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Results 1 - 10 of 10
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EC Number Substrates Commentary Substrates Organism Products Commentary (Products) Reversibility
Display the reaction diagram Show all sequences 2.3.1.B27acetyl-CoA + VLIGKKPVMNY - Saccharolobus solfataricus CoA + VLIG-K(Ac)-KPVMNY - ?
Display the reaction diagram Show all sequences 2.3.1.B27acetyl-CoA + VLIGKKPVMNY - Saccharolobus solfataricus P2 CoA + VLIG-K(Ac)-KPVMNY - ?
Display the reaction diagram Show all sequences 2.3.1.B27acetyl-CoA + [DNA-binding protein Alba1]-L-lysine16 - Saccharolobus solfataricus CoA + [DNA-binding protein Alba1]-N6-acetyl-L-lysine16 - ?
Display the reaction diagram Show all sequences 2.3.1.B27acetyl-CoA + [DNA-binding protein Alba1]-L-lysine16 the DNA binding affinity of the chromatin protein Alba is regulated by acetylation of lysine16. Acetylation lowers the affinity of Alba for DNA. The acetyltransferase is conserved also in bacteria where it appears to play a role in metabolic regulation. The data suggest that Sulfolobus solfataricus has coopted this bacterial regulatory system to generate a rudimentary form of chromatin regulation Saccharolobus solfataricus CoA + [DNA-binding protein Alba1]-N6-acetyl-L-lysine16 - ?
Display the reaction diagram Show all sequences 2.3.1.B27acetyl-CoA + [DNA-binding protein Alba1]-L-lysine16 the Sulfolobus solfataricus protein acetyltransferase acetylates ALBA, an abundant nonspecific DNA-binding protein, on Lys16 to reduce its DNA affinity, and the Sir2 deacetylase reverses the modification to cause transcriptional repression. This represents a primitive model for chromatin regulation analogous to histone modification in eukaryotes Saccharolobus solfataricus CoA + [DNA-binding protein Alba1]-N6-acetyl-L-lysine16 - ?
Display the reaction diagram Show all sequences 2.3.1.B27acetyl-CoA + [DNA-binding protein Alba1]-L-lysine16 the enzyme specifically acetylates protein Alba1 (SSO0962) on L-lysine 16 Saccharolobus solfataricus CoA + [DNA-binding protein Alba1]-N6-acetyl-L-lysine16 - ?
Display the reaction diagram Show all sequences 2.3.1.B27acetyl-CoA + [DNA-binding protein Alba1]-L-lysine16 the DNA binding affinity of the chromatin protein Alba is regulated by acetylation of lysine16. Acetylation lowers the affinity of Alba for DNA. The acetyltransferase is conserved also in bacteria where it appears to play a role in metabolic regulation. The data suggest that Sulfolobus solfataricus has coopted this bacterial regulatory system to generate a rudimentary form of chromatin regulation Saccharolobus solfataricus P2 CoA + [DNA-binding protein Alba1]-N6-acetyl-L-lysine16 - ?
Display the reaction diagram Show all sequences 2.3.1.B27acetyl-CoA + [DNA-binding protein Alba1]-L-lysine16 the enzyme specifically acetylates protein Alba1 (SSO0962) on L-lysine 16 Saccharolobus solfataricus P2 CoA + [DNA-binding protein Alba1]-N6-acetyl-L-lysine16 - ?
Display the reaction diagram Show all sequences 2.3.1.B27acetyl-CoA + [DNA-binding protein Alba1]-L-lysine16 - Saccharolobus solfataricus P2 CoA + [DNA-binding protein Alba1]-N6-acetyl-L-lysine16 - ?
Display the reaction diagram Show all sequences 2.3.1.B27acetyl-CoA + [DNA-binding protein Alba1]-L-lysine16 the Sulfolobus solfataricus protein acetyltransferase acetylates ALBA, an abundant nonspecific DNA-binding protein, on Lys16 to reduce its DNA affinity, and the Sir2 deacetylase reverses the modification to cause transcriptional repression. This represents a primitive model for chromatin regulation analogous to histone modification in eukaryotes Saccharolobus solfataricus P2 CoA + [DNA-binding protein Alba1]-N6-acetyl-L-lysine16 - ?
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