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Literature summary for 1.3.1.42 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
Search for more literature for 1.3.1.42

Crystallization (Commentary)

Crystallization (Comment) Organism
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

Protein Variants Comment Organism
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
Y364F crystallization as a monomer with none of the dimer interactions retained Solanum lycopersicum

Organism

Organism UniProt Comment Textmining
Solanum lycopersicum Q9FEW9 isoform OPR3
-

Substrates and Products (Substrate)

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

Subunits

Subunits Comment Organism
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
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
More rapid monomer-dimer equilibrium with a high dissociation constant in vitro Solanum lycopersicum

Turnover Number [1/s]

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

Cofactor

Cofactor Comment Organism Structure
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