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Keywords: deacetylase
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Biochem J (2018) 475 (24): 3921–3932.
Published: 14 December 2018
...Grace E. Adams; Aditya Chandru; Shaun M. Cowley At face value, the Sin3 histone deacetylase (HDAC) complex appears to be a prototypical co-repressor complex, that is, a multi-protein complex recruited to chromatin by DNA bound repressor proteins to facilitate local histone deacetylation and...
Biochem J (2013) 456 (1): 89–98.
Published: 24 October 2013
... deamination of 5-methyl-cytosine at the CpG dinucleotide, thereby preventing C to T mutations. SIRT1 is a member of class III NAD + -dependent histone/protein deacetylases. In the present study, we demonstrate that SIRT1 interacts with residues 67–110 of hTDG (human TDG). In addition, SIRT1 enhances TDG...
Includes: Supplementary data
Biochem J (2013) 454 (2): 239–247.
Published: 09 August 2013
... , BA1557 has been identified as the N -acetylglucosamine malate deacetylase (BshB); however, a high content of bacillithiol (~70%) was still observed in the B. anthracis ∆ BA1557 strain. Genomic analysis led to the proposal that another deacetylase could exhibit cross-functionality in bacillithiol...
Includes: Supplementary data
Biochem J (2008) 411 (2): 279–285.
Published: 27 March 2008
...Helen M. Cooper; Johannes N. Spelbrink It has recently been suggested that perhaps as many as 20% of all mitochondrial proteins are regulated through lysine acetylation while SIRT3 has been implicated as an important mitochondrial protein deacetylase. It is therefore of crucial importance that the...
Includes: Supplementary data
Biochem J (2007) 408 (1): 105–111.
Published: 29 October 2007
...Hiyaa S. Ghosh; James V. Spencer; Bobby Ng; Michael W. McBurney; Paul D. Robbins Sirt1 is an NAD + -dependent deacetylase that plays a role in cellular processes such as transcriptional regulation, stress response, longevity and apoptosis. Sirt1 deacetylates histone proteins and certain...
Biochem J (2007) 407 (3): 451–460.
Published: 12 October 2007
... pocket domain of Rb. p300 catalysed the acetylation of Rb, and SIRT1 was a potent deacetylase for Rb. The ability of SIRT1 to catalyse the deacetylation of Rb was dependent on NAD and was inhibited by the SIRT1 inhibitor nicotinamide. Deacetylated lysine residues within Rb formed a domain similar to the...
Biochem J (2007) 406 (3): 511–518.
Published: 29 August 2007
... indicate that the deacetylase Sir2/SIRT1, an enzyme promoting stress resistance and aging, is the target of resveratrol. Similarly, down-regulation of insulin-like pathways, of which PI3K (phosphoinositide 3-kinase) is a key mediator, promotes longevity and is an attractive strategy to fight cancer. We...
Includes: Supplementary data