Detail Information for IndEnz0018001256
IED ID IndEnz0018001256
Enzyme Type ID peroxidase001256
Protein Name Linoleate diol synthase
EC 1.13.11.60
EC 5.4.4.6
Linoleate
8R
-dioxygenase
Linoleate 8-dioxygenase
Gene Name
Organism Gaeumannomyces graminis var. graminis (Turf grass take-all root rot fungus)
Taxonomic Lineage cellular organisms Eukaryota Opisthokonta Fungi Dikarya Ascomycota saccharomyceta Pezizomycotina leotiomyceta sordariomyceta Sordariomycetes Sordariomycetidae Magnaporthales Magnaporthaceae Gaeumannomyces Gaeumannomyces graminis var. graminis (Turf grass take-all root rot fungus)
Enzyme Sequence MTVSTHHDDSPGLSGRLRDLLHHVFGNQKSPTVYPNAPGNSAKPVPTGLADDIDKLGFKDIDTLLIFLNSAVKGVNDDQQFLLEKMIQLLAKLPPASREGKKLTDGLINDLWDSLDHPPVASLGKGFSFREPDGSNNNIHLPSLGAANTPYARSTKPLVFQNPNPPDPATIFDTLMVRDPAKFRPHPNKISSMLFYLATIITHDIFQTSPRDFNINLTSSYLDLSPLYGRNHDEQMAVRTGKDGLLKPDTFSSKRVIGFPPGVGAFLIMFNRFHNYVVTQLAKINEGGRFKRPTTPDDTAGWETYDNSLFQTGRLITCGLYINIVLGDYVRTILNLNRANTTWNLDPRTKEGKSLLSKPTPEAVGNQVSVEFNLIYRWHCTISERDDKWTTNAMREALGGQDPATAKMEDVMRALGMFEKNIPDEPEKRTLAGLTRQSDGAFDDTELVKILQESIEDVAGAFGPNHVPACMRAIEILGIKQSRTWNVATLNEFRQFIGLTPHDSFYHMNPDPKICKILAQMYDSPDAVELYPGIMAEAAKPPFSPGSGLCPPYTTSRAILSDAVSLVRGDRFYTVDYTPRNITNWGFNEASTDKAVDWGHVIYKLFFRAFPNHFLPNSVYAHFPFVVPSENKLIFEGLGAANKYSWDPPKARAPIQFIRSHKAVLEVLSNQKDYKVTWGPAIKMLSGDPATSFALAGDEPANAASRHHVIAALTAPKQWRDEVRRFYEVTTRDLLRRHGAPVHGVGAGPRTHEVDVIRDVIGLAHARFMASLFSLPLKEEGKEEGAYGEHELYRSLVTIFAAIFWDSDVCNSLKLHQASKAAADKMSALIAEHVREMEAGTGFLGALGKLKDLITGNDVHANGNGVYTNGNGVYTNGNGVHTNGNGVHTNGNGVPHAAPSLRSFGDQLLQRMLSQDGRSIEETVSGTILPVVMAGTANQTQLLAQCLDYYLGVGEKHLPEMKRLAMLNTSEADEKLLKYTMEGCRIRGCVALYRAVVTDQAVDDTIPCIPNKDDPTFARPLSNPQVAESARTLKLSTGTRMLVDLTTASHDPAAFPDPDEVRLDRPLESYVHFGLGPHRCAGEPISQIALSSVMKVLLQLDGLRRAAGPRGEIRSYPASQWPGQAGRPPRDPAWSGLRTFTSADQSAFSPLATTMKINWEGRGDL
Enzyme Length 1165
Uniprot Accession Number Q9UUS2
Absorption
Active Site ACT_SITE 376; /evidence=ECO:0000255
Activity Regulation
Binding Site
Calcium Binding
catalytic Activity CATALYTIC ACTIVITY: Reaction=(9Z,12Z)-octadecadienoate + O2 = (8R,9Z,12Z)-8-hydroperoxyoctadeca-9,12-dienoate; Xref=Rhea:RHEA:25395, ChEBI:CHEBI:15379, ChEBI:CHEBI:30245, ChEBI:CHEBI:58659; EC=1.13.11.60; Evidence={ECO:0000269|PubMed:8662736}; CATALYTIC ACTIVITY: Reaction=(8R,9Z,12Z)-8-hydroperoxyoctadeca-9,12-dienoate = (7S,8S,9Z,12Z)-7,8-dihydroxyoctadeca-9,12-dienoate; Xref=Rhea:RHEA:25399, ChEBI:CHEBI:57468, ChEBI:CHEBI:58659; EC=5.4.4.6; Evidence={ECO:0000269|PubMed:8662736};
DNA Binding
EC Number 1.13.11.60; 5.4.4.6
Enzyme Function FUNCTION: Catalyzes the dioxygenation of linoleic acid to (8R)-hydroperoxylinoleate and isomerization of the resulting hydroperoxide to (7S,8S)-dihydroxylinoleate.
Temperature Dependency
PH Dependency BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 7.2-7.4. {ECO:0000269|PubMed:8662736};
Pathway
nucleotide Binding
Features Active site (1); Chain (1); Metal binding (2); Region (1)
Keywords Dioxygenase;Direct protein sequencing;Heme;Iron;Isomerase;Metal-binding;Oxidoreductase;Peroxidase
Interact With
Induction
Subcellular Location
Modified Residue
Post Translational Modification PTM: The N-terminus is blocked.
Signal Peptide
Structure 3D
Cross Reference PDB -
Mapped Pubmed ID -
Motif
Gene Encoded By
Mass 128,322
Kinetics BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=30 uM for oxygen {ECO:0000269|PubMed:8662736}; KM=8 uM for linoleic acid {ECO:0000269|PubMed:8662736}; Vmax=2.2 umol/min/mg enzyme toward oxygen {ECO:0000269|PubMed:8662736}; Vmax=4 umol/min/mg enzyme toward linoleic acid {ECO:0000269|PubMed:8662736};
Metal Binding METAL 203; /note=Iron (heme b axial ligand); /evidence=ECO:0000255|PROSITE-ProRule:PRU00298; METAL 379; /note=Iron (heme b axial ligand); /evidence=ECO:0000255|PROSITE-ProRule:PRU00298
Rhea ID RHEA:25395; RHEA:25399
Cross Reference Brenda 1.13.11.60;5.4.4.6;