Literature summary 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.

Cloned(Commentary)

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

Protein Variants

EC Number	Protein Variants	Comment	Organism
1.21.4.2	C353	mutation of potentially redox-active motif UxxCxxC, 44% of wild-type peroxidase activity	Peptoclostridium acidaminophilum
1.21.4.2	C356	mutation of potentially redox-active motif UxxCxxC, 40% of wild-type peroxidase activity	Peptoclostridium acidaminophilum
1.21.4.2	additional information	mutation of potentially redox-active motif UxxCxxC results in still significant, but decreased peroxidase activity	Peptoclostridium acidaminophilum
1.21.4.2	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
1.21.4.2	U350	mutation of potentially redox-active motif UxxCxxC, 60% of wild-type peroxidase activity	Peptoclostridium acidaminophilum

KM Value [mM]

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

Organism

EC Number	Organism	UniProt	Comment	Textmining
1.21.4.2	Peptoclostridium acidaminophilum	-	-	-
1.21.4.2	Peptoclostridium acidaminophilum	-	protein B complex of glycine reductase has peroxidase activity using substrate dithiothreitol and hydroperoxide	-

Purification (Commentary)

EC Number	Purification (Comment)	Organism
1.21.4.2	-	Peptoclostridium acidaminophilum
1.21.4.2	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]

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

Substrates and Products (Substrate)

EC Number	Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
1.21.4.2	dithiothreitol + cumene hydroperoxide	peroxidase activity of enzyme	Peptoclostridium acidaminophilum	?	-	?
1.21.4.2	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	?	-	?

Subunits

EC Number	Subunits	Comment	Organism
1.21.4.2	More	heterologous enzyme is protected from degradation by full-length GrdE or by GrdE domains	Peptoclostridium acidaminophilum
1.21.4.2	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]

EC Number	Temperature Optimum [°C]	Temperature Optimum Maximum [°C]	Comment	Organism
1.21.4.2	20	22	peroxidase activity assay at	Peptoclostridium acidaminophilum

pH Optimum

EC Number	pH Optimum Minimum	pH Optimum Maximum	Comment	Organism
1.21.4.2	7.5	-	peroxidase activity assay at	Peptoclostridium acidaminophilum

Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.

Release 2023.1 (January 2023)