| IED ID | IndEnz0018000352 |
| Enzyme Type ID | peroxidase000352 |
| Protein Name |
Glutathione S-transferase GstA EC 2.5.1.18 GST B1-1 |
| Gene Name | gstA gst b1635 JW1627 |
| Organism | Escherichia coli (strain K12) |
| Taxonomic Lineage | cellular organisms Bacteria Proteobacteria Gammaproteobacteria Enterobacterales Enterobacteriaceae Escherichia Escherichia coli Escherichia coli (strain K12) |
| Enzyme Sequence | MKLFYKPGACSLASHITLRESGKDFTLVSVDLMKKRLENGDDYFAVNPKGQVPALLLDDGTLLTEGVAIMQYLADSVPDRQLLAPVNSISRYKTIEWLNYIATELHKGFTPLFRPDTPEEYKPTVRAQLEKKLQYVNEALKDEHWICGQRFTIADAYLFTVLRWAYAVKLNLEGLEHIAAFMQRMAERPEVQDALSAEGLK |
| Enzyme Length | 201 |
| Uniprot Accession Number | P0A9D2 |
| Absorption | |
| Active Site | |
| Activity Regulation | |
| Binding Site | BINDING 10; /note=Glutathione; /evidence=ECO:0000305|PubMed:9680481; BINDING 35; /note=Glutathione; /evidence=ECO:0000305|PubMed:9680481; BINDING 52; /note=Glutathione; via amide nitrogen and carbonyl oxygen; /evidence=ECO:0000305|PubMed:9680481; BINDING 99; /note=Glutathione; /evidence=ECO:0000305|PubMed:9680481 |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=glutathione + RX = a halide anion + an S-substituted glutathione + H(+); Xref=Rhea:RHEA:16437, ChEBI:CHEBI:15378, ChEBI:CHEBI:16042, ChEBI:CHEBI:17792, ChEBI:CHEBI:57925, ChEBI:CHEBI:90779; EC=2.5.1.18; Evidence={ECO:0000269|PubMed:18778244, ECO:0000269|PubMed:2185038, ECO:0000269|PubMed:7798255}; |
| DNA Binding | |
| EC Number | 2.5.1.18 |
| Enzyme Function | FUNCTION: Catalyzes the conjugation of reduced glutathione (GSH) to a wide number of exogenous and endogenous hydrophobic electrophiles. Shows activity toward 1-chloro-2,4-dinitrobenzene (CDNB) and ethacrynic acid. Also possesses thiol:disulfide oxidoreductase activity, using GSH to reduce bis-(2-hydroxyethyl) disulfide (HEDS). Has a low level of glutathione-dependent peroxidase activity toward cumene hydroperoxide. Is important for defense against oxidative stress, probably via its peroxidase activity. {ECO:0000269|PubMed:17018556, ECO:0000269|PubMed:18778244, ECO:0000269|PubMed:2185038, ECO:0000269|PubMed:7798255}. |
| Temperature Dependency | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 35 degrees Celsius. {ECO:0000269|PubMed:2185038, ECO:0000269|PubMed:7798255}; |
| PH Dependency | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 7.5. {ECO:0000269|PubMed:2185038, ECO:0000269|PubMed:7798255}; |
| Pathway | |
| nucleotide Binding | |
| Features | Beta strand (7); Binding site (4); Chain (1); Domain (2); Helix (11); Mutagenesis (5); Region (2); Sequence conflict (2); Turn (2) |
| Keywords | 3D-structure;Cytoplasm;Direct protein sequencing;Reference proteome;Transferase |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Cytoplasm. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | X-ray crystallography (2) |
| Cross Reference PDB | 1A0F; 1N2A; |
| Mapped Pubmed ID | 16606699; |
| Motif | |
| Gene Encoded By | |
| Mass | 22,868 |
| Kinetics | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.041 mM for glutathione {ECO:0000269|PubMed:18778244, ECO:0000269|PubMed:2185038, ECO:0000269|PubMed:7798255}; KM=0.3 mM for glutathione {ECO:0000269|PubMed:18778244, ECO:0000269|PubMed:2185038, ECO:0000269|PubMed:7798255}; KM=0.99 mM for 1-chloro-2,4-dinitrobenzene {ECO:0000269|PubMed:18778244, ECO:0000269|PubMed:2185038, ECO:0000269|PubMed:7798255}; KM=1.9 mM for 1-chloro-2,4-dinitrobenzene {ECO:0000269|PubMed:18778244, ECO:0000269|PubMed:2185038, ECO:0000269|PubMed:7798255}; Note=kcat is 9 sec(-1) for the GSH transferase reaction with CDNB as substrate. {ECO:0000269|PubMed:18778244}; |
| Metal Binding | |
| Rhea ID | RHEA:16437 |
| Cross Reference Brenda | 2.5.1.18; |