EC Number | Activating Compound | Comment | Organism | Structure |
---|---|---|---|---|
3.1.2.6 | additional information | no dependance on ionic strength | Trypanosoma brucei |
EC Number | Cloned (Comment) | Organism |
---|---|---|
3.1.2.6 | - |
Trypanosoma brucei |
3.1.2.6 | DNA and amino acid sequence determination and analysis, overexpression as N-terminally His-tagged and as free enzyme in Escherichia coli | Trypanosoma brucei |
EC Number | Inhibitors | Comment | Organism | Structure |
---|---|---|---|---|
3.1.2.6 | additional information | the enzyme is not sensitive against ionic strength | Trypanosoma brucei |
EC Number | KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|---|
3.1.2.6 | 0.086 | - |
bis-(lactoyl)trypanothione | pH 7.2, 25°C | Trypanosoma brucei | |
3.1.2.6 | 0.086 | - |
bis-(lactoyl)trypanothione | recombinant enzyme, pH 7.2, 25°C | Trypanosoma brucei | |
3.1.2.6 | 0.108 | - |
mono-(lactoyl)trypanothione | pH 7.2, 25°C | Trypanosoma brucei | |
3.1.2.6 | 0.108 | - |
mono-(lactoyl)trypanothione | recombinant enzyme, pH 7.2, 25°C | Trypanosoma brucei | |
3.1.2.6 | 3 | - |
S-D-lactoylglutathione | above, recombinant enzyme, pH 7.2, 25°C | Trypanosoma brucei | |
3.1.2.6 | 3 | - |
lactoylglutathione | or above, pH 7.2, 25°C | Trypanosoma brucei |
EC Number | Metals/Ions | Comment | Organism | Structure |
---|---|---|---|---|
3.1.2.6 | Cobalt | 0.6 mol per mol of protein | Trypanosoma brucei | |
3.1.2.6 | Iron | 0.42 mol per mol of protein | Trypanosoma brucei | |
3.1.2.6 | additional information | the enzyme contains the highly conserved metal binding motif THXHXDH, total metal ions per mol of enzyme: 1.5 for the His-tagged enzyme, 0.7-0.9 for the free enzyme | Trypanosoma brucei | |
3.1.2.6 | additional information | sequence contains the highly conserved metal binding motif THXHXDH | Trypanosoma brucei | |
3.1.2.6 | Zinc | 0.45 mol per mol of protein | Trypanosoma brucei |
EC Number | Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
---|---|---|---|---|
3.1.2.6 | 25000 | - |
gel filtration | Trypanosoma brucei |
3.1.2.6 | 25000 | - |
recombinant enzyme, gel filtration | Trypanosoma brucei |
3.1.2.6 | 32000 | - |
1 * 32000, recombinant enzyme, SDS-PAGE | Trypanosoma brucei |
3.1.2.6 | 32000 | - |
1 * 32507, calculated, 1 * 32000, SDS-PAGE | Trypanosoma brucei |
3.1.2.6 | 32507 | - |
1 * 32507, calculated, 1 * 32000, SDS-PAGE | Trypanosoma brucei |
EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
3.1.2.6 | S-D-lactoylglutathione + H2O | Trypanosoma brucei | enzyme is involved in the detoxification of ketoaldehydes such as methylglyoxal, which is mainly a byproduct of glycolysis | glutathione + D-lactate | - |
? |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
3.1.2.6 | Trypanosoma brucei | Q6KF36 | - |
- |
EC Number | Purification (Comment) | Organism |
---|---|---|
3.1.2.6 | recombinant enzyme with and without His-tag | Trypanosoma brucei |
3.1.2.6 | recombinant His-tagged and non-tagged enzyme expressed in Escherichia coli | Trypanosoma brucei |
EC Number | Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
---|---|---|---|---|
3.1.2.6 | additional information | - |
- |
Trypanosoma brucei |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
3.1.2.6 | bis-(lactoyl)trypanothione + H2O | preferred substrate | Trypanosoma brucei | trypanothione + D-lactate | trypathione is bis(glutathionyl)spermidine | ? | |
3.1.2.6 | bis-(lactoyl)trypanothione + H2O | - |
Trypanosoma brucei | D-lactate + trypanothione | - |
? | |
3.1.2.6 | lactoylglutathione + H2O | enzyme does not show saturation kinetics up to 5 mM | Trypanosoma brucei | D-lactate + glutathione | - |
? | |
3.1.2.6 | mono-(lactoyl)trypanothione + H2O | preferred substrate | Trypanosoma brucei | trypanothione + D-lactate | trypathione is bis(glutathionyl)spermidine | ? | |
3.1.2.6 | mono-(lactoyl)trypanothione + H2O | - |
Trypanosoma brucei | D-lactate + trypanothione | - |
? | |
3.1.2.6 | S-D-lactoylglutathione + H2O | - |
Trypanosoma brucei | glutathione + D-lactate | - |
? | |
3.1.2.6 | S-D-lactoylglutathione + H2O | enzyme is involved in the detoxification of ketoaldehydes such as methylglyoxal, which is mainly a byproduct of glycolysis | Trypanosoma brucei | glutathione + D-lactate | - |
? |
EC Number | Subunits | Comment | Organism |
---|---|---|---|
3.1.2.6 | monomer | 1 * 32000, recombinant enzyme, SDS-PAGE | Trypanosoma brucei |
3.1.2.6 | monomer | 1 * 32507, calculated, 1 * 32000, SDS-PAGE | Trypanosoma brucei |
EC Number | Synonyms | Comment | Organism |
---|---|---|---|
3.1.2.6 | acetoacetylglutathione hydrolase | - |
Trypanosoma brucei |
3.1.2.6 | Germ cell specific protein | - |
Trypanosoma brucei |
3.1.2.6 | GLO II | - |
Trypanosoma brucei |
3.1.2.6 | glyoxalase II | - |
Trypanosoma brucei |
3.1.2.6 | hydrolase, acetoacetylglutathione | - |
Trypanosoma brucei |
3.1.2.6 | hydrolase, hydroxyacylglutathione | - |
Trypanosoma brucei |
3.1.2.6 | Round spermatid protein RSP29 | - |
Trypanosoma brucei |
3.1.2.6 | S-2-hydroxylacylglutathione hydrolase | - |
Trypanosoma brucei |
EC Number | Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|---|
3.1.2.6 | 25 | - |
assay at | Trypanosoma brucei |
EC Number | pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|---|
3.1.2.6 | 7 | 8 | broad | Trypanosoma brucei |
3.1.2.6 | 7 | 8 | broad optimum | Trypanosoma brucei |
EC Number | Organism | Comment | pI Value Maximum | pI Value |
---|---|---|---|---|
3.1.2.6 | Trypanosoma brucei | calculated from protein sequence | - |
6 |
3.1.2.6 | Trypanosoma brucei | calculated | 6.5 | 6 |