| IED ID | IndEnz0002016524 |
| Enzyme Type ID | protease016524 |
| Protein Name |
Peroxisomal acyl-coenzyme A oxidase 1 AOX EC 1.3.3.6 Palmitoyl-CoA oxidase Straight-chain acyl-CoA oxidase SCOX Cleaved into: Peroxisomal acyl-CoA oxidase 1, A chain; Peroxisomal acyl-CoA oxidase 1, B chain; Peroxisomal acyl-CoA oxidase 1, C chain |
| Gene Name | ACOX1 ACOX |
| 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 | MNPDLRRERDSASFNPELLTHILDGSPEKTRRRREIENMILNDPDFQHEDLNFLTRSQRYEVAVRKSAIMVKKMREFGIADPDEIMWFKKLHLVNFVEPVGLNYSMFIPTLLNQGTTAQKEKWLLSSKGLQIIGTYAQTEMGHGTHLRGLETTATYDPETQEFILNSPTVTSIKWWPGGLGKTSNHAIVLAQLITKGKCYGLHAFIVPIREIGTHKPLPGITVGDIGPKFGYDEIDNGYLKMDNHRIPRENMLMKYAQVKPDGTYVKPLSNKLTYGTMVFVRSFLVGEAARALSKACTIAIRYSAVRHQSEIKPGEPEPQILDFQTQQYKLFPLLATAYAFQFVGAYMKETYHRINEGIGQGDLSELPELHALTAGLKAFTSWTANTGIEACRMACGGHGYSHCSGLPNIYVNFTPSCTFEGENTVMMLQTARFLMKSYDQVHSGKLVCGMVSYLNDLPSQRIQPQQVAVWPTMVDINSPESLTEAYKLRAARLVEIAAKNLQKEVIHRKSKEVAWNLTSVDLVRASEAHCHYVVVKLFSEKLLKIQDKAIQAVLRSLCLLYSLYGISQNAGDFLQGSIMTEPQITQVNQRVKELLTLIRSDAVALVDAFDFQDVTLGSVLGRYDGNVYENLFEWAKNSPLNKAEVHESYKHLKSLQSKL |
| Enzyme Length | 660 |
| Uniprot Accession Number | Q15067 |
| Absorption | |
| Active Site | ACT_SITE 421; /note=Proton acceptor; /evidence=ECO:0000250|UniProtKB:P07872 |
| Activity Regulation | |
| Binding Site | BINDING 139; /note=FAD; /evidence=ECO:0000250|UniProtKB:P07872; BINDING 178; /note=FAD; via amide nitrogen; /evidence=ECO:0000250|UniProtKB:P07872 |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=a 2,3-saturated acyl-CoA + O2 = a (2E)-enoyl-CoA + H2O2; Xref=Rhea:RHEA:38959, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, ChEBI:CHEBI:58856, ChEBI:CHEBI:65111; EC=1.3.3.6; Evidence={ECO:0000269|PubMed:17603022};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38960; Evidence={ECO:0000305|PubMed:17603022}; CATALYTIC ACTIVITY: Reaction=hexadecanoyl-CoA + O2 = (2E)-hexadecenoyl-CoA + H2O2; Xref=Rhea:RHEA:40167, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, ChEBI:CHEBI:57379, ChEBI:CHEBI:61526; Evidence={ECO:0000269|PubMed:17603022};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40168; Evidence={ECO:0000305|PubMed:17603022}; CATALYTIC ACTIVITY: Reaction=dodecanoyl-CoA + O2 = (2E)-dodecenoyl-CoA + H2O2; Xref=Rhea:RHEA:40171, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, ChEBI:CHEBI:57330, ChEBI:CHEBI:57375; Evidence={ECO:0000269|PubMed:17603022};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40172; Evidence={ECO:0000305|PubMed:17603022}; CATALYTIC ACTIVITY: Reaction=O2 + octanoyl-CoA = (2E)-octenoyl-CoA + H2O2; Xref=Rhea:RHEA:40175, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, ChEBI:CHEBI:57386, ChEBI:CHEBI:62242; Evidence={ECO:0000269|PubMed:17603022};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40176; Evidence={ECO:0000305|PubMed:17603022}; CATALYTIC ACTIVITY: Reaction=decanoyl-CoA + O2 = (2E)-decenoyl-CoA + H2O2; Xref=Rhea:RHEA:40179, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, ChEBI:CHEBI:61406, ChEBI:CHEBI:61430; Evidence={ECO:0000269|PubMed:17603022};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40180; Evidence={ECO:0000305|PubMed:17603022}; CATALYTIC ACTIVITY: Reaction=O2 + tetradecanoyl-CoA = (2E)-tetradecenoyl-CoA + H2O2; Xref=Rhea:RHEA:40183, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, ChEBI:CHEBI:57385, ChEBI:CHEBI:61405; Evidence={ECO:0000269|PubMed:17603022};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40184; Evidence={ECO:0000305|PubMed:17603022}; CATALYTIC