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Literature summary for 2.5.1.18 extracted from
- Functional role of Tyr12 in the catalytic activity of novel zeta-like glutathione S-transferase from Acidovorax sp. KKS102 (2018), Protein J., 37, 261-269 .
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| expressed in Escherichia coli Rosettagami B (DE3) cells | Acidovorax sp. KKS102 |
Protein Variants
| Protein Variants | Comment | Organism |
|---|---|---|
| Y12C | the mutant displays low catalytic activity and dehalogenation function against all the substrates when compared with the wild type enzyme. The mutant displays a higher affinity for 4-nitrobenzyl chloride when compared with the wild type, however, no significant change in glutathione affinity is observed | Acidovorax sp. KKS102 |
KM Value [mM]
| KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| 466.1 | - |
glutathione | mutant enzyme Y12C, pH and temperature not specified in the publication | Acidovorax sp. KKS102 |  |
| 532.43 | - |
glutathione | wild type enzyme, pH and temperature not specified in the publication | Acidovorax sp. KKS102 | |
| 773.44 | - |
4-nitrobenzyl chloride | mutant enzyme Y12C, pH and temperature not specified in the publication | Acidovorax sp. KKS102 | |
| 1727 | - |
4-nitrobenzyl chloride | wild type enzyme, pH and temperature not specified in the publication | Acidovorax sp. KKS102 | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Acidovorax sp. KKS102 | K0IAU2 | - |
- |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
| glutathione Sepharose column chromatography | Acidovorax sp. KKS102 |
Specific Activity [micromol/min/mg]
| Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
|---|---|---|---|
| 0.0091 | - |
with 1-chloro-2,4-dinitrobenzene as substrate, mutant enzyme Y12C, pH and temperature not specified in the publication | Acidovorax sp. KKS102 |
| 0.0159 | - |
with 1-chloro-2,4-dinitrobenzene as substrate, wild type enzyme, pH and temperature not specified in the publication | Acidovorax sp. KKS102 |
| 0.0301 | - |
with hydrogen peroxide as substrate, mutant enzyme Y12C, pH and temperature not specified in the publication | Acidovorax sp. KKS102 |
| 0.043 | - |
with hydrogen peroxide as substrate, wild type enzyme, pH and temperature not specified in the publication | Acidovorax sp. KKS102 |
| 0.0907 | - |
with cumene hydroperoxide as substrate, mutant enzyme Y12C, pH and temperature not specified in the publication | Acidovorax sp. KKS102 |
| 0.1396 | - |
with cumene hydroperoxide as substrate, wild type enzyme, pH and temperature not specified in the publication | Acidovorax sp. KKS102 |
| 0.1991 | - |
with ethacrynic acid as substrate, mutant enzyme Y12C, pH and temperature not specified in the publication | Acidovorax sp. KKS102 |
| 0.3001 | - |
with ethacrynic acid as substrate, wild type enzyme, pH and temperature not specified in the publication | Acidovorax sp. KKS102 |
| 0.7975 | - |
with 4-nitrobenzyl chloride as substrate, mutant enzyme Y12C, pH and temperature not specified in the publication | Acidovorax sp. KKS102 |
| 1.0628 | - |
with 4-nitrobenzyl chloride as substrate, wild type enzyme, pH and temperature not specified in the publication | Acidovorax sp. KKS102 |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| glutathione + 1-chloro-2,4-dinitrobenzene | - |
Acidovorax sp. KKS102 | chloride + 2,4-dinitrophenyl-glutathione | - |
? | |
| glutathione + 4-nitrobenzyl chloride | best substrate | Acidovorax sp. KKS102 | ? | - |
? | |
| glutathione + cumene hydroperoxide | - |
Acidovorax sp. KKS102 | ? | - |
? | |
| glutathione + ethacrynic acid | - |
Acidovorax sp. KKS102 | ? | - |
? | |
| glutathione + hydrogen peroxide | - |
Acidovorax sp. KKS102 | ? | - |
? | |
| additional information | the enzyme also displays dehalogenation function against dichloroacetate, permethrin, and dieldrin | Acidovorax sp. KKS102 | ? | - |
- |
|
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| ? | x * 25000, SDS-PAGE | Acidovorax sp. KKS102 |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| glutathione S-transferase | - |
Acidovorax sp. KKS102 |
| GST | - |
Acidovorax sp. KKS102 |
| KKSG9 | - |
Acidovorax sp. KKS102 |
Turnover Number [1/s]
| Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| 0.022 | - |
glutathione | mutant enzyme Y12C, pH and temperature not specified in the publication | Acidovorax sp. KKS102 | |
| 0.083 | - |
4-nitrobenzyl chloride | mutant enzyme Y12C, pH and temperature not specified in the publication | Acidovorax sp. KKS102 | |
| 0.086 | - |
glutathione | wild type enzyme, pH and temperature not specified in the publication | Acidovorax sp. KKS102 | |
| 0.27 | - |
4-nitrobenzyl chloride | wild type enzyme, pH and temperature not specified in the publication | Acidovorax sp. KKS102 | |
kcat/KM [mM/s]
| kcat/KM Value [1/mMs-1] | kcat/KM Value Maximum [1/mMs-1] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| 0.048 | - |
glutathione | mutant enzyme Y12C, pH and temperature not specified in the publication | Acidovorax sp. KKS102 | |
| 0.107 | - |
4-nitrobenzyl chloride | mutant enzyme Y12C, pH and temperature not specified in the publication | Acidovorax sp. KKS102 | |
| 0.158 | - |
4-nitrobenzyl chloride | wild type enzyme, pH and temperature not specified in the publication | Acidovorax sp. KKS102 | |
| 0.161 | - |
glutathione | wild type enzyme, pH and temperature not specified in the publication | Acidovorax sp. KKS102 | |
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