2.3.1.39	?	x * 30000, SDS-PAGE	755875	
2.3.1.39	?	x * 35000, SDS-PAGE	486881	
2.3.1.39	?	x * 68000, recombinant GST-tagged enzyme, SDS-PAGE, x * 41500, about, sequence calculation	-, 737303	
2.3.1.39	monomer	1 * 35000, SDS-PAGE, alkylated: 1 * 35500, SDS-PAGE, native: 1 * 36500, SDS-PAGE	486863, 486882	
2.3.1.39	monomer	crystal structure	-, 688366	
2.3.1.39	monomer	malonyl transferase domain of EC 2.3.1.85, gel filtration	486896	
2.3.1.39	additional information	acyl carrier protein of fatty acid synthase interacts with malonyl-CoA-ACP-transacylase through the negatively charged helix II of acyl carrier protein. The affinity of polyketide synthase acyl carrier protein for malonyl-CoA-ACP-transacylase is lower than the affinity of the fatty acid synthase acyl carrier protein, and polyketide synthase acyl carrier protein may bind to malonyl-CoA-ACP-transacylase in a different manner	701440	
2.3.1.39	additional information	vertebrates, yeast and Mycobacteria fatty acid synthetases contain all individual activities on one or two multifunctional polypeptide chains, plant, Escherichia coli and other prokaryotic fatty acid synthases are non-associated systems of individual enzymes	486863	
2.3.1.39	pentamer	malonate decarboxylase holoenzyme is a heteropentamer, the active form: 1 * 60000, alpha-subunit, plus 1 * 33000, beta-subunit, plus 1 * 28000, gamma subunit, plus 1 * 13000, delta-subunit, plus 1 * 30000, epsilon-subunit. The epsilon subunit functions as malonyl-CoA:ACP transacylase	4866	
2.3.1.39	tetramer	malonate decarboxylase consists of the four subunits MdcA, MdcD, MdcE and MdcC in an apparent 1:1:1:1 stoichiometry. The preparation contains substoichiometric amounts of malonyl-CoA:ACP transacylase MdcH comigrating on SDS/PAGE with MdcD	686493