Detail Information for IndEnz0010001099
IED ID IndEnz0010001099
Enzyme Type ID esterase001099
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 Rattus norvegicus (Rat)
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 Rattus Rattus norvegicus (Rat)
Enzyme Sequence MAAWVPCRKWGWAAVSFGRHRGLIASLARKPPWAWWLSACRQKTTLSFLKRPELPSLAYKRLKGKNPGIIFIPGYLSNMNGKKAVAIEEFCKSIGHAFIRFDYSGVGSSDGNLAECSVGKWRKDVLSILDDIAEGPQILVGSSLGGWLMLHAAIARPEKVIALIGIASATDGVVTQFHSLPVEMQKEIEMKGEWSLPSKYNKEGYYSIPYSFIKEAAHHCLLHSPIPVTCPVRLLHGMKDEIVPWHRSLQVADRVVSPDVDVILRKHSDHRMKETADIHLLICTIDDLIDKLSTVTH
Enzyme Length 297
Uniprot Accession Number Q5I0K5
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:0000250|UniProtKB:Q9NUJ1};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19234; Evidence={ECO:0000250|UniProtKB:Q9NUJ1}; 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. Regulates the mitochondrial S-depalmitoylation of the nucleophilic active site residue of peroxiredoxin-5/PRDX5, a key antioxidant protein, therefore modulating mitochondrial antioxidant ability. Also catalyzes the deglucuronidation of mycophenolic acid acyl-glucuronide, an active metabolite of the immunosuppressant drug mycophenolate. {ECO:0000250|UniProtKB:Q9NUJ1}.
Temperature Dependency
PH Dependency
Pathway
nucleotide Binding
Features Active site (3); Chain (1); Domain (1); Transit peptide (1)
Keywords 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
Cross Reference PDB -
Mapped Pubmed ID -
Motif
Gene Encoded By
Mass 33,153
Kinetics
Metal Binding
Rhea ID RHEA:19233; RHEA:19234; RHEA:34179; RHEA:34180
Cross Reference Brenda