PDBsum entry 1jnq

Oxidoreductase

PDB id: 1jnq

Contents

Protein chain

849 a.a. *

Ligands

EGT

Metals

FE2

Waters ×512

* Residue conservation analysis

PDB id:

1jnq

Name:

Oxidoreductase

Title:

Lipoxygenase-3 (soybean) complex with epigallocathechin (egc)

Structure:

Lipoxygenase-3. Chain: a. Synonym: l-3. Ec: 1.13.11.12

Source:

Glycine max. Soybean. Organism_taxid: 3847. Strain: provar cultivar

Resolution:

2.10Å R-factor: 0.199 R-free: 0.295

Authors:

K.Zhou,E.Skrzypczak-Jankun,J.Jankun

Key ref:

E.Skrzypczak-Jankun et al. (2003). Inhibition of lipoxygenase by (-)-epigallocatechin gallate: X-ray analysis at 2.1 A reveals degradation of EGCG and shows soybean LOX-3 complex with EGC instead. Int J Mol Med, 12, 415-420. PubMed id: 12964012

Date:

24-Jul-01 Release date: 03-Jun-03

Protein chain

P09186  (LOX3_SOYBN) -  Seed linoleate 9S-lipoxygenase-3 from Glycine max

Seq: 857 a.a.

Struc: 849 a.a.*

* PDB and UniProt seqs differ at 7 residue positions (black crosses)

Enzyme reactions

• Enzyme class: E.C.1.13.11.58 - linoleate 9S-lipoxygenase.
• Reaction: (9Z,12Z)-octadecadienoate + O2 = (9S)-hydroperoxy-(10E,12Z)- octadecadienoate
• Cofactor: Fe cation

Molecule diagrams generated from .mol files obtained from the KEGG ftp site

Key reference

Int J Mol Med 12:415-420 (2003)

PubMed id: 12964012

Inhibition of lipoxygenase by (-)-epigallocatechin gallate: X-ray analysis at 2.1 A reveals degradation of EGCG and shows soybean LOX-3 complex with EGC instead.

E.Skrzypczak-Jankun, K.Zhou, J.Jankun.

ABSTRACT

Lipoxygenases (LOXs) are non-heme iron containing enzymes ubiquitous in nature and participating in the metabolism of the polyunsaturated fatty acids (PUFA). They are capable of combining their dioxygenase activity with its co-oxidative activity manifesting itself in biotransformation reactions catalyzed by LOXs for other than PUFA small molecules. LOXs involvement in inflammatory diseases and cancer have been well documented. Catechins are the natural flavonoids of known inhibitory activity toward dioxygenases with a potential to be utilized in disease prevention and treatment. This work presents results obtained from an X-ray analysis of (-)-epigallocatechin gallate (EGCG) interacting with soybean lipoxygenase-3. The 3D structure of the resulting complex reveals the inhibitor depicting (-)-epigallo-catechin that lacks galloyl moiety. The A-ring is near the iron co-factor, attached by the hydrogen bond to the C-terminus of the enzyme, and the B-ring hydroxyl groups participate in the hydrogen bonds and the van der Waals interactions formed by the surrounding amino acids and water molecules.