| IED ID | IndEnz0010001533 |
| Enzyme Type ID | esterase001533 |
| Protein Name |
S-formylglutathione hydrolase YeiG FGH EC 3.1.2.12 |
| Gene Name | yeiG b2154 JW2141 |
| Organism | Escherichia coli (strain K12) |
| Taxonomic Lineage | cellular organisms Bacteria Proteobacteria Gammaproteobacteria Enterobacterales Enterobacteriaceae Escherichia Escherichia coli Escherichia coli (strain K12) |
| Enzyme Sequence | MEMLEEHRCFEGWQQRWRHDSSTLNCPMTFSIFLPPPRDHTPPPVLYWLSGLTCNDENFTTKAGAQRVAAELGIVLVMPDTSPRGEKVANDDGYDLGQGAGFYLNATQPPWATHYRMYDYLRDELPALVQSQFNVSDRCAISGHSMGGHGALIMALKNPGKYTSVSAFAPIVNPCSVPWGIKAFSSYLGEDKNAWLEWDSCALMYASNAQDAIPTLIDQGDNDQFLADQLQPAVLAEAARQKAWPMTLRIQPGYDHSYYFIASFIEDHLRFHAQYLLK |
| Enzyme Length | 278 |
| Uniprot Accession Number | P33018 |
| Absorption | |
| Active Site | ACT_SITE 145; /note=Charge relay system; /evidence=ECO:0000305; ACT_SITE 223; /note=Charge relay system; /evidence=ECO:0000305; ACT_SITE 256; /note=Charge relay system; /evidence=ECO:0000305 |
| Activity Regulation | ACTIVITY REGULATION: Inhibited by the sulfhydryl inhibitors (N-ethylmaleimide, iodoacetate, ZnCl(2) and CuCl(2)). {ECO:0000269|PubMed:16567800}. |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=H2O + S-formylglutathione = formate + glutathione + H(+); Xref=Rhea:RHEA:14961, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15740, ChEBI:CHEBI:57688, ChEBI:CHEBI:57925; EC=3.1.2.12; Evidence={ECO:0000269|PubMed:16567800}; |
| DNA Binding | |
| EC Number | 3.1.2.12 |
| Enzyme Function | FUNCTION: Serine hydrolase involved in the detoxification of formaldehyde. Hydrolyzes S-formylglutathione to glutathione and formate. Shows also esterase activity against alpha-naphthyl acetate, lactoylglutathione, palmitoyl-CoA and several pNP-esters of short chain fatty acids. {ECO:0000269|PubMed:15808744, ECO:0000269|PubMed:16567800}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (3); Chain (1); Mutagenesis (9) |
| Keywords | Hydrolase;Reference proteome;Serine esterase |
| Interact With | |
| Induction | INDUCTION: Constitutively expressed. {ECO:0000269|PubMed:16567800}. |
| Subcellular Location | |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | 16606699; 24561554; |
| Motif | |
| Gene Encoded By | |
| Mass | 31,259 |
| Kinetics | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.43 mM for S-formylglutathione {ECO:0000269|PubMed:16567800}; KM=1.03 mM for alpha-naphthyl acetate {ECO:0000269|PubMed:16567800}; KM=0.45 mM for pNP-acetate {ECO:0000269|PubMed:16567800}; KM=0.70 mM for pNP-butyrate {ECO:0000269|PubMed:16567800}; KM=0.95 mM for pNP-caproate {ECO:0000269|PubMed:16567800}; KM=0.48 mM for pNP-propionate {ECO:0000269|PubMed:16567800}; KM=0.58 mM for S-lactoylglutathione {ECO:0000269|PubMed:16567800}; Vmax=12.6 umol/min/mg enzyme with S-formylglutathione as substrate {ECO:0000269|PubMed:16567800}; Vmax=9.79 umol/min/mg enzyme with alpha-naphthyl acetate as substrate {ECO:0000269|PubMed:16567800}; Vmax=0.50 umol/min/mg enzyme with pNP-acetate as substrate {ECO:0000269|PubMed:16567800}; Vmax=0.70 umol/min/mg enzyme with pNP-butyrate as substrate {ECO:0000269|PubMed:16567800}; Vmax=0.64 umol/min/mg enzyme with pNP-caproate as substrate {ECO:0000269|PubMed:16567800}; Vmax=0.71 umol/min/mg enzyme with pNP-propionate as substrate {ECO:0000269|PubMed:16567800}; Vmax=1.97 umol/min/mg enzyme with S-lactoylglutathione as substrate {ECO:0000269|PubMed:16567800}; |
| Metal Binding | |
| Rhea ID | RHEA:14961 |
| Cross Reference Brenda | 3.1.2.2; |