Detail Information for IndEnz0018001603
IED ID IndEnz0018001603
Enzyme Type ID peroxidase001603
Protein Name Psi-producing oxygenase A
Fatty acid oxygenase ppoA

Includes: Linoleate 8R-lipoxygenase
EC 1.13.11.60
; 9,12-octadecadienoate 8-hydroperoxide 8R-isomerase
EC 5.4.4.5
Gene Name ppoA
Organism Emericella nidulans (Aspergillus nidulans)
Taxonomic Lineage cellular organisms Eukaryota Opisthokonta Fungi Dikarya Ascomycota saccharomyceta Pezizomycotina leotiomyceta Eurotiomycetes Eurotiomycetidae Eurotiales (green and blue molds) Aspergillaceae Aspergillus Aspergillus subgen. Nidulantes Emericella nidulans (Aspergillus nidulans)
Enzyme Sequence MGEDKETNILAGLGNTISQVENVVAASLRPLPTATGDGTYVAESTQTGLAKDLSHVDLKDVRTLAEVVKSAATGEPVDDKQYIMERVIQLAAGLPSTSRNAAELTKSFLNMLWNDLEHPPVSYLGADSMHRKADGSGNNRFWPQLGAAGSAYARSVRPKTMQSPSLPDPETIFDCLLRRKEYREHPNKISSVLFYLASIIIHDLFQTDPKDNSVSKTSSYLDLSPLYGNNQDEQNLVRTFKDGKLKPDCFATKRVLGFPPGVGVLLIMFNRFHNYVVDQLAAINECGRFTKPDESNVDEYAKYDNNLFQTGRLVTCGLYANIILKDYVRTILNINRTDSTWSLDPRMEMKDGLLGEAAAMATGNQVSAEFNVVYRWHACISKRDEKWTEDFHREIMPGVDPSTLSMQDFVAGLGRWQAGLPQEPLERPFSGLQRKPDGAFNDDDLVNLFEKSVEDCAGAFGASHVPAIFKSVEALGIMQARRWNLGTLNEFRQYFNLAPHKTFEDINSDPYIADQLKRLYDHPDLVEIYPGVVVEEAKDSMVPGSGLCTNFTISRAILSDAVALVRGDRFYTVDYTPKHLTNWAYNEIQPNNAVDQGQVFYKLVLRAFPNHFDGNSIYAHFPLVVPSENEKILKSLGVAEKYSWEKPSRISHPIFISSHAACMSILENQETFKVTWGRKIEFLMQRDKHQYGKDFMLSGDRPPNAASRKMMGSALYRDEWEAEVKNFYEQTTLKLLHKNSYKLAGVNQVDIVRDVANLAQVHFCSSVFSLPLKTDSNPRGIFAESELYKIMAAVFTAIFYDADIGKSFELNQAARTVTQQLGQLTMANVEIIAKTGLIANLVNRLHRRDVLSEYGIHMIQRLLDSGLPATEIVWTHILPTAGGMVANQAQLFSQCLDYYLSEEGSGHLPEINRLAKENTPEADELLTRYFMEGARLRSSVALPRVAAQPTVVEDNGEKLTIKAGQVVMCNLVSACMDPTAFPDPEKVKLDRDMNLYAHFGFGPHKCLGLDLCKTGLSTMLKVLGRLDNLRRAPGAQGQLKKLSGPGGIAKYMNEDQSGFTPFPSTMKIQWDGELPQLKEDF
Enzyme Length 1081
Uniprot Accession Number Q6RET3
Absorption
Active Site ACT_SITE 374; /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:19286665}; CATALYTIC ACTIVITY: Reaction=(8R,9Z,12Z)-8-hydroperoxyoctadeca-9,12-dienoate = (5S,8R,9Z,12Z)-5,8-dihydroxyoctadeca-9,12-dienoate; Xref=Rhea:RHEA:31579, ChEBI:CHEBI:58659, ChEBI:CHEBI:63217; EC=5.4.4.5; Evidence={ECO:0000269|PubMed:19286665};
DNA Binding
EC Number 1.13.11.60; 5.4.4.5
Enzyme Function FUNCTION: Bifunctional heme-containing enzyme that oxidizes linoleic acid to (8R,9Z,12Z)-8-hydroperoxyoctadeca-9,12-dienoate (within the N-terminal heme peroxidase domain), which is subsequently isomerized to (5S,8R,9Z,12Z)-5,8-dihydroxyoctadeca-9,12-dienoate (within the C-terminal P450 heme thiolate domain). Oxidized unsaturated fatty acids, so-called oxylipins, derived from endogenous fatty acids, influence the development of the asexual conidiophores and sexual cleistothecia and regulate the secondary metabolism. These substances were collectively named psi factors and are primarily a mixture of hydroxylated oleic, linoleic and alpha-linolenic acids. They are termed psi-beta, psi-alpha, and psi-gamma, respectively. {ECO:0000269|PubMed:14699095}.
Temperature Dependency
PH Dependency BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 7-7.5. {ECO:0000269|PubMed:19286665};
Pathway
nucleotide Binding
Features Active site (1); Chain (1); Metal binding (2); Mutagenesis (2); Region (2)
Keywords Dioxygenase;Heme;Iron;Isomerase;Metal-binding;Multifunctional enzyme;Oxidoreductase;Peroxidase
Interact With
Induction
Subcellular Location
Modified Residue
Post Translational Modification
Signal Peptide
Structure 3D
Cross Reference PDB -
Mapped Pubmed ID -
Motif
Gene Encoded By
Mass 120,784
Kinetics BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=5 uM for palmitoleic acid {ECO:0000269|PubMed:19286665}; KM=6.71 uM for oleic acid {ECO:0000269|PubMed:19286665}; KM=18.3 uM for linoleic acid {ECO:0000269|PubMed:19286665}; KM=22.6 uM for alpha-linolenic acid {ECO:0000269|PubMed:19286665}; Vmax=1.76 umol/min/mg enzyme toward palmitoleic acid {ECO:0000269|PubMed:19286665}; Vmax=2.48 umol/min/mg enzyme toward oleic acid {ECO:0000269|PubMed:19286665}; Vmax=3.16 umol/min/mg enzyme toward linoleic acid {ECO:0000269|PubMed:19286665}; Vmax=2.97 umol/min/mg enzyme toward alpha-linolenic acid {ECO:0000269|PubMed:19286665};
Metal Binding METAL 202; /note=Iron (heme b axial ligand); /evidence=ECO:0000255|PROSITE-ProRule:PRU00298; METAL 377; /note=Iron (heme b axial ligand); /evidence=ECO:0000255|PROSITE-ProRule:PRU00298
Rhea ID RHEA:25395; RHEA:31579
Cross Reference Brenda 1.13.11.60;5.4.4.5;