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Literature summary for 1.13.11.31 extracted from

  • Ivanov, I.; Shang, W.; Toledo, L.; Masgrau, L.; Svergun, D.; Stehling, S.; Gómez, H.; Di Venere, A.; Mei, G.; Lluch, J.; Skrzypczak-Jankun, E.; González-Lafont, A.; Kühn, H.
    Ligand-induced formation of transient dimers of mammalian 12/15-lipoxygenase: A key to allosteric behavior of this class of enzymes? (2012), Proteins, 80, 703-712.
    View publication on PubMed
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Cloned(Commentary)

Cloned (Comment) Organism
expressed in Escherichia coli as a His-tagged fusion protein Oryctolagus cuniculus

Protein Variants

Protein Variants Comment Organism
L183E/L192E introduction of negatively charged residues at the intermonomer interface disturbs the hydrophobic dimer interaction of the wild-type LOX. Double mutant does not follow Michaelis-Menten kinetics. Double mutant are gradually inactivated at increasing substrate concentration Oryctolagus cuniculus
W181E/H585E introduction of negatively charged residues at the intermonomer interface disturbs the hydrophobic dimer interaction of the wild-type LOX. Double mutant does not follow Michaelis-Menten kinetics. Double mutant are gradually inactivated at increasing substrate concentration Oryctolagus cuniculus

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.0213
-
 linoleic acid pH 7.4, 20°C, wild-type Oryctolagus cuniculus

Organism

Organism UniProt Comment Textmining
Oryctolagus cuniculus
-
-
-

Purification (Commentary)

Purification (Comment) Organism
using Ni-NTA chromatography Oryctolagus cuniculus

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
linoleic acid + O2
-
 Oryctolagus cuniculus ?
-
 ?
additional information binding of allosteric effector [13(S)-hydroxyoctadeca-9(Z),11(E)-dienoic acid] shifts the monomer-dimer equilibrium toward dimer formation Oryctolagus cuniculus ?
-
 ?

Subunits

Subunits Comment Organism
dimer binding of allosteric effector [13(S)-hydroxyoctadeca-9(Z),11(E)-dienoic acid] shifts the monomer-dimer equilibrium toward dimer formation. Enzyme dimerization may protect the enzyme from kinetic substrate inhibition by shielding the hydrophobic alpha2 helixes Oryctolagus cuniculus

Synonyms

Synonyms Comment Organism
LOX
-
 Oryctolagus cuniculus

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
47.23
-
 linoleic acid pH 7.4, 20°C, wild-type Oryctolagus cuniculus