2.6.1.44	?	x * 41736, calculated	663368	
2.6.1.44	?	x * 43000, SDS-PAGE	689026	
2.6.1.44	?	x * 50000, about, SDS-PAGE	758712	
2.6.1.44	?	x * 50000, recombinant His-tagged enzyme, SDS-PAGE	-, 759951	
2.6.1.44	?	x * 50000, SDS-PAGE	-, 759951	
2.6.1.44	?	x * 53300, calculated	663117	
2.6.1.44	?	x * 53400, calculated	663117	
2.6.1.44	dimer	2 * 38000, isoenzyme 1, SDS-PAGE	640067	
2.6.1.44	dimer	2 * 40000, SDS-PAGE	640071	
2.6.1.44	dimer	2 * 43000, homodimer	640084	
2.6.1.44	dimer	2 * 43000, immunoreaction	640075	
2.6.1.44	dimer	2 * 43000, SDS-PAGE	640075, 640078, 640081, 640084, 640086	
2.6.1.44	dimer	2 * 44400, homodimer, recombinant enzyme, SDS-PAGE	640077	
2.6.1.44	dimer	2 * 45000, holoenzyme, SDS-PAGE	640074	
2.6.1.44	dimer	2 * 45000, SDS-PAGE	-, 640082, 640083	
2.6.1.44	dimer	crystal structure, enzyme in solution, catalytic enzyme form	759257	
2.6.1.44	dimer	crystallization data	661283	
2.6.1.44	homodimer	-	-, 674458, 703680, 721718, 758763	
2.6.1.44	homodimer	2 * 43000, SDS-PAGE	671206	
2.6.1.44	homodimer	gel filtration	721754, 722393	
2.6.1.44	homodimer	structure modeling with monomer-monomer interface and active site, overview	759584	
2.6.1.44	homodimer	x-ray crystallography	674708	
2.6.1.44	monomer	1 * 45000, apoenzyme, SDS-PAGE	640074	
2.6.1.44	monomer or dimer	the enzyme displays a a dimer-monomer equilibrium	758860	
2.6.1.44	additional information	analysis of wild-type and mutants after partial digestions using trypsin. Partial digestion by trypsin provides an indicator of proper folding of the enzyme, while for some mutants, sensitivity to trypsin can be ameliorated by addition of pyridoxal 5'-phosphate or aminooxyacetic acid	689026	
2.6.1.44	additional information	Arg118, Phe238 and Phe240 are interfacial residues not essential for transaminase activity but important for dimer-monomer dissociation. AGT dimer interface model, overview. A synergic role of the residues Arg118 and Phe240 exist on the formation of the dimer of AGT-Mi, and substitution of both Phe238 and Phe240 with Ser might be relevant in preventing monomer-monomer aggregation. Proposed folding and dimerization pathway of wild-type AGT-Mi and of mutant I244T-Mi and F152T-Mi variant, overviews	758860	
2.6.1.44	additional information	biochemical properties of Pro11 and Ile56 variants: secondary, tertiary, and quaternary structures, overview	759779	
2.6.1.44	additional information	dimerization is considered a crucial event, because it is supposed to influence the overall stability of the protein as well as its intracellular fate, including, in particular, the correct peroxisomal localization. Rigid-body protein-protein docking simulations aiming at predicting and analyzing the quaternary structure of proteins using the structure of dimeric AGT in complex with the tetratricopeptide repeat (TPR) domain of human Pex5p (PDB ID 3R9A), overview	759584	
2.6.1.44	additional information	N-terminal animo acid sequence	662014	
2.6.1.44	additional information	the two allelic forms consist of a wild-type major allele, AGTma, and a minor allele, AGTmi. Wild-type minor allele displays about 46-50% of the activity of the major allele	687769	
2.6.1.44	tetramer	-	640070	
2.6.1.44	tetramer	4 * 42000, SDS-PAGE, 4 * 45169, claculated	662014	
2.6.1.44	tetramer	4 * 50000, mitochondrial holoenzyme, antibody cross reaction	640074	
2.6.1.44	tetramer	4 * 56000, SDS-PAGE	640068	
2.6.1.44	tetramer	in the enzyme crystal, another dimer related by noncrystallographic symmetry makes close interactions to form a tetramer mediated in part by an extra carboxyl-terminal helix conserved in plant homologues of AGT1	759257