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Literature summary extracted from

  • Breithaupt, C.; Kurzbauer, R.; Lilie, H.; Schaller, A.; Strassner, J.; Huber, R.; Macheroux, P.; Clausen, T.
    Crystal structure of 12-oxophytodienoate reductase 3 from tomato: self-inhibition by dimerization (2006), Proc. Natl. Acad. Sci. USA, 103, 14337-14342.
    View publication on PubMedView publication on EuropePMC

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
1.3.1.42 native enzyme and mutants E291L and Y364F. Wild-type enzyme crystallizes as an extraordinary self-inhibiting dimer, dimerization is actively driven by the mutual binding of the two L6 loops into the two active sites Solanum lycopersicum

Protein Variants

EC Number Protein Variants Comment Organism
1.3.1.42 E291L sixfold faster turnover than wild-type. Crystallization in same space group as wild-type, but with strikingly different cell constants. Appears as monomer in the crystal Solanum lycopersicum
1.3.1.42 Y364F crystallization as a monomer with none of the dimer interactions retained Solanum lycopersicum

Organism

EC Number Organism UniProt Comment Textmining
1.3.1.42 Solanum lycopersicum Q9FEW9 isoform OPR3
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.3.1.42 (9S,13S)-12-oxo-phytodienoic acid + NADPH
-
 Solanum lycopersicum 3-oxo-2((2Z)-pentenyl)-cyclopentane-1-octanoic acid + NADP+
-
 ?
1.3.1.42 trans-hex-2-enal + NADPH
-
 Solanum lycopersicum hexanal + NADP+
-
 ?

Subunits

EC Number Subunits Comment Organism
1.3.1.42 dimer concentration-dependent shift from monomer with 40000 Da at 0.022 mM to dimer with 80000 Da at 0.358 mM, dynamic light scattering Solanum lycopersicum
1.3.1.42 monomer concentration-dependent shift from monomer with 40000 Da at 0.022 mM to dimer with 80000 Da at 0.358 mM, dynamic light scattering Solanum lycopersicum
1.3.1.42 More rapid monomer-dimer equilibrium with a high dissociation constant in vitro Solanum lycopersicum

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
1.3.1.42 additional information
-
 additional information for oxidative half-reaction, kox of trans-hex-2-2enal is 0.3 per sec Solanum lycopersicum
1.3.1.42 14
-
 trans-hex-2-enal
-
 Solanum lycopersicum

Cofactor

EC Number Cofactor Comment Organism Structure
1.3.1.42 additional information in the dimer interface of enzyme, a sulfate ion is bound which forms hydrogen bonds with two arginines of protomer A and one arginine of loop L6 of the partner protomer B. Sulfate ion may mimic the phosphate group of phosphorylated T364 Solanum lycopersicum