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Literature summary for 1.13.11.33 extracted from

  • Walther, M.; Roffeis, J.; Jansen, C.; Anton, M.; Ivanov, I.; Kuhn, H.
    Structural basis for pH-dependent alterations of reaction specificity of vertebrate lipoxygenase isoforms (2009), Biochim. Biophys. Acta, 1791, 827-835.
    View publication on PubMed
Search for more literature for 1.13.11.33

Activating Compound

Activating Compound Comment Organism Structure
additional information positional specificity of wild-type 15-LOX-2 does hardly depend on the pH of the reaction buffer. The pH sensitivity can be induced by introduction of a His at the active site Homo sapiens

Cloned(Commentary)

Cloned (Comment) Organism
ligated into the pQE-9 plasmid and expressed as N-terminal His-tag fusion protein in Escherichia coli (XL-1 Blue) Mus musculus
ligated into the pQE-9 plasmid and expressed as N-terminal His-tag fusion protein in Escherichia coli (XL-1 Blue) Oryctolagus cuniculus
LOX isoforms ligated into the pQE-9 plasmid and expressed as N-terminal His-tag fusion protein in Escherichia coli (XL-1 Blue) Homo sapiens

Protein Variants

Protein Variants Comment Organism
D602Y 15-LOX-2 mutant shows a similar pH-profile as the wild-type enzyme Homo sapiens
D602Y/V603H a strong shift of the pH profile of 15-LOX-2 mutant towards more acidic values Homo sapiens
V603H a strong shift of the pH profile of 15-LOX-2 mutant towards more acidic values. 15-H(p)ETE is the major oxygenation product at pH 8 Homo sapiens

Inhibitors

Inhibitors Comment Organism Structure
additional information physico-chemical state of the substrate and the complex equilibrium between fatty acid monomers, acid soaps and micelles may impact the reaction specificity of LOX-isoforms Homo sapiens
additional information physico-chemical state of the substrate and the complex equilibrium between fatty acid monomers, acid soaps and micelles may impact the reaction specificity of LOX-isoforms Mus musculus
additional information pH alterations in the near physiological range impact the iron content of LOX and thus the catalytic activity Oryctolagus cuniculus

Metals/Ions

Metals/Ions Comment Organism Structure
Fe
-
 Oryctolagus cuniculus

Organism

Organism UniProt Comment Textmining
Homo sapiens
-
-
-
Mus musculus
-
-
-
Oryctolagus cuniculus
-
-
-

Purification (Commentary)

Purification (Comment) Organism
on Ni column Homo sapiens
on Ni column Mus musculus
on Ni column Oryctolagus cuniculus

Source Tissue

Source Tissue Comment Organism Textmining
skin
-
 Mus musculus
-

Storage Stability

Storage Stability Organism
-80°C, 10% glycerol Homo sapiens
-80°C, 10% glycerol Mus musculus
-80°C, 10% glycerol Oryctolagus cuniculus

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
arachidonate + O2
-
 Homo sapiens (5Z,8Z,11Z,13E)-(15S)-15-hydroperoxyicosa-5,8,11,13-tetraenoate 15-H(p)ETE is the major reaction product of 15-LOX-2 and 12/15-LOX independent of the pH ?
arachidonate + O2
-
 Mus musculus (5Z,8Z,11Z,13E)-(15S)-15-hydroperoxyicosa-5,8,11,13-tetraenoate
-
 ?
arachidonate + O2
-
 Oryctolagus cuniculus (5Z,8Z,11Z,13E)-(15S)-15-hydroperoxyicosa-5,8,11,13-tetraenoate 15-H(p)ETE is the major reaction product independent of the pH ?
additional information 15-LOX-2 does not oxygenate (5Z,8Z,11Z,14Z)-nonadeca-5,8,11,14-tetraene-1,19-dioic acid at various pH Homo sapiens ?
-
 ?

Synonyms

Synonyms Comment Organism
12/15-LOX
-
 Homo sapiens
12/15-LOX
-
 Mus musculus
12/15-LOX
-
 Oryctolagus cuniculus
15-lipoxygenase
-
 Mus musculus
15-lipoxygenase-2
-
 Homo sapiens
15-LOX-1
-
 Homo sapiens
15-LOX-2
-
 Homo sapiens

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
8 9 pH-optimum of 15-LOX-2 for arachidonic acid oxygenation Homo sapiens

pH Range

pH Minimum pH Maximum Comment Organism
6 9.5 pH 6 about 50% of maximal activity, pH 9.5 about 60% of maximal activity Homo sapiens