1.4.9.1	8-hydroxyquinoline	slight	321	
1.4.9.1	amicyanin mutant M98K	mutant acts as a competitive inhibitor in the reaction of native amicyanin with methylamine dehydrogenase indicating that the M98K mutation has not affected the affinity for its natural electron donor. The crystal structure of M98K amicyanin reveals an overall structure very similar to native amicyanin but the type I binding site is occupied by zinc instead of copper	165859	
1.4.9.1	Borohydride	-	4505	
1.4.9.1	Cuprizone	-	3994	
1.4.9.1	cyclopropylamine	mechanism-based inhibitor. The resulting inactivation is accompanied by the formation of a covalent cross-link between the alpha and beta subunits of the enzyme. No cross-linking is seen with mutant enzymes alphaF55A or alphaF55I mutant enzymes. With mutant enzyme alphaF55E cross-linking of subunits is observed	34526	
1.4.9.1	hydrazine	-	684	
1.4.9.1	hydroxylamine	-	85	
1.4.9.1	iodoacetate	-	93	
1.4.9.1	isoniazid	-	851	
1.4.9.1	KCN	-	161	
1.4.9.1	additional information	immobilized enzyme: little change in sensitivity to inhibition	2	
1.4.9.1	n-Butyraldehyde	-	3828	
1.4.9.1	N-ethylmaleimide	-	49	
1.4.9.1	Neocuproine	slight	4845	
1.4.9.1	p-chloromercuribenzoate	-	43	
1.4.9.1	p-Nitrophenylhydrazine	-	30313	
1.4.9.1	phenylhydrazine	-	398	
1.4.9.1	phenylhydrazine	O6 of cysteine tryptophylquinone is the site of inhibitory attack by phenylhydrazine	398	
1.4.9.1	Quinacrine	-	1593	
1.4.9.1	Quinine	slight	2219	
1.4.9.1	Semicarbazide	-	382