| IED ID | IndEnz0005000441 |
| Enzyme Type ID | lipase000441 |
| Protein Name |
Acylcarnitine hydrolase ACH M1 EC 3.1.1.28 Carboxylesterase 2 CES 2 Carboxylic ester hydrolase EC 3.1.1.- Peroxisome proliferator-inducible acylcarnitine hydrolase |
| Gene Name | Ces2c Ces2 |
| 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 | MTRNQLHNWLNAGFFGLLLLLIHVQGQDSPEANPIRNTHTGQIQGSLIHVKDTKAGVHTFLGIPFAKPPVGPLRFAPPEAPEPWSGVRDGTAHPAMCLQNLDMLNEAGLPDMKMMLSSFPMSEDCLYLNIYTPAHAHEGSNLPVMVWIHGGALVIGMASMFDGSLLTVNEDLVVVTIQYRLGVLGFFSTGDQHARGNWGYLDQAAALRWVQQNIAHFGGNPDRVTIFGESAGGTSVSSHVVSPMSQGLFHGAIMESGVALLPDLISETSEMVSTTVAKLSGCEAMDSQALVRCLRGKSEAEILAINKVFKMIPAVVDGEFFPRHPKELLASEDFHPVPSIIGVNNDEFGWSIPVVMGSAQMIKGITRENLQAVLKDTAVQMMLPPECSDLLMEEYMGDTEDAQTLQIQFTEMMGDFMFVIPALQVAHFQRSHAPVYFYEFQHPPSYFKDVRPPHVKADHADEIPFVFASFFWGMKLDFTEEEELLSRRMMKYWANFARHGNPNSEGLPYWPVMDHDEQYLQLDIQPAVGRALKAGRLQFWTKTLPQKIQELKASQDKHREL |
| Enzyme Length | 561 |
| Uniprot Accession Number | Q91WG0 |
| Absorption | |
| Active Site | ACT_SITE 230; /note=Acyl-ester intermediate; /evidence=ECO:0000255|PROSITE-ProRule:PRU10039; ACT_SITE 347; /note=Charge relay system; /evidence=ECO:0000250|UniProtKB:P23141; ACT_SITE 459; /note=Charge relay system; /evidence=ECO:0000250|UniProtKB:P23141 |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=H2O + O-acyl-(R)-carnitine = (R)-carnitine + a fatty acid + H(+); Xref=Rhea:RHEA:17101, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16347, ChEBI:CHEBI:28868, ChEBI:CHEBI:75659; EC=3.1.1.28; Evidence={ECO:0000269|PubMed:12859986}; CATALYTIC ACTIVITY: Reaction=all-trans-retinyl hexadecanoate + H2O = all-trans-retinol + H(+) + hexadecanoate; Xref=Rhea:RHEA:13933, ChEBI:CHEBI:7896, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17336, ChEBI:CHEBI:17616; Evidence={ECO:0000250|UniProtKB:O70631};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:13934; Evidence={ECO:0000250|UniProtKB:O70631}; |
| DNA Binding | |
| EC Number | 3.1.1.28; 3.1.1.- |
| Enzyme Function | FUNCTION: Hydrolase with high activity towards palmitoylcarnitine. Is also active with p-nitrophenylacetate and alpha-naphthylacetate. May also hydrolyze retinyl esters (By similarity). {ECO:0000250|UniProtKB:O70631, ECO:0000269|PubMed:12859986}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (3); Chain (1); Disulfide bond (2); Motif (1); Signal peptide (1) |
| Keywords | Direct protein sequencing;Disulfide bond;Endoplasmic reticulum;Hydrolase;Lipid metabolism;Microsome;Reference proteome;Serine esterase;Signal |
| Interact With | |
| Induction | INDUCTION: Up-regulated in liver by di-(2-ethylhexyl)phtalate (DEHP). {ECO:0000269|PubMed:12859986}. |
| Subcellular Location | SUBCELLULAR LOCATION: Microsome {ECO:0000269|PubMed:12859986}. Endoplasmic reticulum {ECO:0000305}. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | SIGNAL 1..26; /evidence=ECO:0000255 |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | 16141072; 16527247; 20931200; 28167773; |
| Motif | MOTIF 558..561; /note=Prevents secretion from ER; /evidence=ECO:0000255 |
| Gene Encoded By | |
| Mass | 62,470 |
| Kinetics | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=98.8 uM for palmitoyl-dl-carnitine; KM=392 uM for p-nitrophenylacetate; Vmax=1.67 umol/min/mg enzyme with palmitoyl-dl-carnitine; Vmax=353 umol/min/mg enzyme with p-nitrophenylacetate; |
| Metal Binding | |
| Rhea ID | RHEA:17101; RHEA:13933; RHEA:13934 |
| Cross Reference Brenda |