High impact information on HAT1

• While no other isozymic forms of nuclear acetyltransferase were detected, the enzyme exhibits the properties of both nuclear isozymic forms which have been reported, histone acetyltransferase A and DB, observed in calf thymus and bovine lymphocytes, respectively [1].
• Calf liver nuclear N-acetyltransferases. Purification and properties of two enzymes with both spermidine acetyltransferase and histone acetyltransferase activities [2].
• The same protein catalyzes the reaction with both substrates; this is shown by a constant ratio of spermidine to histone activity over a 5,000-fold purification and identical heat denaturation kinetics for both spermidine and histone acetyltransferase activity with each enzyme [2].
• Kinetic mechanism of the reaction catalyzed by nuclear histone acetyltransferase from calf thymus [3].
• Quantification of histone acetyltransferase and histone deacetylase transcripts during early bovine embryo development [4].

Biological context of HAT1

• Both peptides could be acetylated by a partially purified histone acetyltransferase preparation derived from calf thymus. epsilon-Amino groups of lysyl residues were the sites of the acetylation [5].

Anatomical context of HAT1

• The histone acetyltransferase (EC 2.3.1.-) activity of calf endometrium cytosol has been separated into three separate activities by stepwise chromatography on DEAE-cellulose [6].

References