Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 2.5.1.18 extracted from

  • Hearne, J.L.; Colman, R.F.
    Catalytically active monomer of class mu glutathione transferase from rat (2006), Biochemistry, 45, 5974-5984.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
expression of wild-type and mutant enzymes in Escherichia coli strain JM105 Rattus norvegicus

Protein Variants

Protein Variants Comment Organism
D97K site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme Rattus norvegicus
D97R site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme Rattus norvegicus
E100K site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme Rattus norvegicus
E100R site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme Rattus norvegicus
additional information construction of the monomeric mutant isozyme M1, GST M1, by introducing point mutations in the electrostatic region of the subunit interface and residues Arg77, Asp97, Glu100, Asn101, the mutation leads to formation of monomers instead of dimers and partially reduced activity, at 3 M KBr GST M1 has a specific activity close to that of GST M1-1, overview Rattus norvegicus
N101D site-directed mutagenesis, the mutant shows increased activity compared to the wild-type enzyme Rattus norvegicus
N101K site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme Rattus norvegicus
R77E site-directed mutagenesis, the mutant shows increased activity compared to the wild-type enzyme Rattus norvegicus
R77Q site-directed mutagenesis, the mutant shows increased activity compared to the wild-type enzyme Rattus norvegicus

General Stability

General Stability Organism
72 h, 10°C, pH 6.5, 0-3 M KBr, purified recombinant wild-type enzyme Rattus norvegicus

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.019
-
1-chloro-2,4-dinitrobenzene pH 6.5, 25°C, recombinant wild-type enzyme Rattus norvegicus
0.02
-
1-chloro-2,4-dinitrobenzene pH 6.5, 25°C, recombinant mutant R77Q Rattus norvegicus
0.045
-
1-chloro-2,4-dinitrobenzene pH 6.5, 25°C, recombinant mutant R77E Rattus norvegicus
0.052
-
1-chloro-2,4-dinitrobenzene pH 6.5, 25°C, recombinant mutant D97R Rattus norvegicus
0.069
-
glutathione pH 6.5, 25°C, recombinant wild-type enzyme Rattus norvegicus
0.077
-
1-chloro-2,4-dinitrobenzene pH 6.5, 25°C, recombinant mutant E100K Rattus norvegicus
0.088
-
1-chloro-2,4-dinitrobenzene pH 6.5, 25°C, recombinant mutant D97K Rattus norvegicus
0.089
-
glutathione pH 6.5, 25°C, recombinant mutant R77Q Rattus norvegicus
0.096
-
glutathione pH 6.5, 25°C, recombinant mutant R77E Rattus norvegicus
0.23
-
glutathione pH 6.5, 25°C, recombinant mutant D97K Rattus norvegicus
0.36
-
1-chloro-2,4-dinitrobenzene pH 6.5, 25°C, recombinant mutant N101D Rattus norvegicus
0.36
-
1-chloro-2,4-dinitrobenzene pH 6.5, 25°C, recombinant mutant N101K Rattus norvegicus
0.39
-
glutathione pH 6.5, 25°C, recombinant mutant N101D Rattus norvegicus
0.56
-
glutathione pH 6.5, 25°C, recombinant mutant D97R Rattus norvegicus
0.78
-
glutathione pH 6.5, 25°C, recombinant mutant E100R Rattus norvegicus
2.3
-
glutathione pH 6.5, 25°C, recombinant mutant E100K Rattus norvegicus
6.6
-
glutathione pH 6.5, 25°C, recombinant mutant N101K Rattus norvegicus

Metals/Ions

Metals/Ions Comment Organism Structure
KBr KBr greatly influences the monomer-dimer equilibrium of the wildtype isozyme GST-M1-1 Rattus norvegicus

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
additional information
-
monomer-dimer equilibrium and average molecular weights with and without bound glutathione at different concentrations of KBr, overview Rattus norvegicus
50000
-
about, recombinant wild-type enzyme, analytical ultracentrifugation Rattus norvegicus

Organism

Organism UniProt Comment Textmining
Rattus norvegicus
-
mu class isozyme M1-1, GST-M1-1
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
glutathione + 1-chloro-2,4-dinitrobenzene i.e. CDNB Rattus norvegicus chloride + 2,4-dinitrophenyl-glutathione
-
?
additional information the wild-type dimeric form is not required for catalytic activity Rattus norvegicus ?
-
?

Subunits

Subunits Comment Organism
dimer wild-type isozyme GST-M1-1, homodimer, crystal structure determination Rattus norvegicus
monomer mutant isozyme GST-M1, crystal structure determination Rattus norvegicus
More molecular structure modeling, the wild-type dimeric form is not required for catalytic activity, overview Rattus norvegicus

Synonyms

Synonyms Comment Organism
GST
-
Rattus norvegicus
mu glutathione transferase
-
Rattus norvegicus

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
25
-
assay at Rattus norvegicus

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
6.5
-
assay at Rattus norvegicus