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Fe2+
-
with Zn2+ in a ratio of 1 mol per mole of enzyme, tight metal binding
selenium
selenocysteine-containing
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
selenium
-
selenocysteine-containing
selenium
selenocysteine-containing
selenium
the presence of the selenium atom in its active site is critical for the catalytic function of this enzyme
selenium
selenocysteine-containing
selenium
-
selenoprotein. Se status affects Msr (most likely through effects on the selenoprotein MsrB)
selenium
-
selenocysteine-containing
Zinc
-
zinc-containing enzyme
Zinc
zinc-containing enzyme
Zinc
zinc-containing enzyme
Zinc
-
marginal Zn deficiency has little effect on Msr in liver and kidney
Zn2+
-
about 50% of MsrBs binds a zinc atom in opposite direction of the active site
Zn2+
-
enzyme belongs to the metal-containing MsrB group I, metal binding by 2 CXXC-motifs, role in catalysis
Zn2+
metalloenzyme, content determination
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
Zn2+
-
binding by residues at positions 45, 48, 94, and 97, 2 CXXC-motifs, role in catalysis
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
Zn2+
-
metalloenzyme, content determination
Zn2+
MsrB1 is a zinc-containing protein
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
Zn2+
-
enzyme belongs to the metal-containing MsrB group I, metal binding by 2 CXXC-motifs, role in catalysis
Zn2+
-
enzyme belongs to the metal-containing MsrB group I, metal binding by 2 CXXC-motifs, role in catalysis
Zn2+
-
about 50% of MsrBs binds a zinc atom in opposite direction of the active site
additional information
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the major isozyme of MsrB, MsrB1, is a selenoprotein, selenium affects the expression of MsrB
additional information
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enzyme belongs to the metal-containing MsrB group I
additional information
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the zinc:iron ratio is 8:2 to 6:4, metal content of wild-type and mutant enzymes, overview
additional information
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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
additional information
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the major isozyme of MsrB, MsrB1, is a selenoprotein, selenium affects the expression of MsrB
additional information
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isozyme MsrB1 contains selenocysteine, while isozymes MsrB2 and MsrB3 contain cysteine residues, the thioredoxin dependence is different for selenocysteine- and cysteine-containing enzyme, overview
additional information
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the major isozyme of MsrB, MsrB1, is a selenoprotein, selenium affects the expression of MsrB
additional information
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PilB is a selenocysteine-containing enzyme
additional information
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content of free cysteinyl residues in wild-type and mutant enzymes, MsrA and MsrB domains, overview
additional information
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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
additional information
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the major isozyme of MsrB, MsrB1, is a selenoprotein, selenium affects the expression of MsrB