2.3.1.B27: protein acetyltransferase (Alba1-protein acetylating)
This is an abbreviated version!
For detailed information about protein acetyltransferase (Alba1-protein acetylating), go to the full flat file.
Reaction
Synonyms
SSO2813, ssPat
ECTree
2.3.1.B27 protein acetyltransferase (Alba1-protein acetylating)Advanced search results
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Natural Substrates Products on EC 2.3.1.B27 - protein acetyltransferase (Alba1-protein acetylating)
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NATURAL SUBSTRATE 
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
acetyl-CoA + [DNA-binding protein Alba1]-L-lysine16
CoA + [DNA-binding protein Alba1]-N6-acetyl-L-lysine16
acetyl-CoA + [DNA-binding protein Alba1]-L-lysine16
CoA + [DNA-binding protein Alba1]-N6-acetyl-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
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-
?
acetyl-CoA + [DNA-binding protein Alba1]-L-lysine16
CoA + [DNA-binding protein Alba1]-N6-acetyl-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
-
-
?
acetyl-CoA + [DNA-binding protein Alba1]-L-lysine16
CoA + [DNA-binding protein Alba1]-N6-acetyl-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
-
-
?
acetyl-CoA + [DNA-binding protein Alba1]-L-lysine16
CoA + [DNA-binding protein Alba1]-N6-acetyl-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
-
-
?
