KEGG   ENZYME: 1.13.11.60
Entry
EC 1.13.11.60               Enzyme                                 
Name
linoleate 8R-lipoxygenase;
linoleic acid 8R-dioxygenase;
5,8-LDS (bifunctional enzyme);
7,8-LDS (bifunctional enzyme);
5,8-linoleate diol synthase (bifunctional enzyme);
7,8-linoleate diol synthase (bifunctional enzyme);
PpoA
Class
Oxidoreductases;
Acting on single donors with incorporation of molecular oxygen (oxygenases);
With incorporation of two atoms of oxygen
Sysname
linoleate:oxygen (8R)-oxidoreductase
Reaction(IUBMB)
linoleate + O2 = (8R,9Z,12Z)-8-hydroperoxyoctadeca-9,12-dienoate [RN:R07061]
Reaction(KEGG)
R07061
Substrate
linoleate [CPD:C01595];
O2 [CPD:C00007]
Product
(8R,9Z,12Z)-8-hydroperoxyoctadeca-9,12-dienoate [CPD:C14831]
Comment
The enzyme contains heme [1,4]. The bifunctional enzyme from Aspergillus nidulans uses different heme domains to catalyse two separate reactions. Linoleic acid is oxidized within the N-terminal heme peroxidase domain to (8R,9Z,12Z)-8-hydroperoxyoctadeca-9,12-dienoate, which is subsequently isomerized by the C-terminal P-450 heme thiolate domain to (5S,8R,9Z,12Z)-5,8-dihydroxyoctadeca-9,12-dienoate (cf. EC 5.4.4.5, 9,12-octadecadienoate 8-hydroperoxide 8R-isomerase) [1]. The bifunctional enzyme from Gaeumannomyces graminis also catalyses the oxidation of linoleic acid to (8R,9Z,12Z)-8-hydroperoxyoctadeca-9,12-dienoate, but its second domain isomerizes it to (7S,8S,9Z,12Z)-5,8-dihydroxyoctadeca-9,12-dienoate (cf. EC 5.4.4.6, 9,12-octadecadienoate 8-hydroperoxide 8S-isomerase) [4].
History
EC 1.13.11.60 created 2011
Pathway
ec00591  Linoleic acid metabolism
Orthology
K17863  linoleate 8R-lipoxygenase / 9,12-octadecadienoate 8-hydroperoxide 8R-isomerase
K17864  linoleate 8R-lipoxygenase / 9,12-octadecadienoate 8-hydroperoxide 8S-isomerase
Genes
PAN: PODANSg09720
PBEL: QC761_104690
PPSD: QC762_104690
PPSP: QC763_104690
PPSA: QC764_104690
MGR: MGG_13239
PPEI: PpBr36_02801
PGRI: PgNI_01911
CHIG: CH63R_03596
ANI: ANIA_01967
AFM: AFUA_4G10770
ACT: ACLA_049940
NFI: NFIA_105320
AOR: AO090003001138
ANG: An04g05880
AFV: AFLA_000529
ALUC: AKAW2_51557A
ACHE: ACHE_10811S
APUU: APUU_21090S
PCS: N7525_005537
PDP: PDIP_33150
POU: POX_d06058
TMF: EYB26_002074
CIM: CIMG_01479
CPW: CPC735_049620
URE: UREG_05116
ABE: ARB_02272
TVE: TRV_04981
PBL: PAAG_02631
PBN: PADG_01651
AJE: HCAG_01669
RSX: RhiXN_10303
MORE: E1B28_012947
PTRC: PtA15_12A250
PSTR: Pst134EA_022959
RIE: OCT59_013577
 » show all
Reference
1  [PMID:19286665]
  Authors
Brodhun F, Gobel C, Hornung E, Feussner I
  Title
Identification of PpoA from Aspergillus nidulans as a fusion protein of a fatty acid heme dioxygenase/peroxidase and a cytochrome P450.
  Journal
J Biol Chem 284:11792-805 (2009)
DOI:10.1074/jbc.M809152200
  Sequence
[ani:ANIA_01967]
Reference
2  [PMID:8117115]
  Authors
Hamberg M, Zhang LY, Brodowsky ID, Oliw EH.
  Title
Sequential oxygenation of linoleic acid in the fungus Gaeumannomyces graminis: stereochemistry of dioxygenase and hydroperoxide isomerase reactions.
  Journal
Arch Biochem Biophys 309:77-80 (1994)
DOI:10.1006/abbi.1994.1087
Reference
3  [PMID:18586008]
  Authors
Garscha U, Oliw E
  Title
Pichia expression and mutagenesis of 7,8-linoleate diol synthase change the dioxygenase and hydroperoxide isomerase.
  Journal
Biochem Biophys Res Commun 373:579-83 (2008)
DOI:10.1016/j.bbrc.2008.06.060
Reference
4  [PMID:8662736]
  Authors
Su C, Oliw EH
  Title
Purification and characterization of linoleate 8-dioxygenase from the fungus Gaeumannomyces graminis as a novel hemoprotein.
  Journal
J Biol Chem 271:14112-8 (1996)
DOI:10.1074/jbc.271.24.14112
  Sequence
[ag:AAD49559]
Other DBs
ExplorEnz - The Enzyme Database: 1.13.11.60
IUBMB Enzyme Nomenclature: 1.13.11.60
ExPASy - ENZYME nomenclature database: 1.13.11.60
BRENDA, the Enzyme Database: 1.13.11.60
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