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Catalytic Site Atlas

CSA LITERATURE entry for 1lnh

E.C. namelinoleate 9S-lipoxygenase
SpeciesGlycine max (Glycine hispida)
E.C. Number (IntEnz)
CSA Homologues of 1lnhThere are 36 Homologs
CSA Entries With UniProtID P09186
CSA Entries With EC Number
PDBe Entry 1lnh
PDBSum Entry 1lnh
MACiE Entry 1lnh

Literature Report

IntroductionLipoxygenase catalysis is an important aspect of polyunsaturated fatty acid metabolism. The enzyme catalyses the regio- and stereoselective incorporation of molecular oxygen into the methylene interrupted diene system of the substrate to produce a conjugated hydroperoxide product. The peroxidases are intermediates in biosynthetic pathways leading to physiologically potent metabolites in both plants (jasmonates) and animals (leukotrienes and lipoxins). Lipoxygenases contain a distinctive non-heme iron cofactor. Structure is Lipoxygenase 3 from soybean.
MechansimThe current working hypothesis concerning the mechanism of the catalysed reaction, the iron(III) form combines with substrate to produce a free radical intermediate by a hydrogen tunnelling process. The free radical then combines with molecular oxygen to form a peroxy radical. The iron(II) species obtained in the hydrogen abstraction step transfers an electron to the peroxy radical intermediate, along with proton transfer, to complete the catalysed reaction and regenerate the iron(III) form.

Catalytic Sites for 1lnh

Annotated By Reference To The Literature - Site 1 (Perform Site Search)
ResidueChainNumberUniProtKB NumberFunctional PartFunctionTargetDescription
AsnA713713macie:sideChainPostulated to aid catalysis via hydrogen-bonding.

Literature References

Kariapper MS
Iron extraction from soybean lipoxygenase 3 and reconstitution of catalytic activity from the apoenzyme.
Biochem Biophys Res Commun 2001 284 563-567
PubMed: 11396936
Kramer JA
Position 713 is critical for catalysis but not iron binding in soybean lipoxygenase 3.
Biochemistry 1994 33 15017-15022
PubMed: 7999759