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Literature summary for 1.21.4.2 extracted from

  • Groebe, T.; Reuter, M.; Gursinsky, T.; Soehling, B.; Andreesen, J.R.
    Peroxidase activity of selenoprotein GrdB of glycine reductase and stabilisation of its integrity by components of proprotein GrdE from Eubacterium acidaminophilum (2007), Arch. Microbiol., 187, 29-43.
    View publication on PubMed
Search for more literature for 1.21.4.2

Cloned(Commentary)

Cloned (Comment) Organism
expression of wild-type and mutant B protein complex components in Escherichia coli strain XL1-Blue Peptoclostridium acidaminophilum

Protein Variants

Protein Variants Comment Organism
C353 mutation of potentially redox-active motif UxxCxxC, 44% of wild-type peroxidase activity Peptoclostridium acidaminophilum
C356 mutation of potentially redox-active motif UxxCxxC, 40% of wild-type peroxidase activity Peptoclostridium acidaminophilum
additional information mutation of potentially redox-active motif UxxCxxC results in still significant, but decreased peroxidase activity Peptoclostridium acidaminophilum
additional information mutation of the potentially redox-active UxxCxxC motif in subunit GrdB of the B protein complex results in still signifiant, but decreased peroxidase activity, overview Peptoclostridium acidaminophilum
U350 mutation of potentially redox-active motif UxxCxxC, 60% of wild-type peroxidase activity Peptoclostridium acidaminophilum

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
 additional information kinetics of the DTT-dependent peroxidase activity of the protein B complex Peptoclostridium acidaminophilum

Organism

Organism UniProt Comment Textmining
Peptoclostridium acidaminophilum
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-
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Peptoclostridium acidaminophilum
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 protein B complex of glycine reductase has peroxidase activity using substrate dithiothreitol and hydroperoxide
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Purification (Commentary)

Purification (Comment) Organism
-
 Peptoclostridium acidaminophilum
copurification of recombinant GrdE with recombinant Strep-tagged GrdB, native DTT-dependent peroxidase activity 14fold by anion exchange and hydrophobic interaction chromatography, ammonium sulfate fractionation, and gel filtration Peptoclostridium acidaminophilum

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
additional information
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 the protein B complex shows 1.7 U/mg peroxidase activity with DTT and cumene hydroperoxide as substrates Peptoclostridium acidaminophilum

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
dithiothreitol + cumene hydroperoxide peroxidase activity of enzyme Peptoclostridium acidaminophilum ?
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 ?
additional information the B protein complex, consisting of the selenocysteine-containing GrdB subunit and two subunits, which are derived from the GrdE proprotein, shows 1.7 U/mg peroxidase activity with DTT and cumene hydroperoxide as substrates, the protein exhibits DTT- as well as NADPH-dependent peroxidase activity, overview Peptoclostridium acidaminophilum ?
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 ?

Subunits

Subunits Comment Organism
More heterologous enzyme is protected from degradation by full-length GrdE or by GrdE domains Peptoclostridium acidaminophilum
More the enzyme consists of three subunits A, B, and C. The protein B-complex consists of the selenocysteine-containing GrdB subunit, subunit B, and two subunits, which derive from the GrdE proprotein, one of which shows peroxidase activity and protects the sensitive selenoproteins in the organism Peptoclostridium acidaminophilum

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
20 22 peroxidase activity assay at Peptoclostridium acidaminophilum

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.5
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 peroxidase activity assay at Peptoclostridium acidaminophilum