ACTIVITY: Reaction=hexadecanedioyl-CoA + O2 = (2E)-hexadecenedioyl-CoA + H2O2; Xref=Rhea:RHEA:40275, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, ChEBI:CHEBI:77075, ChEBI:CHEBI:77085; Evidence={ECO:0000269|PubMed:17603022};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40276; Evidence={ECO:0000305|PubMed:17603022}; CATALYTIC ACTIVITY: Reaction=O2 + tetracosanoyl-CoA = (2E)-tetracosenoyl-CoA + H2O2; Xref=Rhea:RHEA:40319, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, ChEBI:CHEBI:65052, ChEBI:CHEBI:74693; Evidence={ECO:0000250|UniProtKB:P07872};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40320; Evidence={ECO:0000250|UniProtKB:P07872}; CATALYTIC ACTIVITY: Reaction=glutaryl-CoA + O2 = (2E)-glutaconyl-CoA + H2O2; Xref=Rhea:RHEA:40315, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, ChEBI:CHEBI:57353, ChEBI:CHEBI:57378; Evidence={ECO:0000250|UniProtKB:P07872};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40316; Evidence={ECO:0000250|UniProtKB:P07872}; CATALYTIC ACTIVITY: Reaction=hexanoyl-CoA + O2 = (2E)-hexenoyl-CoA + H2O2; Xref=Rhea:RHEA:40311, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, ChEBI:CHEBI:62077, ChEBI:CHEBI:62620; Evidence={ECO:0000250|UniProtKB:P07872};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40312; Evidence={ECO:0000250|UniProtKB:P07872}; CATALYTIC ACTIVITY: Reaction=O2 + octadecanoyl-CoA = (2E)-octadecenoyl-CoA + H2O2; Xref=Rhea:RHEA:38971, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, ChEBI:CHEBI:57394, ChEBI:CHEBI:71412; Evidence={ECO:0000250|UniProtKB:P07872};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38972; Evidence={ECO:0000250|UniProtKB:P07872}; |
| DNA Binding | |
| EC Number | 1.3.3.6 |
| Enzyme Function | FUNCTION: Catalyzes the desaturation of acyl-CoAs to 2-trans-enoyl-CoAs. First enzyme of the fatty acid beta-oxidation pathway. {ECO:0000269|PubMed:15060085, ECO:0000269|PubMed:17458872, ECO:0000269|PubMed:17603022, ECO:0000269|PubMed:32169171}.; FUNCTION: [Isoform 1]: Shows highest activity against medium-chain fatty acyl-CoAs and activity decreases with increasing chain length. {ECO:0000269|PubMed:17603022}.; FUNCTION: [Isoform 2]: Is active against a much broader range of substrates and shows activity towards very long-chain acyl-CoAs. Is twice as active as isoform 1 against 16-hydroxy-palmitoyl-CoA and is 25% more active against 1,16-hexadecanodioyl-CoA. {ECO:0000269|PubMed:17603022}. |
| Temperature Dependency | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature for isoform 1 at pH 7.5 is 40 degrees Celsius with no activity at 50 degrees Celsius. Optimum temperature for isoform 2 at pH 7.5 is 47.5 degrees Celsius with 57% activity retained at 50 degrees Celsius. {ECO:0000269|PubMed:17603022}; |
| PH Dependency | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 8.5 for isoform 1 and 7.5-8.5 for isoform 2. {ECO:0000269|PubMed:17603022}; |
| Pathway | PATHWAY: Lipid metabolism; peroxisomal fatty acid beta-oxidation. {ECO:0000269|PubMed:17603022}. |
| nucleotide Binding | |
| Features | Active site (1); Alternative sequence (2); Binding site (2); Chain (3); Erroneous initiation (1); Modified residue (24); Motif (1); Natural variant (11); Sequence conflict (22); Site (1) |
