2.3.1.255	?	consists of the subunits Nat1p, Ard1p, and Nat5p	659937	
2.3.1.255	?	x * 22000, SDS-PAGE	719333	
2.3.1.255	?	x * 26000, calculated from amino acid sequence	740508	
2.3.1.255	?	x * 27000 (Ard1p) + x * 99000 (Nat1p), Ard1p is the catalytic subunit, Nat1p is the auxiliary subunit	657745	
2.3.1.255	?	x * 27000, Ard1p, SDS-PAGE	-, 659935	
2.3.1.255	?	x * 27500, subunit ARD1, calculated from amino acid sequence	-, 740977	
2.3.1.255	?	x * 30000, FLAG-tagged enzyme, SDS-PAGE	703852	
2.3.1.255	?	x * 35000, SDS-PAGE	741046	
2.3.1.255	dimer	the Trypanosoma cruzi Nat A protein complex consists of an Esmeraldo-like catalytic NatA complex subunit ARD1/TcNaa10 and a non-Esmeraldo-like auxilliary NatA complex subunit Nat1/TcNaa15	-, 757472	
2.3.1.255	heterotrimer	-	705613	
2.3.1.255	heterotrimer	Nat1p, Nat5p and a catalytic subunit, Ard1p	706924	
2.3.1.255	monomer	active form	757723	
2.3.1.255	additional information	secondary structure prediction of MtRimI, overview	-, 755712	
2.3.1.255	additional information	size-exclusion analysis reveals that most recombinant hARD1/NAA10 form oligomers over time, resulting in the loss of KAT activity. After purification, rhARD1/NAA10 mainly exists in a high oligomeric state and has only a few monomers. The NAT activity is highest for the monomeric enzyme, about 2fold higher compared to the oligomeric enzyme and about 20% higher compared to the dimeric enzyme	757723	
2.3.1.255	additional information	the NatA enzyme complex is composed of the subunits Naa10 and Naa15	-, 758492	
2.3.1.255	additional information	the oligomeric recombinant hARD1/NAA10 loses the ability for lysine acetylation, while the monomeric form clearly shows lysine acetylation activity in vitro	757723