BRENDA - Enzyme Database
show all sequences of 1.13.11.40

Understanding the molecular mechanism of the Ala-versus-Gly concept controlling the product specificity in reactions catalyzed by lipoxygenases a combined molecular dynamics and QM/MM study of coral 8R-lipoxygenase

Saura, P.; Suardiaz, R.; Masgrau, L.; Gonzalez-Lafont, A.; Rosta, E.; Lluch, J.; ACS Catal. 7, 4854-4866 (2017)
No PubMed abstract available

Data extracted from this reference:

Crystallization (Commentary)
Crystallization (Commentary)
Organism
purified enzyme 8R-LOX containing the arachidonate substrate in subunit C
Plexaura homomalla
Engineering
Protein Variants
Commentary
Organism
G427A
site-directed mutagenesis. In wild-type, molecular oxygen adds to C8 of arachidonic acid with an R stereochemistry. In the mutant, Ala427 pushes Leu385, blocks the region over C8, and opens an oxygen access channel now directed to C12, where molecular oxygen is added with an S stereochemistry. Thus, the specificity turns out to be dramatically inverted
Plexaura homomalla
Organism
Organism
UniProt
Commentary
Textmining
Plexaura homomalla
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Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
Substrate Product ID
additional information
usage of a combination of molecular dynamics simulations with quantum mechanics/molecular mechanics calculations to study the hydrogen abstraction step and the molecular oxygen addition step of the hydroperoxidation reaction of arachidonic acid catalyzed by both wild-type Coral 8R-LOX and its Gly427Ala mutant
741487
Plexaura homomalla
?
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?
Synonyms
Synonyms
Commentary
Organism
8R-lipoxygenase
-
Plexaura homomalla
Crystallization (Commentary) (protein specific)
Crystallization
Organism
purified enzyme 8R-LOX containing the arachidonate substrate in subunit C
Plexaura homomalla
Engineering (protein specific)
Protein Variants
Commentary
Organism
G427A
site-directed mutagenesis. In wild-type, molecular oxygen adds to C8 of arachidonic acid with an R stereochemistry. In the mutant, Ala427 pushes Leu385, blocks the region over C8, and opens an oxygen access channel now directed to C12, where molecular oxygen is added with an S stereochemistry. Thus, the specificity turns out to be dramatically inverted
Plexaura homomalla
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
ID
additional information
usage of a combination of molecular dynamics simulations with quantum mechanics/molecular mechanics calculations to study the hydrogen abstraction step and the molecular oxygen addition step of the hydroperoxidation reaction of arachidonic acid catalyzed by both wild-type Coral 8R-LOX and its Gly427Ala mutant
741487
Plexaura homomalla
?
-
-
-
?
General Information
General Information
Commentary
Organism
additional information
molecular dynamics simulations, quantum mechanics/molecular mechanics calculations, overview. In wild-type, molecular oxygen adds to C8 of arachidonic acid with an R stereochemistry. In the mutant, Ala427 pushes Leu385, blocks the region over C8, and opens an oxygen access channel now directed to C12, where molecular oxygen is added with an S stereochemistry. Thus, the specificity turns out to be dramatically inverted
Plexaura homomalla
physiological function
lipoxygenases (LOXs) are a family of enzymes that catalyze the highly specific hydroperoxidation of polyunsaturated fatty acids, such as arachidonic acid. Different stereo- or/and regioisomer hydroperoxidation products lead later to different metabolites that exert opposite physiological effects in the animal body and play a central role in inflammatory processes. The Gly-Ala switch of a single residue is crucial for the stereo- and regiocontrol in many lipoxygenases
Plexaura homomalla
General Information (protein specific)
General Information
Commentary
Organism
additional information
molecular dynamics simulations, quantum mechanics/molecular mechanics calculations, overview. In wild-type, molecular oxygen adds to C8 of arachidonic acid with an R stereochemistry. In the mutant, Ala427 pushes Leu385, blocks the region over C8, and opens an oxygen access channel now directed to C12, where molecular oxygen is added with an S stereochemistry. Thus, the specificity turns out to be dramatically inverted
Plexaura homomalla
physiological function
lipoxygenases (LOXs) are a family of enzymes that catalyze the highly specific hydroperoxidation of polyunsaturated fatty acids, such as arachidonic acid. Different stereo- or/and regioisomer hydroperoxidation products lead later to different metabolites that exert opposite physiological effects in the animal body and play a central role in inflammatory processes. The Gly-Ala switch of a single residue is crucial for the stereo- and regiocontrol in many lipoxygenases
Plexaura homomalla
Other publictions for EC 1.13.11.40
No.
1st author
Pub Med
title
organims
journal
volume
pages
year
Activating Compound
Application
Cloned(Commentary)
Crystallization (Commentary)
Engineering
General Stability
Inhibitors
KM Value [mM]
Localization
Metals/Ions
Molecular Weight [Da]
Natural Substrates/ Products (Substrates)
Organic Solvent Stability
Organism
Oxidation Stability
Posttranslational Modification
Purification (Commentary)
Reaction
Renatured (Commentary)
Source Tissue
Specific Activity [micromol/min/mg]
Storage Stability
Substrates and Products (Substrate)
Subunits
Synonyms
Temperature Optimum [C]
Temperature Range [C]
Temperature Stability [C]
Turnover Number [1/s]
pH Optimum
pH Range
pH Stability
Cofactor
Ki Value [mM]
pI Value
IC50 Value
Activating Compound (protein specific)
Application (protein specific)
Cloned(Commentary) (protein specific)
Cofactor (protein specific)
Crystallization (Commentary) (protein specific)
Engineering (protein specific)
General Stability (protein specific)
IC50 Value (protein specific)
Inhibitors (protein specific)
Ki Value [mM] (protein specific)
KM Value [mM] (protein specific)
Localization (protein specific)
Metals/Ions (protein specific)
Molecular Weight [Da] (protein specific)
Natural Substrates/ Products (Substrates) (protein specific)
Organic Solvent Stability (protein specific)
Oxidation Stability (protein specific)
Posttranslational Modification (protein specific)
Purification (Commentary) (protein specific)
Renatured (Commentary) (protein specific)
Source Tissue (protein specific)
Specific Activity [micromol/min/mg] (protein specific)
Storage Stability (protein specific)
Substrates and Products (Substrate) (protein specific)
Subunits (protein specific)
Temperature Optimum [C] (protein specific)
Temperature Range [C] (protein specific)
Temperature Stability [C] (protein specific)
Turnover Number [1/s] (protein specific)
pH Optimum (protein specific)
pH Range (protein specific)
pH Stability (protein specific)
pI Value (protein specific)
Expression
General Information
General Information (protein specific)
Expression (protein specific)
KCat/KM [mM/s]
KCat/KM [mM/s] (protein specific)
741487
Saura
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Understanding the molecular m ...
Plexaura homomalla
ACS Catal.
7
4854-4866
2017
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Neau
Crystal structure of a lipoxy ...
Plexaura homomalla
J. Biol. Chem.
289
31905-31913
2014
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702338
Neau
The 1.85 A structure of an 8R- ...
Plexaura homomalla
Biochemistry
48
7906-7915
2009
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702435
Walther
Structural basis for pH-depend ...
Mus musculus
Biochim. Biophys. Acta
1791
827-835
2009
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688221
Schweiger
Inducible expression of 15-lip ...
Mus musculus
J. Lipid Res.
48
553-564
2007
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671715
Jisaka
Double dioxygenation by mouse ...
Mus musculus
Biochem. Biophys. Res. Commun.
338
136-143
2005
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674505
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Insights from the X-ray crysta ...
Plexaura homomalla
J. Biol. Chem.
280
39545-39552
2005
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659650
Schneider
Upregulation of 8-lipoxygenase ...
Mus musculus
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122
691-698
2004
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660365
Coffa
A single active site residue d ...
Plexaura homomalla
Proc. Natl. Acad. Sci. USA
101
15579-15584
2004
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439401
Qiao
Leukotriene A synthase activit ...
Mus musculus
Biochim. Biophys. Acta
1438
131-139
1999
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439400
Steel
Identification of an 8-lipoxyg ...
Aplysia californica
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272
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439399
Brash
Purification and molecular clo ...
Asteroidea, Callista chione, Plexaura homomalla, Strongylocentrotus purpuratus
J. Biol. Chem.
271
20949-20957
1996
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439398
Fuerstenberger
Characterization of an 8-lipox ...
Mus musculus
J. Biol. Chem.
266
15738-15745
1991
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439397
Brash
On non-cyclooxygenase prostagl ...
Plexaura homomalla
J. Biol. Chem.
262
15829-15839
1987
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439396
Bundy
Discovery of an arachidonic ac ...
Pseudoplexaura porosa
J. Biol. Chem.
261
747-751
1986
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