| Keywords | Acetylation;Alternative splicing;Deafness;Disease variant;FAD;Fatty acid metabolism;Flavoprotein;Lipid metabolism;Neuropathy;Oxidoreductase;Peroxisome;Phosphoprotein;Reference proteome |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Peroxisome {ECO:0000269|PubMed:32169171}. |
| Modified Residue | MOD_RES 26; /note="Phosphoserine"; /evidence="ECO:0007744|PubMed:17081983, ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"; MOD_RES 89; /note="N6-succinyllysine"; /evidence="ECO:0000250|UniProtKB:Q9R0H0"; MOD_RES 90; /note="N6-succinyllysine"; /evidence="ECO:0000250|UniProtKB:Q9R0H0"; MOD_RES 216; /note="N6-acetyllysine"; /evidence="ECO:0000250|UniProtKB:Q9R0H0"; MOD_RES 241; /note="N6-succinyllysine"; /evidence="ECO:0000250|UniProtKB:Q9R0H0"; MOD_RES 255; /note="N6-acetyllysine"; /evidence="ECO:0007744|PubMed:19608861"; MOD_RES 267; /note="N6-acetyllysine"; /evidence="ECO:0007744|PubMed:19608861"; MOD_RES 272; /note="N6-acetyllysine"; /evidence="ECO:0000250|UniProtKB:Q9R0H0"; MOD_RES 349; /note="N6-succinyllysine"; /evidence="ECO:0000250|UniProtKB:Q9R0H0"; MOD_RES 437; /note="N6-acetyllysine; alternate"; /evidence="ECO:0007744|PubMed:19608861"; MOD_RES 437; /note="N6-succinyllysine; alternate"; /evidence="ECO:0000250|UniProtKB:Q9R0H0"; MOD_RES 446; /note="N6-acetyllysine; alternate"; /evidence="ECO:0000250|UniProtKB:Q9R0H0"; MOD_RES 446; /note="N6-succinyllysine; alternate"; /evidence="ECO:0000250|UniProtKB:Q9R0H0"; MOD_RES 500; /note="N6-acetyllysine"; /evidence="ECO:0007744|PubMed:19608861"; MOD_RES 504; /note="N6-acetyllysine"; /evidence="ECO:0007744|PubMed:19608861"; MOD_RES 512; /note="N6-acetyllysine; alternate"; /evidence="ECO:0000250|UniProtKB:Q9R0H0"; MOD_RES 512; /note="N6-succinyllysine; alternate"; /evidence="ECO:0000250|UniProtKB:Q9R0H0"; MOD_RES 542; /note="N6-succinyllysine"; /evidence="ECO:0000250|UniProtKB:Q9R0H0"; MOD_RES 637; /note="N6-acetyllysine; alternate"; /evidence="ECO:0000250|UniProtKB:Q9R0H0"; MOD_RES 637; /note="N6-succinyllysine; alternate"; /evidence="ECO:0000250|UniProtKB:Q9R0H0"; MOD_RES 643; /note="N6-succinyllysine"; /evidence="ECO:0000250|UniProtKB:Q9R0H0"; MOD_RES 649; /note="Phosphoserine"; /evidence="ECO:0000250|UniProtKB:Q9R0H0"; MOD_RES 651; /note="N6-acetyllysine"; /evidence="ECO:0000250|UniProtKB:Q9R0H0"; MOD_RES 654; /note="N6-succinyllysine"; /evidence="ECO:0000250|UniProtKB:Q9R0H0" |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | 10022913; 11101887; 11500517; 11734571; 12456682; 12559034; 12578380; 12885776; 17007944; 17255948; 18536048; 18660489; 18712838; 19197237; 19584060; 19632994; 19710929; 20110263; 20178365; 20562859; 21976670; 22002062; 22747494; 23459139; 23933200; 23963456; 24189400; 24235149; 24418004; 25260751; 25854684; 26220973; 28765278; 28787099; 31126802; 32434419; 33234382; 7719337; 7790377; 8656081; 8824437; 8858165; 9653144; 9668159; 9837948; |
| Motif | MOTIF 658..660; /note=Microbody targeting signal |
| Gene Encoded By | |
| Mass | 74,424 |
| Kinetics | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=73 uM for palmitoyl-CoA (isoform 1) {ECO:0000269|PubMed:17603022}; KM=90 uM for palmitoyl-CoA (isoform 2) {ECO:0000269|PubMed:17603022}; |
| Metal Binding | |
| Rhea ID | RHEA:38959; RHEA:38960; RHEA:40167; RHEA:40168; RHEA:40171; RHEA:40172; RHEA:40175; RHEA:40176; RHEA:40179; RHEA:40180; RHEA:40183; RHEA:40184; RHEA:40275; RHEA:40276; RHEA:40319; RHEA:40320; RHEA:40315; RHEA:40316; RHEA:40311; RHEA:40312; RHEA:38971; RHEA:38972 |
| Cross Reference Brenda | 1.3.3.6; |