6.6.1.1	?	-	644254	
6.6.1.1	?	x * 150000, subunit ChlH, SDS-PAGE	-, 749215	
6.6.1.1	?	x * 153491, calculation from sequence of cDNA, ChlH subunit	644269	
6.6.1.1	?	x * 38000, SDS-PAGE, a construct expressing I subunit	644264	
6.6.1.1	?	x * 40000 + x * 70000 + x * 140000	661635	
6.6.1.1	?	x * 40000, SDS-PAGE, I subunit	644256	
6.6.1.1	?	x * 42000, SDS-PAGE, a construct expressing I subunit	644264	
6.6.1.1	?	x * 44000, SDS-PAGE, ChlI subunit	644270	
6.6.1.1	?	x * 46000, calculation from sequence of cDNA, I subunit	644254, 644256	
6.6.1.1	?	x * 60000, calculation from sequence of cDNA, D subunit	644254	
6.6.1.1	?	x * 73000, calculation from sequence of cDNA, D subunit	644254	
6.6.1.1	?	x * 82900, calculation from sequence of cDNA, D subunit	644274	
6.6.1.1	?	x * 87000, calculation from sequence of cDNA, D subunit	644254	
6.6.1.1	?	x * 90000-130000, gel filtration, BchI subunit	644261	
6.6.1.1	dimer	2 * 40000, BchI subunit	644275	
6.6.1.1	heterotrimer	1 * 148000 + 1 * 39000 + 1 * 73000, subunits ChlH, ChlI and ChlD	715033	
6.6.1.1	heterotrimer	1 * 150000 + 1 * 70000 + 1 * 40000, SDS-PAGE	747024	
6.6.1.1	homodimer	2 * 150000, subunit ChlH, SDS-PAGE	748752	
6.6.1.1	additional information	-	644254	
6.6.1.1	additional information	1 * 110000, gel filtration, BchH subunit	644265	
6.6.1.1	additional information	1 * 140000, BchH subunit	644275	
6.6.1.1	additional information	1 * 148000, gel filtration, ChlH subunit	644265	
6.6.1.1	additional information	ChlH forms high-molecular aggregates when preincubated with ATP and Mg2+	644265	
6.6.1.1	additional information	ChlI subunit forms high-molecular-mass aggregates	644258	
6.6.1.1	additional information	enzyme interacts with the next enzyme in the pathway, magnesium protoporphyrine IX methyltransferase BchM. Activitiy of BchM in presence of isoform BchH1 is 132% of the activity of BchM alone	687761	
6.6.1.1	additional information	enzyme interacts with the next enzyme in the pathway, magnesium protoporphyrine IX methyltransferase BchM. Activitiy of BchM in presence of isoform BchH2 is 157% of the activity of BchM alone	687761	
6.6.1.1	additional information	enzyme interacts with the next enzyme in the pathway, magnesium protoporphyrine IX methyltransferase BchM. Activitiy of BchM in presence of isoform BchH3 is 68% of the activity of BchM alone	687761	
6.6.1.1	additional information	enzyme is composed of subunits BchI, BchD, BchH. The BchIBchD complex has intrinsic ATPase activity, and addition of BchH greatly increased ATPase activity. This is concentration-dependent and gives sigmoidal kinetics. ATPase activity is about 40fold higher than magnesium chelatase activity and continues despite cessation of magnesium chelation, implying secondary roles for ATP hydrolysis	693170	
6.6.1.1	additional information	H subunit is a monomer and I subunit is a dimer, determined by dynamic-light-scattering studies	644254	
6.6.1.1	additional information	I subunit is hexameric	644255	
6.6.1.1	additional information	M1 and M2 domains of ChlD subunit participate in homodimerization and interaction between ChlI and ChlD	644260	
6.6.1.1	additional information	the 40000 Da subunit functions as a chaperon that is esential for the survival of the 70000 Da subunit. The ATPase activity of the 40000 Da subunit is essential for this function. Binding between the two subunits is not sufficient to maintain the 70000 Da subunit in the cell	661635	
6.6.1.1	additional information	the enzyme has three subunits, BchI, BchH and BchD	644254, 644255, 644264, 644275	
6.6.1.1	additional information	the enzyme has three subunits, ChlI, ChlH and ChlD	644254, 644256, 644274	
6.6.1.1	octamer	8 * 70000, D subunit, the molecular mass of the polymeric protein is approximately 550000 Da	644275	
6.6.1.1	trimer	1 * 40000 (I-subunit) + 1 * 70000 (D-subunit) + 1 * 140000 (H-subunit)	671881