| IED ID | IndEnz0018001638 |
| Enzyme Type ID | peroxidase001638 |
| Protein Name |
Disulfide-bond oxidoreductase YfcG EC 1.8.4.- GSH-dependent disulfide-bond oxidoreductase YfcG GST N1-1 GST-like protein YfcG Organic hydroperoxidase EC 1.11.1.- |
| Gene Name | yfcG b2302 JW2299 |
| Organism | Escherichia coli (strain K12) |
| Taxonomic Lineage | cellular organisms Bacteria Proteobacteria Gammaproteobacteria Enterobacterales Enterobacteriaceae Escherichia Escherichia coli Escherichia coli (strain K12) |
| Enzyme Sequence | MIDLYFAPTPNGHKITLFLEEAELDYRLIKVDLGKGGQFRPEFLRISPNNKIPAIVDHSPADGGEPLSLFESGAILLYLAEKTGLFLSHETRERAATLQWLFWQVGGLGPMLGQNHHFNHAAPQTIPYAIERYQVETQRLYHVLNKRLENSPWLGGENYSIADIACWPWVNAWTRQRIDLAMYPAVKNWHERIRSRPATGQALLKAQLGDERSDS |
| Enzyme Length | 215 |
| Uniprot Accession Number | P77526 |
| Absorption | |
| Active Site | |
| Activity Regulation | |
| Binding Site | BINDING 11; /note=Glutathione 1; /evidence=ECO:0000269|PubMed:19537707; BINDING 38; /note=Glutathione 1; /evidence=ECO:0000269|PubMed:19537707; BINDING 40; /note=Glutathione; /evidence=ECO:0000250|UniProtKB:P08263; BINDING 52; /note=Glutathione 1; via amide nitrogen and carbonyl oxygen; /evidence=ECO:0000269|PubMed:19537707; BINDING 132; /note=Glutathione 2; /evidence=ECO:0000269|PubMed:19537707 |
| Calcium Binding | |
| catalytic Activity | |
| DNA Binding | |
| EC Number | 1.8.4.-; 1.11.1.- |
| Enzyme Function | FUNCTION: Exhibits a very robust glutathione (GSH)-dependent disulfide-bond reductase activity toward the model substrate, 2-hydroxyethyl disulfide; the actual physiological substrates are not known. Has also a low GSH-dependent hydroperoxidase activity toward cumene hydroperoxide, but does not reduce H(2)O(2), tert-butyl hydroperoxide, benzyl peroxide, or lauroyl peroxide. Exhibits little or no GSH transferase activity with most typical electrophilic substrates, and has no detectable transferase activity using glutathionylspermidine (GspSH) as the nucleophilic substrate. Is involved in defense against oxidative stress, probably via its peroxidase activity. {ECO:0000269|PubMed:17018556, ECO:0000269|PubMed:19537707}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Beta strand (5); Binding site (5); Chain (1); Domain (2); Helix (13); Mutagenesis (4); Region (1) |
| Keywords | 3D-structure;Oxidoreductase;Peroxidase;Reference proteome |
| Interact With | |
| Induction | |
| Subcellular Location | |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | X-ray crystallography (2) |
| Cross Reference PDB | 3GX0; 5HFK; |
| Mapped Pubmed ID | 16606699; |
| Motif | |
| Gene Encoded By | |
| Mass | 24,516 |
| Kinetics | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=1.6 mM for glutathione (when assaying the disulfide-bond reductase activity with 2-hydroxyethyl disulfide) {ECO:0000269|PubMed:19537707}; Note=kcat is 180 sec(-1) for the disulfide-bond reductase reaction toward 2-hydroxyethyl disulfide. kcat is 0.27 sec(-1) for the hydroperoxidase reaction with cumene hydroperoxide. kcat is 0.1 sec(-1) for the GSH transferase reaction with chloro-2,4-dinitrobenzene (CDNB) as substrate.; |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |