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Literature summary for 1.13.11.40 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
Search for more literature for 1.13.11.40

Cloned(Commentary)

Cloned (Comment) Organism
-
 Plexaura homomalla

Crystallization (Commentary)

Crystallization (Comment) Organism
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

Protein Variants Comment Organism
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
I433W has no measurable activity, presumably because the Trp side chain effectively blocks the arachidonic acid binding site Plexaura homomalla
L432A less than 5% of the activity of the wild-type Plexaura homomalla
L432F less than 5% of the activity of the wild-type Plexaura homomalla
L432I less than 5% of the activity of the wild-type Plexaura homomalla
L432V less than 20% of the activity of the wild-type Plexaura homomalla
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]

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

Metals/Ions

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

Organism

Organism UniProt Comment Textmining
Plexaura homomalla O16025
-
-

Purification (Commentary)

Purification (Comment) Organism
-
 Plexaura homomalla

Substrates and Products (Substrate)

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

Synonyms

Synonyms Comment Organism
8R-lipoxygenase
-
 Plexaura homomalla
8R-LOX
-
 Plexaura homomalla

Turnover Number [1/s]

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

pH Optimum

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