Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary 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

Cloned(Commentary)

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

Protein Variants

EC Number Protein Variants Comment Organism
1.13.11.31 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
1.13.11.31 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]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.13.11.31 0.0213
-
linoleic acid pH 7.4, 20°C, wild-type Oryctolagus cuniculus

Organism

EC Number Organism UniProt Comment Textmining
1.13.11.31 Oryctolagus cuniculus
-
-
-

Purification (Commentary)

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

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.13.11.31 linoleic acid + O2
-
Oryctolagus cuniculus ?
-
?
1.13.11.31 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

EC Number Subunits Comment Organism
1.13.11.31 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

EC Number Synonyms Comment Organism
1.13.11.31 LOX
-
Oryctolagus cuniculus

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
1.13.11.31 47.23
-
linoleic acid pH 7.4, 20°C, wild-type Oryctolagus cuniculus