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Literature summary extracted from

  • Walther, M.; Wiesner, R.; Kuhn, H.
    Investigations into calcium-dependent membrane association of 15-lipoxygenase-1. Mechanistic roles of surface-exposed hydrophobic amino acids and calcium (2004), J. Biol. Chem., 279, 3717-3725.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.13.11.33 expression in Escherichia coli Oryctolagus cuniculus

Protein Variants

EC Number Protein Variants Comment Organism
1.13.11.33 F412E mutation slightly impairs membrane binding, mutant enzyme shows 29% of the arachidonic acid oxygenase activity of the wild-type enzyme Oryctolagus cuniculus
1.13.11.33 F70H mutation impairs membrane binding, mutant enzyme shows 53% of the arachidonic acid oxygenase activity of the wild-type enzyme Oryctolagus cuniculus
1.13.11.33 L195E mutation impairs membrane binding, mutant enzyme shows 42% of the arachidonic acid oxygenase activity of the wild-type enzyme Oryctolagus cuniculus
1.13.11.33 L71K mutation impairs membrane binding, mutant enzyme shows 50% of the arachidonic acid oxygenase activity of the wild-type enzyme Oryctolagus cuniculus
1.13.11.33 W181E mutation strongly impairs membrane binding, mutant enzyme shows 34% of the arachidonic acid oxygenase activity of the wild-type enzyme Oryctolagus cuniculus
1.13.11.33 Y15E mutation impairs membrane binding, mutant enzyme shows 61% of the arachidonic acid oxygenase activity of the wild-type enzyme Oryctolagus cuniculus
1.13.11.33 Y292E mutation slightly impairs membrane binding, mutant enzyme shows 112% of the arachidonic acid oxygenase activity of the wild-type enzyme Oryctolagus cuniculus

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
1.13.11.33 membrane the enzyme associates to biomembranes primarily via hydrophobic interactions between surface-exposed apolar amino acid side chains and membrane lipids. Calcium supports membrane binding probably by forming salt bridges between the negatively charged head groups of membrane phospholipids and acidic surface amino acids of the membrane Oryctolagus cuniculus 16020
-

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
1.13.11.33 Ca2+ at 0.005-0.05 mM is required for efficient membrane binding Oryctolagus cuniculus

Organism

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

Purification (Commentary)

EC Number Purification (Comment) Organism
1.13.11.33
-
 Oryctolagus cuniculus

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.13.11.33 arachidonic acid + O2
-
 Oryctolagus cuniculus (15S)-hydroperoxy-(5Z,8Z,11Z,13E)-eicosatetraenoic acid + (12S,5Z,8Z,10E,14Z)-12-hydroperoxyeicosa-5,8,10,14-tetraenoic acid the ratio of (15S)-hydroperoxy-(5Z,8Z,11Z,13E)-eicosatetraenoic acid to (12S)-hydroperoxy-(5Z,8Z,11Z,13E)-eicosatetraenoic acid is 20 for the wild-type enzyme ?

Synonyms

EC Number Synonyms Comment Organism
1.13.11.33 15-LOX
-
 Oryctolagus cuniculus