, 2021
Small molecule activators of SIRT1 as therapeutics for the treatment of type 2 diabetes.Nature, , Nov-29, Volume: 450, Issue:7170, 2007
[no title available]Bioorganic & medicinal chemistry letters, , 11-01, Volume: 26, Issue:21, 2016
Development of pyrazolone and isoxazol-5-one cambinol analogues as sirtuin inhibitors.Journal of medicinal chemistry, , Apr-24, Volume: 57, Issue:8, 2014
Discovery of thieno[3,2-d]pyrimidine-6-carboxamides as potent inhibitors of SIRT1, SIRT2, and SIRT3.Journal of medicinal chemistry, , May-09, Volume: 56, Issue:9, 2013
Discovery of Dihydro-1,4-Benzoxazine Carboxamides as Potent and Highly Selective Inhibitors of Sirtuin-1.Journal of medicinal chemistry, , 05-13, Volume: 64, Issue:9, 2021
Sensitive fluorogenic substrates for sirtuin deacylase inhibitor discovery.European journal of medicinal chemistry, , Apr-15, Volume: 192, 2020
Discovery of potent and selective sirtuin 2 (SIRT2) inhibitors using a fragment-based approach.Journal of medicinal chemistry, , Oct-23, Volume: 57, Issue:20, 2014
Discovery of thieno[3,2-d]pyrimidine-6-carboxamides as potent inhibitors of SIRT1, SIRT2, and SIRT3.Journal of medicinal chemistry, , May-09, Volume: 56, Issue:9, 2013
Inhibitors of the NAD(+)-Dependent Protein Desuccinylase and Demalonylase Sirt5.ACS medicinal chemistry letters, , Dec-13, Volume: 3, Issue:12, 2012
Discovery of indoles as potent and selective inhibitors of the deacetylase SIRT1.Journal of medicinal chemistry, , Dec-15, Volume: 48, Issue:25, 2005
Synthesis and in Vitro and in Vivo Biological Evaluation of Tissue-Specific Bisthiazole Histone Deacetylase (HDAC) Inhibitors.Journal of medicinal chemistry, , 01-23, Volume: 63, Issue:2, 2020
Squaramides as novel class I and IIB histone deacetylase inhibitors for topical treatment of cutaneous t-cell lymphoma.Bioorganic & medicinal chemistry letters, , 09-15, Volume: 28, Issue:17, 2018
Discovery of 2-((4,6-dimethylpyrimidin-2-yl)thio)-N-phenylacetamide derivatives as new potent and selective human sirtuin 2 inhibitors.European journal of medicinal chemistry, , Jul-07, Volume: 134, 2017
Small molecule activators of SIRT1 as therapeutics for the treatment of type 2 diabetes.Nature, , Nov-29, Volume: 450, Issue:7170, 2007
Sirtuin inhibition and anti-cancer activities of ethyl 2-benzimidazole-5-carboxylate derivatives.MedChemComm, , Dec-01, Volume: 10, Issue:12, 2019
An overview of Sirtuins as potential therapeutic target: Structure, function and modulators.European journal of medicinal chemistry, , Jan-01, Volume: 161, 2019
[no title available]Bioorganic & medicinal chemistry letters, , 11-01, Volume: 26, Issue:21, 2016
Enables
This protein enables 7 target(s):
| Target | Category | Definition |
|---|
| protein binding | molecular function | Binding to a protein. [GOC:go_curators] |
| zinc ion binding | molecular function | Binding to a zinc ion (Zn). [GOC:ai] |
| enzyme binding | molecular function | Binding to an enzyme, a protein with catalytic activity. [GOC:jl] |
| NAD-dependent protein lysine deacetylase activity | molecular function | Catalysis of the reaction: N(6)-acetyl-L-lysyl-[protein] + NAD+ + H2O = L-lysyl-[protein] + 2''-O-acetyl-ADP-D-ribose + nicotinamide. [GOC:BHF, GOC:mah, RHEA:43636] |
| sequence-specific DNA binding | molecular function | Binding to DNA of a specific nucleotide composition, e.g. GC-rich DNA binding, or with a specific sequence motif or type of DNA e.g. promotor binding or rDNA binding. [GOC:jl] |
| NAD+ binding | molecular function | Binding to the oxidized form, NAD, of nicotinamide adenine dinucleotide, a coenzyme involved in many redox and biosynthetic reactions. [GOC:mah] |
| NAD-dependent histone deacetylase activity | molecular function | Catalysis of the reaction: histone N6-acetyl-L-lysine + H2O = histone L-lysine + acetate. This reaction requires the presence of NAD, and represents the removal of an acetyl group from a histone. [PMID:28450737] |
