| IED ID | IndEnz0007000032 |
| Enzyme Type ID | catalase000032 |
| Protein Name |
Allene oxide synthase-lipoxygenase protein Includes: Allene oxide synthase AOS EC 4.2.1.- Hydroperoxidehydrase ; Arachidonate 8-lipoxygenase EC 1.13.11.40 |
| Gene Name | |
| Organism | Plexaura homomalla (Black sea rod) |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Metazoa Eumetazoa Cnidaria Anthozoa (anthozoans) Octocorallia Alcyonacea (soft corals) Holaxonia Plexauridae Plexaura Plexaura homomalla (Black sea rod) |
| Enzyme Sequence | MTWKNFGFEIFGEKYGQEELEKRIKDEHTPPPDSPVFGGLKLKLKKEKFKTLFTLGTTLKGFRRATHTVGTGGIGEITIVNDPKFPEHEFFTAGRTFPARLRHANLKYPDDAGADARSFSIKFADSDSDGPLDIVMNTGEANIFWNSPSLEDFVPVEEGDAAEEYVYKNPYYYYNLVEALRRAPDTFAHLYYYSQVTMPFKAKDGKVRYCRYRALPGDVDIKEEDESGRLTEEEQRKIWIFSRHENEKRPDDYLRKEYVERLQKGPVNYRLQIQIHEASPDDTATIFHAGILWDKETHPWFDLAKVSIKTPLSPDVLEKTAFNIANQPASLGLLEAKSPEDYNSIGELRVAVYTWVQHLRKLKIGSLVPAGQNAIYNVEVETGDREHAGTDATITIRITGAKGRTDYLKLDKWFHNDFEAGSKEQYTVQGFDVGDIQLIELHSDGGGYWSGDPDWFVNRVIIISSTQDRVYSFPCFRWVIKDMVLFPGEATLPFNEVPAIVSEQRQKELEQRKLTYQWDYVSDDMPGNIKAKTHDDLPRDVQFTDEKSRSYQESRKAALVNLGIGSLFTMFENWDSYDDYHILYRNWILGGTPNMADRWHEDRWFGYQFLNGANPVILTRCDALPSNFPVTNEHVNASLDRGKNLDEEIKDGHIYIVDFKVLVGAKSYGGPVLEDIGYKVPDHLKHDEADIRYCAAPLALFYVNKLGHLMPIAIQINQEPGPENPIWTPHEENEHDWMMAKFWLGVAESNFHQLNTHLLRTHLTTESFALSTWRNLASAHPVFKLLQPHIYGVLAIDTIGRKELIGSGGIVDQSLSLGGGGHVTFMEKCFKEVNLQDYHLPNALKKRGVDDPSKLPGFYYRDDGLALWEAIETFIGEIIAIFYKNDDDVKRDNEIQSWIYDVHKNGWRVNPGHQDHGVPASFESREQLKEVLTSLVFTFSCQHAAVNFSQKDHYGFTPNAPAVLRHPPPKKKGEATLQSILSTLPSKSQAAKAIATVYILTKFSEDERYLGNYSATAWEDKDALDAINRFQDKLEDISKKIKQRNENLEVPYIYLLPERIPNGTAI |
| Enzyme Length | 1066 |
| Uniprot Accession Number | O16025 |
| Absorption | |
| Active Site | |
| Activity Regulation | ACTIVITY REGULATION: Lipoxygenase activity is stimulated by calcium, sodium, lithium and potassium ions. Calcium binding promotes interaction with membranes and thus facilitates access to substrates. {ECO:0000269|PubMed:10559269, ECO:0000269|PubMed:16162493}. |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=(5Z,8Z,11Z,14Z)-eicosatetraenoate + O2 = (8R)-hydroperoxy-(5Z,9E,11Z,14Z)-eicosatetraenoate; Xref=Rhea:RHEA:14985, ChEBI:CHEBI:15379, ChEBI:CHEBI:32395, ChEBI:CHEBI:57447; EC=1.13.11.40; Evidence={ECO:0000269|PubMed:10559269, ECO:0000269|PubMed:9302294};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:14986; Evidence={ECO:0000269|PubMed:10559269, ECO:0000269|PubMed:9302294}; CATALYTIC ACTIVITY: Reaction=(8R)-hydroperoxy-(5Z,9E,11Z,14Z)-eicosatetraenoate = 8,9-epoxy-(5Z,9E,11Z,14Z)-eicosatetraenoate + H2O; Xref=Rhea:RHEA:51344, ChEBI:CHEBI:15377, ChEBI:CHEBI:57447, ChEBI:CHEBI:134054; Evidence={ECO:0000269|PubMed:10559269, ECO:0000269|PubMed:29909837, ECO:0000269|PubMed:9302294};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:51345; Evidence={ECO:0000269|PubMed:10559269, ECO:0000269|PubMed:29909837, ECO:0000269|PubMed:9302294}; CATALYTIC