2.2.1.6	ATP	activates	395883	
2.2.1.6	FAD	-	395875, 395911, 657718, 657720, 657724, 658223, 667251, 671290, 671854, 672368, 672568, 672865, 672867, 673626, 674354, 675377, 677228, 697061, 697349, 699740, 719010, 733241, 733685, 735336, 736351, 740761, 755711, 756475, 756700, 757918, 757919, 758232, 758241, 758259	
2.2.1.6	FAD	0.005 mM, 35-40% enhancement of activity	395872	
2.2.1.6	FAD	absolutly required for isoenzyme I and II, no requirement for isoenzyme III	395884	
2.2.1.6	FAD	apparent Km value 0.00015 mM	733241	
2.2.1.6	FAD	contains bound FAD, 0.88 mol per mol of protomer of 69000 Da	395879	
2.2.1.6	FAD	dependent on	695852, 733745, 733747	
2.2.1.6	FAD	Km value 0.00033 mM	719329	
2.2.1.6	FAD	Km value 0.061 microM	719117	
2.2.1.6	FAD	Km: 0.00016 mM for isoenzyme I	395887	
2.2.1.6	FAD	Km: 0.0003 mM	395885, 395915	
2.2.1.6	FAD	Km: 0.0004 mM	395921	
2.2.1.6	FAD	no requirement	395894, 395914	
2.2.1.6	FAD	no stimulation	395892	
2.2.1.6	FAD	noncovalently bound, one FAD per monomer	733657	
2.2.1.6	FAD	one molecule per enzyme molecule	733089, 733660	
2.2.1.6	FAD	partial requirement for isoenzyme III	395884	
2.2.1.6	FAD	required	395885, 395886, 395894, 395915, 395923, 733241, 733597, 734625, 734994	
2.2.1.6	FAD	required as cofactor	395902	
2.2.1.6	FAD	required by isoenzyme I, no requirement by isoenzyme III	395887	
2.2.1.6	FAD	required for the enzyme in anabolic function, but not in catabolic function, the conserved motif 372RFDDR376 is a possible determinant of the FAD-dependent and herbicide-resistant properties of tobacco, overview	672866	
2.2.1.6	FAD	required, presence of FAD in AHAS is an evolutionary relic of the ancestry of its sub-family of ThDP-dependent enzymes	700782	
2.2.1.6	FAD	required, presence of FAD in AHAS is an evolutionary relic of the ancestry of its sub-family of ThDP-dependent enzymes, binding structure, overview	700782	
2.2.1.6	FAD	residues W573 is structurally important for FAD binding	672868	
2.2.1.6	FAD	the anabolic enzyme form is dependent on the presence of FAD, structure of the enamine-FAD adduct	733685	
2.2.1.6	FAD	the anabolic enzyme form is dependent on the presence of FAD, structure of the enamine-FAD adduct, reaction mechanism molecular modeling	733685	
2.2.1.6	FAD	the flavin plays a crucial role in the structural integrity, and is reduced in the course of catalysis as a result of an internal redox side reaction	673213	
2.2.1.6	FAD	the secondary structure of the FAD binding domain of large subunit ilvB is similar to the structure of this domain in the catalytic subunit of yeast AHAS. The regulatory subunit ilvN interacts with ilvBalpha and ilvBbeta domains of the catalytic subunit and not with the ilvBgamma domain. ilvN binds close to the FAD binding site in ilvBbeta and proximal to the intrasubunit ilvBalpha/ilvBbeta domain interface	699605	
2.2.1.6	FMN	stimulates, Km: 0.0013 mM	395921	
2.2.1.6	additional information	FAD-independent enzyme	733987	
2.2.1.6	additional information	spectral analysis and kinetics of cofactor binding, overview	672865	
2.2.1.6	additional information	the crystal structure shows a homotetramer with one noncovalently bound FAD and one thiamine diphosphate per monomer	733657	
2.2.1.6	additional information	the enzyme is not FAD-dependent	733744	
2.2.1.6	O2	each subunit contains two molecules of oxygen (O2(I) and O2(II))	756475	
2.2.1.6	riboflavin	plus 10 mM phosphate, stimulates	395921	
2.2.1.6	thiamine diphosphate	-	395873, 395886, 395911, 657852, 658223, 667251, 671290, 671854, 672568, 672865, 672866, 672867, 674354, 675377, 677228, 697061, 697349, 699740, 733241, 733658, 733685, 733744, 733745, 733747, 733987, 733995, 734625, 734734, 734841, 734978, 734994, 735039, 735336, 755711, 756075, 756209, 756475, 756622, 756700, 757918, 757919, 758232, 758241, 758259	
2.2.1.6	thiamine diphosphate	apparent Km value 0.057 mM	733241	
2.2.1.6	thiamine diphosphate	binding kinetics	673626	
2.2.1.6	thiamine diphosphate	dependent on	672368, 695852, 733088, 733241, 733597, 733744, 733747, 734625, 734841, 734978, 735336	