Located In
This protein is located in 3 target(s):
| Target | Category | Definition |
|---|
| nucleoplasm | cellular component | That part of the nuclear content other than the chromosomes or the nucleolus. [GOC:ma, ISBN:0124325653] |
| mitochondrion | cellular component | A semiautonomous, self replicating organelle that occurs in varying numbers, shapes, and sizes in the cytoplasm of virtually all eukaryotic cells. It is notably the site of tissue respiration. [GOC:giardia, ISBN:0198506732] |
| mitochondrial matrix | cellular component | The gel-like material, with considerable fine structure, that lies in the matrix space, or lumen, of a mitochondrion. It contains the enzymes of the tricarboxylic acid cycle and, in some organisms, the enzymes concerned with fatty acid oxidation. [GOC:as, ISBN:0198506732] |
Active In
This protein is active in 1 target(s):
| Target | Category | Definition |
|---|
| nucleus | cellular component | A membrane-bounded organelle of eukaryotic cells in which chromosomes are housed and replicated. In most cells, the nucleus contains all of the cell's chromosomes except the organellar chromosomes, and is the site of RNA synthesis and processing. In some species, or in specialized cell types, RNA metabolism or DNA replication may be absent. [GOC:go_curators] |
Part Of
This protein is part of 1 target(s):
| Target | Category | Definition |
|---|
| protein-containing complex | cellular component | A stable assembly of two or more macromolecules, i.e. proteins, nucleic acids, carbohydrates or lipids, in which at least one component is a protein and the constituent parts function together. [GOC:dos, GOC:mah] |
Involved In
This protein is involved in 10 target(s):
| Target | Category | Definition |
|---|
| chromatin remodeling | biological process | A dynamic process of chromatin reorganization resulting in changes to chromatin structure. These changes allow DNA metabolic processes such as transcriptional regulation, DNA recombination, DNA repair, and DNA replication. [GOC:jid, GOC:vw, PMID:12042764, PMID:12697820] |
| protein deacetylation | biological process | The removal of an acetyl group from a protein amino acid. An acetyl group is CH3CO-, derived from acetic [ethanoic] acid. [GOC:ai] |
| aerobic respiration | biological process | The enzymatic release of energy from inorganic and organic compounds (especially carbohydrates and fats) which requires oxygen as the terminal electron acceptor. [GOC:das, GOC:jl, ISBN:0140513590] |
| positive regulation of insulin secretion | biological process | Any process that activates or increases the frequency, rate or extent of the regulated release of insulin. [GOC:mah] |
| peptidyl-lysine deacetylation | biological process | The removal of an acetyl group from an acetylated lysine residue in a peptide or protein. [GOC:BHF, GOC:mah] |
| negative regulation of ERK1 and ERK2 cascade | biological process | Any process that stops, prevents, or reduces the frequency, rate or extent of signal transduction mediated by the ERK1 and ERK2 cascade. [GOC:add, ISBN:0121245462, ISBN:0896039986] |
| positive regulation of superoxide dismutase activity | biological process | Any process that activates or increases the frequency, rate or extent of superoxide dismutase activity. [GOC:TermGenie] |
| positive regulation of catalase activity | biological process | Any process that activates or increases the frequency, rate or extent of catalase activity. [GOC:TermGenie, PMID:24285797] |
| positive regulation of ceramide biosynthetic process | biological process | Any process that activates or increases the frequency, rate or extent of ceramide biosynthetic process. [GOC:dph] |
| negative regulation of reactive oxygen species metabolic process | biological process | Any process that stops, prevents or reduces the frequency, rate or extent of reactive oxygen species metabolic process. [GOC:mah] |