| IED ID | IndEnz0005001210 |
| Enzyme Type ID | lipase001210 |
| Protein Name |
Arylacetamide deacetylase EC 3.1.1.3 |
| Gene Name | AADAC DAC |
| 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 | MGRKSLYLLIVGILIAYYIYTPLPDNVEEPWRMMWINAHLKTIQNLATFVELLGLHHFMDSFKVVGSFDEVPPTSDENVTVTETKFNNILVRVYVPKRKSEALRRGLFYIHGGGWCVGSAALSGYDLLSRWTADRLDAVVVSTNYRLAPKYHFPIQFEDVYNALRWFLRKKVLAKYGVNPERIGISGDSAGGNLAAAVTQQLLDDPDVKIKLKIQSLIYPALQPLDVDLPSYQENSNFLFLSKSLMVRFWSEYFTTDRSLEKAMLSRQHVPVESSHLFKFVNWSSLLPERFIKGHVYNNPNYGSSELAKKYPGFLDVRAAPLLADDNKLRGLPLTYVITCQYDLLRDDGLMYVTRLRNTGVQVTHNHVEDGFHGAFSFLGLKISHRLINQYIEWLKENL |
| Enzyme Length | 399 |
| Uniprot Accession Number | P22760 |
| Absorption | |
| Active Site | ACT_SITE 189; /evidence="ECO:0000250|UniProtKB:Q8BLF1, ECO:0000255|PROSITE-ProRule:PRU10038"; ACT_SITE 343; /evidence="ECO:0000250|UniProtKB:Q8BLF1"; ACT_SITE 373; /evidence="ECO:0000250|UniProtKB:Q8BLF1" |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=a triacylglycerol + H2O = a diacylglycerol + a fatty acid + H(+); Xref=Rhea:RHEA:12044, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17855, ChEBI:CHEBI:18035, ChEBI:CHEBI:28868; EC=3.1.1.3; |
| DNA Binding | |
| EC Number | 3.1.1.3 |
| Enzyme Function | FUNCTION: Displays cellular triglyceride lipase activity in liver, increases the levels of intracellular fatty acids derived from the hydrolysis of newly formed triglyceride stores and plays a role in very low-density lipoprotein assembly. Displays serine esterase activity in liver. Deacetylates a variety of arylacetamide substrates, including xenobiotic compounds and procarcinogens, converting them to the primary arylamide compounds and increasing their toxicity. {ECO:0000269|PubMed:17936933, ECO:0000269|PubMed:19339378, ECO:0000269|PubMed:22207054, ECO:0000269|PubMed:22415931, ECO:0000269|PubMed:23542347}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (3); Chain (1); Disulfide bond (1); Frameshift (1); Glycosylation (2); Motif (1); Mutagenesis (2); Natural variant (2); Sequence conflict (2); Topological domain (2); Transmembrane (1) |
| Keywords | Direct protein sequencing;Disulfide bond;Endoplasmic reticulum;Glycoprotein;Hydrolase;Lipid metabolism;Membrane;Microsome;Reference proteome;Signal-anchor;Transmembrane;Transmembrane helix |
| Interact With | Q92624 |
| Induction | INDUCTION: Down-regulated following infection with hepatis C virus which results in impaired triacylglycerol lipolysis and impaired assembly of very low density lipoproteins. This may represent a cellular adaptation to infection that is aimed at limiting viral production. {ECO:0000269|PubMed:23542347}. |
| Subcellular Location | SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Single-pass type II membrane protein. Microsome membrane; Single-pass type II membrane protein. |
| Modified Residue | |
| Post Translational Modification | PTM: Glycosylation is required for enzyme activity. {ECO:0000269|PubMed:19159218, ECO:0000269|PubMed:24125761}. |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | 10318829; 19343046; 20379614; 20542992; 21856291; 22813719; 26444075; 27422753; 28606603; 29253601; 30670438; 31235486; 34450168; |
| Motif | MOTIF 111..113; /note=Involved in the stabilization of the negatively charged intermediate by the formation of the oxyanion hole; /evidence=ECO:0000250|UniProtKB:Q5NUF3 |
| Gene Encoded By | |
| Mass | 45,734 |
| Kinetics | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.8 mM for flutamide {ECO:0000269|PubMed:19339378, ECO:0000269|PubMed:22207054, ECO:0000269|PubMed:22415931, ECO:0000269|PubMed:24125761}; KM=0.6 mM for flutamide {ECO:0000269|PubMed:19339378, ECO:0000269|PubMed:22207054, ECO:0000269|PubMed:22415931, ECO:0000269|PubMed:24125761}; KM=0.472 mM for flutamide {ECO:0000269|PubMed:19339378, ECO:0000269|PubMed:22207054, ECO:0000269|PubMed:22415931, ECO:0000269|PubMed:24125761}; KM=3.05 mM for phenacetin {ECO:0000269|PubMed:19339378, ECO:0000269|PubMed:22207054, ECO:0000269|PubMed:22415931, ECO:0000269|PubMed:24125761}; KM=1.8 mM for phenacetin {ECO:0000269|PubMed:19339378, ECO:0000269|PubMed:22207054, ECO:0000269|PubMed:22415931, ECO:0000269|PubMed:24125761}; KM=1.42 mM for phenacetin {ECO:0000269|PubMed:19339378, ECO:0000269|PubMed:22207054, ECO:0000269|PubMed:22415931, ECO:0000269|PubMed:24125761}; KM=0.2 mM for rifampicin {ECO:0000269|PubMed:19339378, ECO:0000269|PubMed:22207054, ECO:0000269|PubMed:22415931, ECO:0000269|PubMed:24125761}; KM=0.154 mM for rifampicin {ECO:0000269|PubMed:19339378, ECO:0000269|PubMed:22207054, ECO:0000269|PubMed:22415931, ECO:0000269|PubMed:24125761}; Vmax=1.1 nmol/min/mg enzyme toward flutamide {ECO:0000269|PubMed:19339378, ECO:0000269|PubMed:22207054, ECO:0000269|PubMed:22415931, ECO:0000269|PubMed:24125761}; Vmax=0.617 nmol/min/mg enzyme toward flutamide {ECO:0000269|PubMed:19339378, ECO:0000269|PubMed:22207054, ECO:0000269|PubMed:22415931, ECO:0000269|PubMed:24125761}; Vmax=1.34 nmol/min/mg enzyme toward phenacetin {ECO:0000269|PubMed:19339378, ECO:0000269|PubMed:22207054, ECO:0000269|PubMed:22415931, ECO:0000269|PubMed:24125761}; Vmax=6.4 nmol/min/mg enzyme toward phenacetin {ECO:0000269|PubMed:19339378, ECO:0000269|PubMed:22207054, ECO:0000269|PubMed:22415931, ECO:0000269|PubMed:24125761}; Vmax=1.42 nmol/min/mg enzyme toward phenacetin {ECO:0000269|PubMed:19339378, ECO:0000269|PubMed:22207054, ECO:0000269|PubMed:22415931, ECO:0000269|PubMed:24125761}; Vmax=0.149 nmol/min/mg enzyme toward rifampicin {ECO:0000269|PubMed:19339378, ECO:0000269|PubMed:22207054, ECO:0000269|PubMed:22415931, ECO:0000269|PubMed:24125761}; Vmax=0.060 nmol/min/mg enzyme toward rifampicin {ECO:0000269|PubMed:19339378, ECO:0000269|PubMed:22207054, ECO:0000269|PubMed:22415931, ECO:0000269|PubMed:24125761}; |
| Metal Binding | |
| Rhea ID | RHEA:12044 |
| Cross Reference Brenda |