Title : Caffeine Targets SIRT3 to Enhance SOD2 Activity in Mitochondria.

Pub. Date : 2020

PMID : 33015038






5 Functional Relationships(s)
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Compound Name
Protein Name
Organism
1 Sirtuin 3 (SIRT3) is the major mitochondrial nicotinamide adenine dinucleotide (NAD+)-dependent deacetylase, which deacetylates two critical lysine residues (lysine 68 and lysine 122) on SOD2 and promotes its antioxidative activity. NAD sirtuin 3 Homo sapiens
2 Sirtuin 3 (SIRT3) is the major mitochondrial nicotinamide adenine dinucleotide (NAD+)-dependent deacetylase, which deacetylates two critical lysine residues (lysine 68 and lysine 122) on SOD2 and promotes its antioxidative activity. NAD sirtuin 3 Homo sapiens
3 Sirtuin 3 (SIRT3) is the major mitochondrial nicotinamide adenine dinucleotide (NAD+)-dependent deacetylase, which deacetylates two critical lysine residues (lysine 68 and lysine 122) on SOD2 and promotes its antioxidative activity. NAD sirtuin 3 Homo sapiens
4 Sirtuin 3 (SIRT3) is the major mitochondrial nicotinamide adenine dinucleotide (NAD+)-dependent deacetylase, which deacetylates two critical lysine residues (lysine 68 and lysine 122) on SOD2 and promotes its antioxidative activity. NAD sirtuin 3 Homo sapiens
5 Mechanistically, caffeine bound to SIRT3 with high affinity (K D = 6.858 x 10-7 M); the binding affinity between SIRT3 and its substrate acetylated p53 was also 9.03 (without NAD+) or 6.87 (with NAD+) times higher in the presence of caffeine. NAD sirtuin 3 Homo sapiens