1.8.4.12	Fe2+	with Zn2+ in a ratio of 1 mol per mole of enzyme, tight metal binding	670824	
1.8.4.12	additional information	content of free cysteinyl residues in wild-type and mutant enzymes, MsrA and MsrB domains, overview	394110	
1.8.4.12	additional information	enzyme belongs to the metal-containing MsrB group I	658216	
1.8.4.12	additional information	isozyme MsrB1 contains selenocysteine, while isozymes MsrB2 and MsrB3 contain cysteine residues, the thioredoxin dependence is different for selenocysteine- and cysteine-containing enzyme, overview	670646	
1.8.4.12	additional information	native isozyme MsrB1 contains selenocysteine, while native isozymes MsrB2 and MsrB3 contain cysteine residues, the thioredoxin dependence is different for selenocysteine- and cysteine-containing enzyme, overview	670646	
1.8.4.12	additional information	PilB is a selenocysteine-containing enzyme	669501	
1.8.4.12	additional information	the major isozyme of MsrB, MsrB1, is a selenoprotein, selenium affects the expression of MsrB	668357	
1.8.4.12	additional information	the zinc:iron ratio is 8:2 to 6:4, metal content of wild-type and mutant enzymes, overview	670824	
1.8.4.12	additional information	wild-type MsrB of Neisseria meningitidis is no metal-binding enzyme, but contains a preformed metal binding site, metal binding to MsrB results in inhibition of binary complex formation between oxidized MsrB and reduced thioredoxin but not between reduced MsrB and substrate, metal content of wild-type and mutant enzymes, overview	670824	
1.8.4.12	selenium	selenocysteine-containing	684984	
1.8.4.12	selenium	selenoprotein	393076, 658212, 658704, 710848, 765497, 765804	
1.8.4.12	selenium	selenoprotein. Se status affects Msr (most likely through effects on the selenoprotein MsrB)	685479	
1.8.4.12	selenium	the presence of the selenium atom in its active site is critical for the catalytic function of this enzyme	763918	
1.8.4.12	selenium	the selenocysteine-containing Clostridium MsrB form exhibits 100fold higher activity than its Cys-containing form, revealing that selenocysteine provides the catalytic advantage of higher activity. A resolving Cys is required for the thioredoxin-dependent recycling process of the selenocysteine-containing form. Thus, thioredoxin can reduce the selenylsulfide bond, but its Trx-dependent recycling process is much less efficient compared to that for the disulfide bond in the Cys-containing form, demonstrating an obvious catalytic disadvantage	684729	
1.8.4.12	Zinc	marginal Zn deficiency has little effect on Msr in liver and kidney	685479	
1.8.4.12	Zinc	zinc-containing enzyme	684984	
1.8.4.12	Zn2+	about 50% of MsrB binds a zinc atom in opposite direction of the active site, enzyme contains the CXXC motif, binding of Zn2+ modulates the catalytic efficiency via structural changes	658215	
1.8.4.12	Zn2+	about 50% of MsrBs binds a zinc atom in opposite direction of the active site	658215	
1.8.4.12	Zn2+	binding by residues at positions 45, 48, 94, and 97, 2 CXXC-motifs, role in catalysis	658216	
1.8.4.12	Zn2+	contains zinc	726460	
1.8.4.12	Zn2+	enzyme belongs to the metal-containing MsrB group I, metal binding by 2 CXXC-motifs, role in catalysis	658216	
1.8.4.12	Zn2+	metalloenzyme, content determination	393076	
1.8.4.12	Zn2+	MsrB1 is a zinc-containing protein	712476	
1.8.4.12	Zn2+	with Fe2+ in a ratio of 1 mol per mole of enzyme, tight metal binding, the metal binding site is composed of two CXXC motifs located at the opposite side of the active site, role in catalysis and structural stability, overview	670824