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Literature summary for 1.13.11.33 extracted from

  • Suardiaz, R.; Masgrau, L.; Lluch, J.M.; Gonzalez-Lafont, A.
    Regio- and stereospecificity in the oxygenation of arachidonic acid catalyzed by Leu597 mutants of rabbit 15-lipoxygenase a QM/MM study (2014), Chemphyschem, 15, 2303-2310 .
    View publication on PubMed
Search for more literature for 1.13.11.33

Protein Variants

Protein Variants Comment Organism
L597A site-directed mutagenesis, regiospecificity favoring addition to C15 is sharper than that in the wild-type, but the stereochemistry is R. This is because the extra space created by the mutation to Ala is big enough for arachidonate to move so that it can adopt an alternative binding mode. The L597A mutant of 15r-LO works as an aspirin-acetylated cyclooxygenase-2, which synthesizes 15-(R)-hydroperoxyeicosatetraenoic acid Oryctolagus cuniculus
L597V site-directed mutagenesis, the addition of O2 to C15 of arachidonate is the predominant path, although it reduces the C15/C11 product ratio by almost ten times with respect to the wild-type enzyme. The S stereochemistry is kept Oryctolagus cuniculus

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
arachidonate + O2 Oryctolagus cuniculus best substrate (5Z,8Z,11Z,13E)-(15S)-15-hydroperoxyicosa-5,8,11,13-tetraenoate
-
 ?

Organism

Organism UniProt Comment Textmining
Oryctolagus cuniculus P12530
-
-

Reaction

Reaction Comment Organism Reaction ID
arachidonate + O2 = (5Z,8Z,11Z,13E)-(15S)-15-hydroperoxyicosa-5,8,11,13-tetraenoate important role of Leu597 in the mechanism of lipoxygenases Oryctolagus cuniculus
a

Source Tissue

Source Tissue Comment Organism Textmining
reticulocyte
-
 Oryctolagus cuniculus
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
arachidonate + O2 best substrate Oryctolagus cuniculus (5Z,8Z,11Z,13E)-(15S)-15-hydroperoxyicosa-5,8,11,13-tetraenoate
-
 ?

Synonyms

Synonyms Comment Organism
15-lipoxygenase
-
 Oryctolagus cuniculus
15-rLO
-
 Oryctolagus cuniculus
reticulocyte-type 15-LO-1
-
 Oryctolagus cuniculus

General Information

General Information Comment Organism
additional information quantum mechanics/molecular mechanics calculations with molecular dynamics simulations to study the addition of O2 to the pentadienyl radical of arachidonic acid catalyzed by the Leu597Val and Leu597Ala mutants of rabbit 15-lipoxygenase, detailed overview Oryctolagus cuniculus