| IED ID | IndEnz0018001633 |
| Enzyme Type ID | peroxidase001633 |
| Protein Name |
Disulfide-bond oxidoreductase YghU EC 1.8.4.- GSH-dependent disulfide-bond oxidoreductase YghU GST N2-2 Organic hydroperoxidase EC 1.11.1.- |
| Gene Name | yghU b2989 JW5492 |
| Organism | Escherichia coli (strain K12) |
| Taxonomic Lineage | cellular organisms Bacteria Proteobacteria Gammaproteobacteria Enterobacterales Enterobacteriaceae Escherichia Escherichia coli Escherichia coli (strain K12) |
| Enzyme Sequence | MTDNTYQPAKVWTWDKSAGGAFANINRPVSGPTHEKTLPVGKHPLQLYSLGTPNGQKVTIMLEELLALGVTGAEYDAWLIRIGDGDQFSSGFVEVNPNSKIPALRDHTHNPPIRVFESGSILLYLAEKFGYFLPQDLAKRTETMNWLFWLQGAAPFLGGGFGHFYHYAPVKIEYAINRFTMEAKRLLDVLDKQLAQHKFVAGDEYTIADMAIWPWFGNVVLGGVYDAAEFLDAGSYKHVQRWAKEVGERPAVKRGRIVNRTNGPLNEQLHERHDASDFETNTEDKRQG |
| Enzyme Length | 288 |
| Uniprot Accession Number | Q46845 |
| Absorption | |
| Active Site | |
| Activity Regulation | |
| Binding Site | BINDING 26; /note=Glutathione 2; /evidence=ECO:0000269|PubMed:21222452; BINDING 87; /note=Glutathione 1; /evidence=ECO:0000269|PubMed:21222452; BINDING 101; /note=Glutathione 1; via amide nitrogen and carbonyl oxygen; /evidence=ECO:0000269|PubMed:21222452; BINDING 151; /note=Glutathione 1; /evidence=ECO:0000269|PubMed:21222452; BINDING 178; /note=Glutathione 2; /evidence=ECO:0000269|PubMed:21222452 |
| Calcium Binding | |
| catalytic Activity | |
| DNA Binding | |
| EC Number | 1.8.4.-; 1.11.1.- |
| Enzyme Function | FUNCTION: Exhibits a robust glutathione (GSH)-dependent disulfide-bond reductase activity toward the model substrate, 2-hydroxyethyl disulfide; the actual physiological substrates are not known. Also displays a modest GSH-dependent peroxidase activity toward several organic hydroperoxides, such as cumene hydroperoxide and linoleic acid 13(S)-hydroperoxide, but does not reduce H(2)O(2) or tert-butyl hydroperoxide at appreciable rates. Exhibits little or no GSH transferase activity with most typical electrophilic substrates, and has no detectable transferase activity toward 1-chloro-2,4-dinitrobenzene (CDNB) with glutathionylspermidine (GspSH) as the nucleophilic substrate. {ECO:0000269|PubMed:21222452}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Beta strand (7); Binding site (5); Chain (1); Compositional bias (1); Domain (2); Erroneous initiation (1); Helix (17); Region (3); Turn (3) |
| Keywords | 3D-structure;Oxidoreductase;Peroxidase;Reference proteome |
| Interact With | |
| Induction | |
| Subcellular Location | |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | X-ray crystallography (1) |
| Cross Reference PDB | 3C8E; |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 32,392 |
| Kinetics | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=80 uM for glutathione (when assaying the GSH transferase activity with CDNB) {ECO:0000269|PubMed:21222452}; KM=1.1 mM for glutathione (when assaying the disulfide-bond reductase activity with 2-hydroxyethyl disulfide) {ECO:0000269|PubMed:21222452}; KM=16 uM for cumene hydroperoxide {ECO:0000269|PubMed:21222452}; KM=130 uM for linoleic acid 13(S)-hydroperoxide {ECO:0000269|PubMed:21222452}; KM=28 uM for 15(S)-HpETE {ECO:0000269|PubMed:21222452}; Note=kcat is 74 sec(-1) for the disulfide-bond reductase reaction toward 2-hydroxyethyl disulfide. kcat is 0.050, 0.19 and 0.096 sec(-1) for the hydroperoxidase reaction with cumene hydroperoxide, linoleic acid 13(S)-hydroperoxide, and 15(S)-HpETE as substrate, respectively. kcat is 0.109 sec(-1) for the GSH transferase reaction with CDNB as substrate.; |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |