Proteins > NAD-dependent protein deacylase sirtuin-5, mitochondrial
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NAD-dependent protein deacylase sirtuin-5, mitochondrial
An NAD-dependent deacetylase sirtuin-5 that is encoded in the genome of human. [PRO:DNx, UniProtKB:Q9NXA8]
Synonyms
EC 2.3.1.-;
Regulatory protein SIR2 homolog 5;
SIR2-like protein 5
Research
Bioassay Publications (12)
| Timeframe | Studies on this Protein(%) | All Drugs % |
|---|
| pre-1990 | 0 (0.00) | 18.7374 |
| 1990's | 0 (0.00) | 18.2507 |
| 2000's | 0 (0.00) | 29.6817 |
| 2010's | 5 (41.67) | 24.3611 |
| 2020's | 7 (58.33) | 2.80 |
Compounds (27)
Drugs with Inhibition Measurements
Drugs with Activation Measurements
Drugs with Other Measurements
Identification of isoform/domain-selective fragments from the selection of DNA-encoded dynamic library.Bioorganic & medicinal chemistry, , 09-01, Volume: 45, 2021
A FRET-based assay for screening SIRT5 specific modulators.Bioorganic & medicinal chemistry letters, , Apr-15, Volume: 25, Issue:8, 2015
Inhibitors of the NAD(+)-Dependent Protein Desuccinylase and Demalonylase Sirt5.ACS medicinal chemistry letters, , Dec-13, Volume: 3, Issue:12, 2012
A FRET-based assay for screening SIRT5 specific modulators.Bioorganic & medicinal chemistry letters, , Apr-15, Volume: 25, Issue:8, 2015
Inhibition of the human deacylase Sirtuin 5 by the indole GW5074.Bioorganic & medicinal chemistry letters, , Jan-01, Volume: 23, Issue:1, 2013
Inhibitors of the NAD(+)-Dependent Protein Desuccinylase and Demalonylase Sirt5.ACS medicinal chemistry letters, , Dec-13, Volume: 3, Issue:12, 2012
Substrates for efficient fluorometric screening employing the NAD-dependent sirtuin 5 lysine deacylase (KDAC) enzyme.Journal of medicinal chemistry, , Jun-14, Volume: 55, Issue:11, 2012
Therapeutic Potential and Activity Modulation of the Protein Lysine Deacylase Sirtuin 5.Journal of medicinal chemistry, , 07-28, Volume: 65, Issue:14, 2022
Development of hetero-triaryls as a new chemotype for subtype-selective and potent Sirt5 inhibition.European journal of medicinal chemistry, , Oct-05, Volume: 240, 2022
Discovery of new human Sirtuin 5 inhibitors by mimicking glutaryl-lysine substrates.European journal of medicinal chemistry, , Dec-05, Volume: 225, 2021
Identification of the subtype-selective Sirt5 inhibitor balsalazide through systematic SAR analysis and rationalization via theoretical investigations.European journal of medicinal chemistry, , Nov-15, Volume: 206, 2020
A FRET-based assay for screening SIRT5 specific modulators.Bioorganic & medicinal chemistry letters, , Apr-15, Volume: 25, Issue:8, 2015
Inhibitors of the NAD(+)-Dependent Protein Desuccinylase and Demalonylase Sirt5.ACS medicinal chemistry letters, , Dec-13, Volume: 3, Issue:12, 2012
Substrates for efficient fluorometric screening employing the NAD-dependent sirtuin 5 lysine deacylase (KDAC) enzyme.Journal of medicinal chemistry, , Jun-14, Volume: 55, Issue:11, 2012
Enables
This protein enables 6 target(s):
| Target | Category | Definition |
|---|
| zinc ion binding | molecular function | Binding to a zinc ion (Zn). [GOC:ai] |
| 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] |
| protein-malonyllysine demalonylase activity | molecular function | Catalysis of the reaction: protein-malonyllysine + H2O => protein-lysine + malonate. This reaction is the removal of a malonyl group (CO-CH2-CO) from a malonylated lysine residue of a protein or peptide. [GOC:sp, PMID:21908771, PMID:22076378] |
| protein-succinyllysine desuccinylase activity | molecular function | Catalysis of the reaction: H2O + N(6)-succinyl-L-lysyl-[protein] + NAD+ = 2''-O-succinyl-ADP-D-ribose + L-lysyl-[protein] + nicotinamide. [GOC:sp, PMID:22076378] |
| protein-glutaryllysine deglutarylase activity | molecular function | Catalysis of the reaction: H2O + N(6)-glutaryl-L-lysyl-[protein] + NAD+ = 2''-O-glutaryl-ADP-D-ribose + L-lysyl-[protein] + nicotinamide. [GOC:dph, PMID:24703693] |
| 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] |
Located In
This protein is located in 5 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] |
| 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 intermembrane space | cellular component | The region between the inner and outer lipid bilayers of the mitochondrial envelope. [GOC:mah] |
| 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] |
| cytosol | cellular component | The part of the cytoplasm that does not contain organelles but which does contain other particulate matter, such as protein complexes. [GOC:hjd, GOC:jl] |
Active In
This protein is active in 1 target(s):
| Target | Category | Definition |
|---|
| 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] |
Involved In
This protein is involved in 12 target(s):
| Target | Category | Definition |
|---|
| 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] |
| mitochondrion organization | biological process | A process that is carried out at the cellular level which results in the assembly, arrangement of constituent parts, or disassembly of a mitochondrion; includes mitochondrial morphogenesis and distribution, and replication of the mitochondrial genome as well as synthesis of new mitochondrial components. [GOC:dph, GOC:jl, GOC:mah, GOC:sgd_curators, PMID:9786946] |
| regulation of ketone biosynthetic process | biological process | Any process that modulates the frequency, rate or extent of the chemical reactions and pathways resulting in the formation of a ketone, carried out by individual cells. [GOC:dph, GOC:tb] |
| negative regulation of cardiac muscle cell apoptotic process | biological process | Any process that decreases the rate or extent of cardiac cell apoptotic process, a form of programmed cell death induced by external or internal signals that trigger the activity of proteolytic caspases whose actions dismantle a cardiac muscle cell and result in its death. [GOC:BHF, GOC:dph, GOC:mtg_apoptosis, GOC:rl, GOC:tb] |
| response to nutrient levels | biological process | Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a stimulus reflecting the presence, absence, or concentration of nutrients. [GOC:mah] |
| protein demalonylation | biological process | The removal of a malonyl group (CO-CH2-CO), from an amino acid residue within a protein or peptide. [GOC:sp, PMID:22076378] |
| peptidyl-lysine demalonylation | biological process | The process of removing a malonyl group (CO-CH2-CO) from an malonylated lysine residue in a peptide or protein. [GOC:sp, PMID:22076378] |
| protein desuccinylation | biological process | The removal of a succinyl group (CO-CH2-CH2-CO) from a residue in a peptide or protein. [GOC:sp, PMID:22076378] |
| peptidyl-lysine desuccinylation | biological process | The removal of a succinyl group (CO-CH2-CH2-CO) from a succinylated lysine residue in a peptide or protein. [GOC:sp, PMID:22076378] |
| protein deglutarylation | biological process | The removal of a glutaryl group (CO-CH2-CH2-CH2-CO) from a residue in a peptide or protein. [GOC:dph, PMID:24703693] |
| 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] |
| epigenetic regulation of gene expression | biological process | A process that modulates the frequency, rate or extent of gene expression through chromatin remodeling either by modifying higher order chromatin fiber structure, nucleosomal histones, or cytosine methylation of DNA. Once established, this regulation may be maintained over many cell divisions. It can also be heritable in the absence of the instigating signal. [PMID:10521337, PMID:11498582, PMID:22243696, PMID:34414474] |