1.14.17.1	copper	contains copper	728562	
1.14.17.1	Cu2+	-	438609, 438631, 438632	
1.14.17.1	Cu2+	1.1 Cu2+/subunit, increasing stimulation of activity by addition of up to 1 Cu2+/subunit, further additions up to at least 4 Cu/subunit gave neither stimulation nor inhibition	438628	
1.14.17.1	Cu2+	2,6-dimethylphenyl isocyanide as the isocyanide ligand demonstrated, first: the formation of a mono-DIMPI-four-coordinate complex at each copper, second: the formation of complexes containing more than one isocyanide per copper	438635	
1.14.17.1	Cu2+	3 mol of copper per mol of tetramer, MW 290000	438623	
1.14.17.1	Cu2+	4 atoms of tightly bound copper per tetramer	438602	
1.14.17.1	Cu2+	a copper protein	438589, 438601, 438604, 438608, 438623, 438628	
1.14.17.1	Cu2+	about 8 Cu2+ per tetramer	438601	
1.14.17.1	Cu2+	DBH is an ascorbate-dependent glycoprotein that requires two type 2 bound copper ions per subunit to be active. copper sites are labile and termed CuH and CuM, respectively. CuH is coordinated to three histidines and CuM to two histidines and a methionine. CuM is involved in dioxygen binding and is the site for substrate hydroxylation, and CuH is the site of electron transfer	746431	
1.14.17.1	Cu2+	enzyme contains a constant amount of Cu2+, 2 mol per mol of protein, and a variable amount of Cu2+, copper content is a linear function of the purity of the enzyme	438608	
1.14.17.1	Cu2+	enzyme not activated by exogenous copper but activity decreases at high concentrations	438633	
1.14.17.1	Cu2+	enzyme-bound, required for activity	744950	
1.14.17.1	Cu2+	Km: 0.00003-0.0002 mM	438624	
1.14.17.1	Cu2+	required	745892	
1.14.17.1	Cu2+	The enzyme contains two copper centers, one performs the substrate hydroxylation, while the second is used for electron storage/transfer	674660	
1.14.17.1	Cu2+	tyramine can bind to either the Cu(I) or Cu(II) forms of TbetaM	704443	
1.14.17.1	Fe2+	0.0004 mM per mol of enzyme	438608	
1.14.17.1	Mg2+	regulates the translation of enzyme and affects the ratio of the two glycosylated forms of the enzyme	438637	
1.14.17.1	additional information	Cu2+, Mn2+, Ni2+, Co2+, Zn2+, Pb2+, Fe2+, Fe3+ reduce translation of enzyme at concentrations above 1.5 mM, Ni2+ and Cu2+ inhibit the glycosylation	438637	
1.14.17.1	additional information	the structure of the common DOMON (dopamine beta-monooxygenase N-terminal) domain reveals a possible metal-binding site and a ligand-binding pocket, coordinating residues are Asp99, Leu100, Ala115, and Asp130	746431	
1.14.17.1	NaCl	-	438603	
1.14.17.1	VO2+	1 VO2+/subunits during catalysis	438628