| IED ID | IndEnz0005000483 |
| Enzyme Type ID | lipase000483 |
| Protein Name |
Acylcarnitine hydrolase ACH M1 EC 3.1.1.28 Carboxylic ester hydrolase EC 3.1.1.- |
| Gene Name | Ces2c Ces2 Ces2l |
| 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 | MARKQPHSWLNAVLFGLLLILIHVWGQDSPESSSIRTTHTGQVRGKLDHVRDTKAGVHTFLGIPFAKAPVGPLRFAPPEDPEPWSGVRDGTSHPAMCLQNIDMLDEVGLTDMKMILSSIPMSEDCLYLNIYTPAHAHEGSNLPVMVCIHGGALVIGMASMCDGSLLAVNEDLVVVAIQYRLGVLGFFSTGDEHARGNWGYLDQVAALRWVQQNIAHFGGNPNRVTIFGVSAGGTSVSSHVISPMSQGLFHGAIMESGVALLPDLISETSETVSTTVAKLSGCEATDSETLVRCLRAKSGAEILVINKVFKMIPAVVDGEFLPRHPKELLASEDFHPVPSIIGVNTDEYCCTIPMVMGTAQIIKELSRENLQAVLKDTAAQMMLPPECGDLLMEEYMGNTDDPQTLQIQYAEMMGDFLFVIPALQVAHFQRSHAPVYFYEFQHAPSYFKNVRPPHVKADHADEVPFVFGSFFWGIKVDFTEEEKLLSRRMMKYWANFARHGNPNSEGLPYWPVLDHDEQYLQLDTQPAVDRALKARRLQFWTKTLPQKIQELNGAQKNHAEL |
| Enzyme Length | 561 |
| Uniprot Accession Number | O70631 |
| 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=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:0000305|PubMed:12230550};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:13934; Evidence={ECO:0000305|PubMed:12230550}; 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:0000250|UniProtKB:Q91WG0}; |
| 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 (By similarity). May also hydrolyze retinyl esters (PubMed:12230550). {ECO:0000250|UniProtKB:Q91WG0, ECO:0000269|PubMed:12230550}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (3); Chain (1); Disulfide bond (2); Sequence conflict (1); Signal peptide (1) |
| Keywords | Disulfide bond;Endoplasmic reticulum;Hydrolase;Lipid metabolism;Microsome;Reference proteome;Signal |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Microsome {ECO:0000269|PubMed:12230550}. Endoplasmic reticulum {ECO:0000250|UniProtKB:Q91WG0}. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | SIGNAL 1..26; /evidence=ECO:0000255|RuleBase:RU361235 |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 62,170 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | RHEA:13933; RHEA:13934; RHEA:17101 |
| Cross Reference Brenda | 3.1.1.1; |