ACTIVITY: Reaction=(5Z,8Z,11Z,14Z,17Z)-eicosapentaenoate + O2 = (8R)-hydroperoxy-(5Z,9E,11Z,14Z,17Z)-eicosapentaenoate; Xref=Rhea:RHEA:51412, ChEBI:CHEBI:15379, ChEBI:CHEBI:58562, ChEBI:CHEBI:134079; Evidence={ECO:0000305|PubMed:10559269};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:51413; Evidence={ECO:0000305|PubMed:10559269}; CATALYTIC ACTIVITY: Reaction=(4Z,7Z,10Z,13Z,16Z,19Z)-docosahexaenoate + O2 = 10-hydroperoxy-(4Z,7Z,11E,13Z,16Z,19Z)-docosahexaenoate; Xref=Rhea:RHEA:51340, ChEBI:CHEBI:15379, ChEBI:CHEBI:77016, ChEBI:CHEBI:134057; Evidence={ECO:0000269|PubMed:10559269};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:51341; Evidence={ECO:0000269|PubMed:10559269}; CATALYTIC ACTIVITY: Reaction=(8Z,11Z,14Z)-eicosatrienoate + O2 = (8R)-hydroperoxy-(9E,11Z,14Z)-eicosatrienoate; Xref=Rhea:RHEA:51324, ChEBI:CHEBI:15379, ChEBI:CHEBI:71589, ChEBI:CHEBI:134051; Evidence={ECO:0000305|PubMed:10559269};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:51325; Evidence={ECO:0000305|PubMed:10559269}; CATALYTIC ACTIVITY: Reaction=(8Z,11Z,14Z)-eicosatrienoate + O2 = 10-hydroperoxy-(8Z,11Z,14Z)-eicosatrienoate; Xref=Rhea:RHEA:51328, ChEBI:CHEBI:15379, ChEBI:CHEBI:71589, ChEBI:CHEBI:134052; Evidence={ECO:0000269|PubMed:10559269};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:51329; Evidence={ECO:0000269|PubMed:10559269}; CATALYTIC ACTIVITY: Reaction=(8Z,11Z,14Z)-eicosatrienoate + O2 = 11-hydroperoxy-(8Z,12E,14Z)-eicosatrienoate; Xref=Rhea:RHEA:51332, ChEBI:CHEBI:15379, ChEBI:CHEBI:71589, ChEBI:CHEBI:134053; Evidence={ECO:0000269|PubMed:10559269};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:51333; Evidence={ECO:0000269|PubMed:10559269}; |
| DNA Binding | |
| EC Number | 4.2.1.-; 1.13.11.40 |
| Enzyme Function | FUNCTION: Bifunctional enzyme which is responsible for allene oxide biosynthesis via a two-step reaction; first the lipoxygenase reaction that converts polyunsaturated fatty acids such as arachidonate ((5Z,8Z,11Z,14Z)-eicosatetraenoate) into a (8R)-hydroperoxide intermediate ((8R)-hydroperoxy-(5Z,9E,11Z,14Z)-eicosatetraenoate) followed by the allene oxide synthase reaction that converts the hydroperoxide intermediate ((8R)-hydroperoxy-(5Z,9E,11Z,14Z)-eicosatetraenoate) into the allene oxide (8,9-epoxy-(5Z,9E,11Z,14Z)-eicosatetraenoate) (PubMed:9302294, PubMed:10559269). Shows preference for C20 or C22 highly polyunsaturated fatty acids and no activity with C18 fatty acids in vitro (PubMed:10559269). Fatty acid allene oxides are intermediates in the formation of cyclopentenones or hydrolytic products in marine systems, most notably the prostanoid-related clavulones (PubMed:29909837). {ECO:0000269|PubMed:10559269, ECO:0000269|PubMed:9302294, ECO:0000303|PubMed:29909837}. |
