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Literature summary extracted from

  • Neau, D.B.; Gilbert, N.C.; Bartlett, S.G.; Boeglin, W.; Brash, A.R.; Newcomer, M.E.
    The 1.85 A structure of an 8R-lipoxygenase suggests a general model for lipoxygenase product specificity (2009), Biochemistry, 48, 7906-7915.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.13.11.40
-
 Plexaura homomalla

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
1.13.11.40 deletion mutant of 8R-LOX crystallized by sitting drop vapor diffusion, to 1.85 A resolution, belongs to space group P21 with four molecules in the asymmetric unit. U-shaped channel in 8R-LOX Plexaura homomalla

Protein Variants

EC Number Protein Variants Comment Organism
1.13.11.40 I433A absence of the Ile side chain destabilizes the roof of the U-shaped channel, measurable activity only in the presence of CaCl2 and the detergent emolphogen Plexaura homomalla
1.13.11.40 I433W has no measurable activity, presumably because the Trp side chain effectively blocks the arachidonic acid binding site Plexaura homomalla
1.13.11.40 L432A less than 5% of the activity of the wild-type Plexaura homomalla
1.13.11.40 L432F less than 5% of the activity of the wild-type Plexaura homomalla
1.13.11.40 L432I less than 5% of the activity of the wild-type Plexaura homomalla
1.13.11.40 L432V less than 20% of the activity of the wild-type Plexaura homomalla
1.13.11.40 additional information deletion mutant lacks one of the loops, as well as chelating amino acids from two of the three Ca2+ binding sites (the center site and that most distal from the catalytic domain). The Ca2+ site proximal to the catalytic domain, defined primarily by main chain contacts, remains intact and occupied in the mutant structure. Deletion mutant displays wild-type activity in a membrane-free assay, but Ca2+ does not promote membrane binding of the mutant and does not stimulate enzyme activity in a membrane-based assay Plexaura homomalla

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.13.11.40 0.018
-
 arachidonate mutant L432I Plexaura homomalla
1.13.11.40 0.028
-
 arachidonate mutant L432V Plexaura homomalla
1.13.11.40 0.033
-
 arachidonate mutant L432A Plexaura homomalla
1.13.11.40 0.05
-
 arachidonate wild-type Plexaura homomalla
1.13.11.40 0.135
-
 arachidonate mutant I433A Plexaura homomalla

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
1.13.11.40 Ca2+ has three Ca2+ binding sites flanked by putative membrane insertion loops in the C2-like domain Plexaura homomalla

Organism

EC Number Organism UniProt Comment Textmining
1.13.11.40 Plexaura homomalla O16025
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
1.13.11.40
-
 Plexaura homomalla

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.13.11.40 arachidonate + O2
-
 Plexaura homomalla (5Z,9E,11Z,14Z)-(8R)-8-hydroperoxyicosa-5,9,11,14-tetraenoate
-
 ?

Synonyms

EC Number Synonyms Comment Organism
1.13.11.40 8R-lipoxygenase
-
 Plexaura homomalla
1.13.11.40 8R-LOX
-
 Plexaura homomalla

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
1.13.11.40 7
-
 arachidonate mutant L432I Plexaura homomalla
1.13.11.40 12
-
 arachidonate mutant L432A Plexaura homomalla
1.13.11.40 19
-
 arachidonate mutant I433A Plexaura homomalla
1.13.11.40 42
-
 arachidonate mutant L432V Plexaura homomalla
1.13.11.40 206
-
 arachidonate wild-type Plexaura homomalla

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
1.13.11.40 7.5
-
 assay at Plexaura homomalla