| IED ID | IndEnz0010001554 |
| Enzyme Type ID | esterase001554 |
| Protein Name |
S-formylglutathione hydrolase AtSFGH EC 3.1.2.12 Esterase D |
| Gene Name | SFGH At2g41530 T32G6.5 |
| Organism | Arabidopsis thaliana (Mouse-ear cress) |
| Taxonomic Lineage | cellular organisms Eukaryota Viridiplantae Streptophyta Streptophytina Embryophyta Tracheophyta Euphyllophyta Spermatophyta Magnoliopsida Mesangiospermae eudicotyledons Gunneridae Pentapetalae rosids malvids Brassicales Brassicaceae Camelineae Arabidopsis Arabidopsis thaliana (Mouse-ear cress) |
| Enzyme Sequence | MASGLSEIGSTKMFDGYNKRYKHFSETLGCSMTFSIYFPPSASSSHKSPVLYWLSGLTCTDENFIIKSGAQRAASTHGIALVAPDTSPRGLNVEGEADSYDFGVGAGFYLNATQEKWKNWRMYDYVVKELPKLLSENFSQLDTTKASISGHSMGGHGALTIYLRNLDKYKSVSAFAPITNPINCAWGQKAFTNYLGDNKAAWEEYDATCLISKYNNLSATILIDQGENDQFYPDQLLPSKFEEACKKVNAPLLLRLHPGYDHSYYFIATFIEDHISHHAQALEL |
| Enzyme Length | 284 |
| Uniprot Accession Number | Q8LAS8 |
| Absorption | |
| Active Site | ACT_SITE 152; /note=Charge relay system; /evidence=ECO:0000250; ACT_SITE 229; /note=Charge relay system; /evidence=ECO:0000250; ACT_SITE 262; /note=Charge relay system; /evidence=ECO:0000250 |
| Activity Regulation | ACTIVITY REGULATION: Activity toward p-nitrophenyl acetate inhibited by N-ethylmaleimide, 10-(fluoroethoxyphosphinyl)-N-(biotinamidopentyl)decanamide (FP-biotin), iodoacetamide, CuCl(2) and ZnSO(4), but not by phenylmethylsulfonyl fluoride, EDTA, Mg(2+), Mn(2+), Ca(2+) or paraoxon, an organo-phosphate inhibitor of serine hydrolases. {ECO:0000269|PubMed:16626737}. |
| Binding Site | BINDING 63; /note=Substrate; BINDING 67; /note=Substrate |
| 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:0000305|PubMed:11888210};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:14962; Evidence={ECO:0000305|PubMed:11888210}; |
| DNA Binding | |
| EC Number | 3.1.2.12 |
| Enzyme Function | FUNCTION: Serine hydrolase which catalyzes the hydrolysis of S-formylglutathione to glutathione and formic acid (Probable). Also hydrolyzes S-acetylglutathione and a range of carboxyesters in vitro (PubMed:11888210). Involved in the detoxification of formaldehyde (PubMed:16626737). {ECO:0000269|PubMed:11888210, ECO:0000269|PubMed:16626737, ECO:0000305|PubMed:11888210}. |
| Temperature Dependency | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Fully active up to 55 degrees Celsius.; |
| PH Dependency | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 7.6-8 for carboxyesterase activity.; |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (3); Binding site (2); Chain (1); Erroneous initiation (1); Initiator methionine (1); Modified residue (1); Mutagenesis (2); Sequence conflict (1) |
| Keywords | Acetylation;Hydrolase;Reference proteome;Serine esterase |
| Interact With | |
| Induction | |
| Subcellular Location | |
| Modified Residue | MOD_RES 2; /note=N-acetylalanine; /evidence=ECO:0007744|PubMed:22223895 |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | 15769804; 16502469; 17270225; 17309689; 17828791; 18315867; 18538804; 20405473; 26408809; 28627464; |
| Motif | |
| Gene Encoded By | |
| Mass | 31,656 |
| Kinetics | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.13 mM for S-formylglutathione {ECO:0000269|PubMed:11888210}; KM=0.15 mM for S-acetylglutathione {ECO:0000269|PubMed:11888210}; KM=1.02 mM for p-nitrophenyl acetate {ECO:0000269|PubMed:11888210}; KM=0.57 mM for alpha-naphthyl acetate {ECO:0000269|PubMed:11888210}; KM=0.54 mM for beta-naphthyl acetate {ECO:0000269|PubMed:11888210}; KM=0.03 mM for fluorescein diacetate {ECO:0000269|PubMed:11888210}; KM=0.12 mM for 4-methylumbelliferyl acetate {ECO:0000269|PubMed:11888210}; Vmax=219 nmol/sec/mg enzyme with S-formylglutathione as substrate {ECO:0000269|PubMed:11888210}; Vmax=311 nmol/sec/mg enzyme with S-acetylglutathione as substrate {ECO:0000269|PubMed:11888210}; Vmax=185 nmol/sec/mg enzyme with p-nitrophenyl acetate as substrate {ECO:0000269|PubMed:11888210}; Vmax=350 nmol/sec/mg enzyme with alpha-naphthyl acetate as substrate {ECO:0000269|PubMed:11888210}; Vmax=22 nmol/sec/mg enzyme with beta-naphthyl acetate as substrate {ECO:0000269|PubMed:11888210}; Vmax=3 nmol/sec/mg enzyme with fluorescein diacetate as substrate {ECO:0000269|PubMed:11888210}; Vmax=714 nmol/sec/mg enzyme with 4-methylumbelliferyl acetate as substrate {ECO:0000269|PubMed:11888210}; |
| Metal Binding | |
| Rhea ID | RHEA:14961; RHEA:14962 |
| Cross Reference Brenda | 3.1.2.12; |