1.1.3.4	FAD	-	389792, 389802, 389804, 389827, 389836, 389837, 654780, 695717, 695790, 696864, 696865, 699078, 699600, 699771, 710858, 710903, 710920, 712059, 712533, 712857, 725199, 741479, 741835, 742144, 742213, 742360, 743105, 743193, 743283, 743644, 743744, 743759, 743775, 762774	
1.1.3.4	FAD	1.5 mol of flavin per mol of protein	389785	
1.1.3.4	FAD	1.76 nmol FAD per nmol enzyme	389833	
1.1.3.4	FAD	2 mol per mol of enzyme	389784, 389805, 389806	
1.1.3.4	FAD	4 mol flavin per mol of enzyme	389828	
1.1.3.4	FAD	a flavoenzyme with a tightly but non-covalently bound FAD cofactor	743824	
1.1.3.4	FAD	a flavoprotein, the flavin cofactor is covalently linked to the polypeptide chain, covalent anchoring of the FAD cofactor is an autocatalytic process and that only occurs upon correct folding of the polypeptide chain	695833	
1.1.3.4	FAD	bound	673385	
1.1.3.4	FAD	coenzyme FAD acts as electron shuttle during catalytic action of the enzyme. The FAD extinction is used for enzyme quantification	741632	
1.1.3.4	FAD	covalently bound to the recombinant protein of Mala s12, flavin content per monomer of protein calculated	684268	
1.1.3.4	FAD	defined as flavoprotein oxidase, two very tightly bound FAD molecules per dimer, kinetic behavior	389803	
1.1.3.4	FAD	dependent on, the FAD cofactor is not covalently but tightly bound to the enzyme domain, that consists of a five-stranded beta-sheet sandwiched between a three-stranded beta-sheet and three alpha-helices	743597	
1.1.3.4	FAD	dimerization is only possible with the proper incorporation of the cofactor in the FAD-binding pocket	726896	
1.1.3.4	FAD	dissociation of FAD from the holoenzyme is responsible for the thermal inaction of the enzyme	656139	
1.1.3.4	FAD	each monomer has one co-enzyme molecule of FAD, which acts as an electron receptor during catalysis	743857	
1.1.3.4	FAD	each subunit of dimeric GOD contains one tightly bound FAD as cofactor	710908	
1.1.3.4	FAD	electron transfer between FAD centers and metal electrodes after chemical modification of enzyme	389817	
1.1.3.4	FAD	enzyme pen-GOx contains one mol of tightly but not covalently bound FAD cofactor at the active site of each subunit. The FAD-binding domain of GOx is formed by a beta-sheet lid. The lid prevents the release of FAD from the dimer. Loosening of tertiary structure leads to opening of this lid, causing FAD loss anddissociation of the dimer. Loss of FAD from GOx is concurrent with tertiary structure loss. FAD, especially isoalloxazine, is important for the catalytic activity for beta-D-glucose. The binding of FAD cofactor also plays a key role on the catalytic activity of flavoproteins for the correct folding, assembly and protein stability. The three-dimensional structure of the glucose oxidase is stabilized by FAD, which can act as a redox carrier in catalysis	743111	
1.1.3.4	FAD	flavin-dependent oxidase with covalently linked FAD which is located at the bottom of a funnel-shaped pocket that forms the active site	696297	
1.1.3.4	FAD	flavoenzyme	676974	
1.1.3.4	FAD	not detectable in honey enzyme	389818	
1.1.3.4	FAD	semiempirical quantum chemical calculations are used to investigate the role of FAD in the catalytic oxidation of glucose. Only the hydride ion is transferred to the FAD coenzyme	728045	
1.1.3.4	FAD	the active site holds the tightly, non-covalently bound FAD cofactor	743277	
1.1.3.4	flavin	both the thermal and chemical denaturation of the enzyme cause dissociation of the flavin cofactor	656254	
1.1.3.4	Flavin-hypoxanthine dinucleotide	FHD, can substitute FAD	389802	
1.1.3.4	additional information	FAD-binding site studies, active site geometry	389827	
1.1.3.4	additional information	specification of the relative contribution of structure and dynamics to the catalytic activity, using infrared absorption spectroscopy of the amide I' band, tryptophan fluorescence quenching and hydrogen isotopic exchange on the oxidized and reduced enzymes	389836