Detail Information for IndEnz0010000093
IED ID IndEnz0010000093
Enzyme Type ID esterase000093
Protein Name S-formylglutathione hydrolase
FGH
EC 3.1.2.12
Esterase D
Methylumbelliferyl-acetate deacetylase
EC 3.1.1.56
Gene Name ESD
Organism Homo sapiens (Human)
Taxonomic Lineage cellular organisms Eukaryota Opisthokonta Metazoa Eumetazoa Bilateria Deuterostomia Chordata Craniata Vertebrata Gnathostomata (jawed vertebrates) Teleostomi Euteleostomi Sarcopterygii Dipnotetrapodomorpha Tetrapoda Amniota Mammalia Theria Eutheria Boreoeutheria Euarchontoglires Primates Haplorrhini Simiiformes Catarrhini Hominoidea (apes) Hominidae (great apes) Homininae Homo Homo sapiens (Human)
Enzyme Sequence MALKQISSNKCFGGLQKVFEHDSVELNCKMKFAVYLPPKAETGKCPALYWLSGLTCTEQNFISKSGYHQSASEHGLVVIAPDTSPRGCNIKGEDESWDFGTGAGFYVDATEDPWKTNYRMYSYVTEELPQLINANFPVDPQRMSIFGHSMGGHGALICALKNPGKYKSVSAFAPICNPVLCPWGKKAFSGYLGTDQSKWKAYDATHLVKSYPGSQLDILIDQGKDDQFLLDGQLLPDNFIAACTEKKIPVVFRLQEGYDHSYYFIATFITDHIRHHAKYLNA
Enzyme Length 282
Uniprot Accession Number P10768
Absorption
Active Site ACT_SITE 149; /note=Charge relay system; /evidence=ECO:0000269|PubMed:19126594; ACT_SITE 226; /note=Charge relay system; /evidence=ECO:0000269|PubMed:19126594; ACT_SITE 260; /note=Charge relay system; /evidence=ECO:0000269|PubMed:19126594
Activity Regulation
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:4768551}; CATALYTIC ACTIVITY: Reaction=4-methylumbelliferyl acetate + H2O = 4-methylumbelliferone + acetate + H(+); Xref=Rhea:RHEA:12208, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17224, ChEBI:CHEBI:17763, ChEBI:CHEBI:30089; EC=3.1.1.56; Evidence={ECO:0000269|PubMed:4768551};
DNA Binding
EC Number 3.1.2.12; 3.1.1.56
Enzyme Function FUNCTION: Serine hydrolase involved in the detoxification of formaldehyde. {ECO:0000269|PubMed:3770744, ECO:0000269|PubMed:4768551}.
Temperature Dependency
PH Dependency
Pathway
nucleotide Binding
Features Active site (3); Beta strand (10); Chain (1); Helix (14); Initiator methionine (1); Modified residue (3); Mutagenesis (8); Natural variant (2); Turn (2)
Keywords 3D-structure;Acetylation;Cytoplasm;Cytoplasmic vesicle;Direct protein sequencing;Hydrolase;Reference proteome;Serine esterase
Interact With Itself; A1L4K1
Induction
Subcellular Location SUBCELLULAR LOCATION: Cytoplasm. Cytoplasmic vesicle.
Modified Residue MOD_RES 2; /note=N-acetylalanine; /evidence=ECO:0000250|UniProtKB:Q9R0P3; MOD_RES 4; /note=N6-succinyllysine; /evidence=ECO:0000250|UniProtKB:Q9R0P3; MOD_RES 200; /note=N6-acetyllysine; /evidence=ECO:0007744|PubMed:19608861
Post Translational Modification
Signal Peptide
Structure 3D X-ray crystallography (1)
Cross Reference PDB 3FCX;
Mapped Pubmed ID 11436564; 11785295; 11963573; 12942785; 17353931; 18552983; 18624398; 19343046; 20562859; 21596165; 22623428; 23752268; 25416956; 25814554; 26337638; 26752685;
Motif
Gene Encoded By
Mass 31,463
Kinetics
Metal Binding
Rhea ID RHEA:14961; RHEA:12208
Cross Reference Brenda