| Temperature Dependency | |
| PH Dependency | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 7.0. {ECO:0000269|PubMed:10559269}; |
| Pathway | PATHWAY: Lipid metabolism; arachidonate metabolism.; PATHWAY: Lipid metabolism; fatty acid metabolism. |
| nucleotide Binding | |
| Features | Beta strand (31); Chain (1); Domain (2); Helix (43); Metal binding (15); Mutagenesis (4); Region (2); Turn (9) |
| Keywords | 3D-structure;Calcium;Cytoplasm;Dioxygenase;Fatty acid biosynthesis;Fatty acid metabolism;Heme;Iron;Lipid biosynthesis;Lipid metabolism;Lyase;Membrane;Metal-binding;Multifunctional enzyme;Oxidoreductase;Oxylipin biosynthesis |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|PROSITE-ProRule:PRU00726, ECO:0000269|PubMed:16162493}. Membrane {ECO:0000269|PubMed:16162493}; Peripheral membrane protein {ECO:0000269|PubMed:16162493}. Note=Calcium binding promotes binding to membranes. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | X-ray crystallography (7) |
| Cross Reference PDB | 1U5U; 2FNQ; 3DY5; 3FG1; 3FG3; 3FG4; 4QWT; |
| Mapped Pubmed ID | 18007054; 18785758; 19594169; 25231982; |
| Motif | |
| Gene Encoded By | |
| Mass | 121,783 |
| Kinetics | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=45.28 uM for arachidonate ((5Z,8Z,11Z,14Z)-eicosatetraenoate) {ECO:0000269|PubMed:10559269}; |
| Metal Binding | METAL 353; /note=Iron (heme axial ligand); catalytic; METAL 387; /note=Calcium 1; via carbonyl oxygen; structural; /evidence=ECO:0000269|PubMed:16162493; METAL 389; /note=Calcium 1; via carbonyl oxygen; structural; /evidence=ECO:0000269|PubMed:16162493; METAL 390; /note=Calcium 2; via carbonyl oxygen; structural; /evidence=ECO:0000269|PubMed:16162493; METAL 391; /note=Calcium 2; structural; /evidence=ECO:0000269|PubMed:16162493; METAL 416; /note=Calcium 2; structural; /evidence=ECO:0000269|PubMed:16162493; METAL 417; /note=Calcium 2; via carbonyl oxygen; structural; /evidence=ECO:0000269|PubMed:16162493; METAL 419; /note=Calcium 2; structural; /evidence=ECO:0000269|PubMed:16162493; METAL 452; /note=Calcium 1; via carbonyl oxygen; structural; /evidence=ECO:0000269|PubMed:16162493; METAL 454; /note=Calcium 1; via carbonyl oxygen; structural; /evidence=ECO:0000269|PubMed:16162493; METAL 757; /note=Iron; catalytic; METAL 762; /note=Iron; catalytic; METAL 943; /note=Iron; catalytic; METAL 947; /note=Iron; catalytic; METAL 1066; /note=Iron; via carboxylate; catalytic |
| Rhea ID | RHEA:14985; RHEA:14986; RHEA:51344; RHEA:51345; RHEA:51412; RHEA:51413; RHEA:51340; RHEA:51341; RHEA:51324; RHEA:51325; RHEA:51328; RHEA:51329; RHEA:51332; RHEA:51333 |
| Cross Reference Brenda | 1.13.11.40; |