2.2.1.6	thiamine diphosphate	dependent on, located centrally in the active site of cALS with a unique V-conformation at the dimer interface to play a central role of intramolecular protontransfer in the catalytic cycle. In catalysis, a divalent metal ion Mg2+ serves to anchor the diphosphate moiety of thiamine diphosphate at the active site of the catalbolic enzyme	733987	
2.2.1.6	thiamine diphosphate	dependent on, one molecule per enzyme molecule	733089, 733660	
2.2.1.6	thiamine diphosphate	dependent on, one thiamine diphosphate per monomer	733657	
2.2.1.6	thiamine diphosphate	dependent on, the bound cofactor adopts a V-conformation in the active site, fixing the 4'-NH2 group very close to the C2-H of the thiazolium group	673213	
2.2.1.6	thiamine diphosphate	dependent on, the cofactor plays a key role in catalysis. The thiamine diphosphate binding pocket contains the highly conserved proline 126 residue, binding pocket structure, overview. Thiamine diphosphate is located centrally in the active site of AHAS with a unique V-conformation at the dimer interface. In the dimeric structure, one subunit is in contact with the diphosphate moiety of thiamine diphosphate, and the other subunit is in contact with the aminopyrimidine moiety	733745	
2.2.1.6	thiamine diphosphate	dependent on, the thiamine function of ThDP interacts with residues of one monomer and the adjacent monomer	733658	
2.2.1.6	thiamine diphosphate	dependent on, TPP binding site of the model structure of enzyme TtALS, overview	735039	
2.2.1.6	thiamine diphosphate	dependent on, upon removal of the cofactor, the activity of the enzyme is completely abolished and again restored by readdition of thiamine diphosphate. ThDP has a central role in the enzymes catalytic mechanism. In the active site of enzyme, it is located at its centre with a unique V-conformation at the dimer interface. Decarboxylation of pyruvate is carried out by ThDP	733685	
2.2.1.6	thiamine diphosphate	dependent on, upon removal of the cofactor, the activity of the enzyme is completely abolished and again restored by readdition of thiamine diphosphate. ThDP has a central role in the enzyymes catalytic mechanism. In the active site of enzyme, it is located at its centre with a unique V-conformation at the dimer interface. Decarboxylation of pyruvate is carried out by ThDP	733685	
2.2.1.6	thiamine diphosphate	K0.5 value for holoenzyme 0.0055 mM, for the isolated large subunit 0.24 mM	736351	
2.2.1.6	thiamine diphosphate	Km value 0.0092 mM	719329	
2.2.1.6	thiamine diphosphate	Km value 0.027 mM	719375	
2.2.1.6	thiamine diphosphate	Km value 0.036 mM	719375	
2.2.1.6	thiamine diphosphate	Km value 0.2 mM	719117	
2.2.1.6	thiamine diphosphate	Km: 0.0012 mM	395885, 395914	
2.2.1.6	thiamine diphosphate	Km: 0.0015 mM	395879	
2.2.1.6	thiamine diphosphate	Km: 0.0016	395921	
2.2.1.6	thiamine diphosphate	Km: 0.0031 mM	395875	
2.2.1.6	thiamine diphosphate	Km: 0.0032 mM	395922	
2.2.1.6	thiamine diphosphate	Km: 0.0033 mM	395875	
2.2.1.6	thiamine diphosphate	Km: 0.0087 mM for isoenzyme I, 0.026 mM for isoenzyme III	395887	
2.2.1.6	thiamine diphosphate	Km: 0.11 mM	395915	
2.2.1.6	thiamine diphosphate	Ks value 0.042 mM	720392	
2.2.1.6	thiamine diphosphate	required after dialysis	395875	
2.2.1.6	thiamine diphosphate	required as cofactor	395872, 395873, 395875, 395879, 395885, 395887, 395894, 395896, 395902, 395906, 395914, 395915, 395921, 395922	
2.2.1.6	thiamine diphosphate	required cofactor, apparent Km: 0.0088 mM	727336	
2.2.1.6	thiamine diphosphate	required, ThDP is anchored in the active site by a divalent metal ion cofactor such as Mg2+	700782	
2.2.1.6	thiamine diphosphate	residue Glu47 is involved in cofactor activation, substrate binding, and product elimination and plays a crucial catalytic role in the carboligation of the acceptor and the hydroxyethyl-thiamine diphosphate enamine intermediate. The Glu47-cofactor proton shuttle acts in concert with Gln110 in the carboligation	718895	
2.2.1.6	thiamine diphosphate	saturated at 0.5 mM thiamine diphosphate	395872	
2.2.1.6	thiamine diphosphate	stimulates	395892	
2.2.1.6	thiamine diphosphate	the mobile loop comprising residues 567-582 on the C-terminus are involved in the binding/stabilization of the active dimer and thiamin diphosphate binding, overview	672868