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Literature summary extracted from

  • Shehu, D.; Alias, Z.
    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 .
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
2.5.1.18 expressed in Escherichia coli Rosettagami B (DE3) cells Acidovorax sp. KKS102

Protein Variants

EC Number Protein Variants Comment Organism
2.5.1.18 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]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
2.5.1.18 466.1
-
 glutathione mutant enzyme Y12C, pH and temperature not specified in the publication Acidovorax sp. KKS102
2.5.1.18 532.43
-
 glutathione wild type enzyme, pH and temperature not specified in the publication Acidovorax sp. KKS102
2.5.1.18 773.44
-
 4-nitrobenzyl chloride mutant enzyme Y12C, pH and temperature not specified in the publication Acidovorax sp. KKS102
2.5.1.18 1727
-
 4-nitrobenzyl chloride wild type enzyme, pH and temperature not specified in the publication Acidovorax sp. KKS102

Organism

EC Number Organism UniProt Comment Textmining
2.5.1.18 Acidovorax sp. KKS102 K0IAU2
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
2.5.1.18 glutathione Sepharose column chromatography Acidovorax sp. KKS102

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
2.5.1.18 0.0091
-
 with 1-chloro-2,4-dinitrobenzene as substrate, mutant enzyme Y12C, pH and temperature not specified in the publication Acidovorax sp. KKS102
2.5.1.18 0.0159
-
 with 1-chloro-2,4-dinitrobenzene as substrate, wild type enzyme, pH and temperature not specified in the publication Acidovorax sp. KKS102
2.5.1.18 0.0301
-
 with hydrogen peroxide as substrate, mutant enzyme Y12C, pH and temperature not specified in the publication Acidovorax sp. KKS102
2.5.1.18 0.043
-
 with hydrogen peroxide as substrate, wild type enzyme, pH and temperature not specified in the publication Acidovorax sp. KKS102
2.5.1.18 0.0907
-
 with cumene hydroperoxide as substrate, mutant enzyme Y12C, pH and temperature not specified in the publication Acidovorax sp. KKS102
2.5.1.18 0.1396
-
 with cumene hydroperoxide as substrate, wild type enzyme, pH and temperature not specified in the publication Acidovorax sp. KKS102
2.5.1.18 0.1991
-
 with ethacrynic acid as substrate, mutant enzyme Y12C, pH and temperature not specified in the publication Acidovorax sp. KKS102
2.5.1.18 0.3001
-
 with ethacrynic acid as substrate, wild type enzyme, pH and temperature not specified in the publication Acidovorax sp. KKS102
2.5.1.18 0.7975
-
 with 4-nitrobenzyl chloride as substrate, mutant enzyme Y12C, pH and temperature not specified in the publication Acidovorax sp. KKS102
2.5.1.18 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)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.5.1.18 glutathione + 1-chloro-2,4-dinitrobenzene
-
 Acidovorax sp. KKS102 chloride + 2,4-dinitrophenyl-glutathione
-
 ?
2.5.1.18 glutathione + 4-nitrobenzyl chloride best substrate Acidovorax sp. KKS102 ?
-
 ?
2.5.1.18 glutathione + cumene hydroperoxide
-
 Acidovorax sp. KKS102 ?
-
 ?
2.5.1.18 glutathione + ethacrynic acid
-
 Acidovorax sp. KKS102 ?
-
 ?
2.5.1.18 glutathione + hydrogen peroxide
-
 Acidovorax sp. KKS102 ?
-
 ?
2.5.1.18 additional information the enzyme also displays dehalogenation function against dichloroacetate, permethrin, and dieldrin Acidovorax sp. KKS102 ?
-
-

Subunits

EC Number Subunits Comment Organism
2.5.1.18 ? x * 25000, SDS-PAGE Acidovorax sp. KKS102

Synonyms

EC Number Synonyms Comment Organism
2.5.1.18 glutathione S-transferase
-
 Acidovorax sp. KKS102
2.5.1.18 GST
-
 Acidovorax sp. KKS102
2.5.1.18 KKSG9
-
 Acidovorax sp. KKS102

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
2.5.1.18 0.022
-
 glutathione mutant enzyme Y12C, pH and temperature not specified in the publication Acidovorax sp. KKS102
2.5.1.18 0.083
-
 4-nitrobenzyl chloride mutant enzyme Y12C, pH and temperature not specified in the publication Acidovorax sp. KKS102
2.5.1.18 0.086
-
 glutathione wild type enzyme, pH and temperature not specified in the publication Acidovorax sp. KKS102
2.5.1.18 0.27
-
 4-nitrobenzyl chloride wild type enzyme, pH and temperature not specified in the publication Acidovorax sp. KKS102

kcat/KM [mM/s]

EC Number kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
2.5.1.18 0.048
-
 glutathione mutant enzyme Y12C, pH and temperature not specified in the publication Acidovorax sp. KKS102
2.5.1.18 0.107
-
 4-nitrobenzyl chloride mutant enzyme Y12C, pH and temperature not specified in the publication Acidovorax sp. KKS102
2.5.1.18 0.158
-
 4-nitrobenzyl chloride wild type enzyme, pH and temperature not specified in the publication Acidovorax sp. KKS102
2.5.1.18 0.161
-
 glutathione wild type enzyme, pH and temperature not specified in the publication Acidovorax sp. KKS102