| IED ID | IndEnz0010001098 |
| Enzyme Type ID | esterase001098 |
| Protein Name |
Palmitoyl-protein thioesterase ABHD10, mitochondrial EC 3.1.2.22 Acyl-protein thioesterase ABHD10 Alpha/beta hydrolase domain-containing protein 10 Abhydrolase domain-containing protein 10 Mycophenolic acid acyl-glucuronide esterase, mitochondrial EC 3.1.1.93 |
| Gene Name | Abhd10 |
| Organism | Mus musculus (Mouse) |
| 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 Glires (Rodents and rabbits) Rodentia Myomorpha (mice and others) Muroidea Muridae Murinae Mus Mus Mus musculus (Mouse) |
| Enzyme Sequence | MAAWAPCRRWGWAAVSFGRHPGLSASLARKPPRAWWLSACRQKASLSFLNRSELPNLAYKRLKGKTPGIIFIPGYLSNMNGIKAVAVEEFCKSLGHAFIRFDYSGIGSSDGNLAECTVGKWRKDVLSILDDVAEGPQILVGSSLGGWLMLHAAIARPEKVIALIGIATAADGLVTQYHALPVETQKEIEMKGEWTLPSRYNKEGYFRIPYSFIKEAEHHCLLHSPIPVTCPVRLLHGMKDEIVPWQRSLQVADRIVSPDVDVILRKQGDHRMKEKADIHLLICTIDDLIDKLSTVVP |
| Enzyme Length | 297 |
| Uniprot Accession Number | Q6PE15 |
| Absorption | |
| Active Site | ACT_SITE 143; /note=Charge relay system; /evidence=ECO:0000250|UniProtKB:Q9NUJ1; ACT_SITE 240; /note=Charge relay system; /evidence=ECO:0000250|UniProtKB:Q8N2K0; ACT_SITE 270; /note=Charge relay system; /evidence=ECO:0000250|UniProtKB:Q8N2K0 |
| Activity Regulation | ACTIVITY REGULATION: Inhibited by palmostatin-B. {ECO:0000250|UniProtKB:Q9NUJ1}. |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=H2O + S-hexadecanoyl-L-cysteinyl-[protein] = H(+) + hexadecanoate + L-cysteinyl-[protein]; Xref=Rhea:RHEA:19233, Rhea:RHEA-COMP:10131, Rhea:RHEA-COMP:11032, ChEBI:CHEBI:7896, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:29950, ChEBI:CHEBI:74151; EC=3.1.2.22; Evidence={ECO:0000269|PubMed:31740833};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19234; Evidence={ECO:0000305|PubMed:31740833}; CATALYTIC ACTIVITY: Reaction=H2O + mycophenolic acid O-acyl-beta-D-glucuronide = D-glucuronate + H(+) + mycophenolate; Xref=Rhea:RHEA:34179, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:58720, ChEBI:CHEBI:62932, ChEBI:CHEBI:66982; EC=3.1.1.93; Evidence={ECO:0000250|UniProtKB:Q9NUJ1};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:34180; Evidence={ECO:0000250|UniProtKB:Q9NUJ1}; |
| DNA Binding | |
| EC Number | 3.1.2.22; 3.1.1.93 |
| Enzyme Function | FUNCTION: Acts as an acyl-protein thioesterase that hydrolyzes fatty acids from acylated residues in proteins (PubMed:31740833). Regulates the mitochondrial S-depalmitoylation of the nucleophilic active site residue of peroxiredoxin-5/PRDX5, a key antioxidant protein, therefore modulating mitochondrial antioxidant ability (PubMed:31740833). Also catalyzes the deglucuronidation of mycophenolic acid acyl-glucuronide, an active metabolite of the immunosuppressant drug mycophenolate (By similarity). {ECO:0000250|UniProtKB:Q9NUJ1, ECO:0000269|PubMed:31740833}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (3); Alternative sequence (2); Beta strand (12); Chain (1); Domain (1); Helix (11); Sequence conflict (1); Transit peptide (1); Turn (3) |
| Keywords | 3D-structure;Alternative splicing;Hydrolase;Mitochondrion;Reference proteome;Transit peptide |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250|UniProtKB:Q9NUJ1}. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | X-ray crystallography (1) |
| Cross Reference PDB | 6NY9; |
| Mapped Pubmed ID | 12466851; 14610273; 16615898; 18614015; 21078990; 22294686; |
| Motif | |
| Gene Encoded By | |
| Mass | 33,040 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | RHEA:19233; RHEA:19234; RHEA:34179; RHEA:34180 |
| Cross Reference Brenda |