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Literature summary extracted from

  • Hughes, R.K.; Lawson, D.M.; Hornostaj, A.R.; Fairhurst, S.A.; Casey, R.
    Mutagenesis and modelling of linoleate-binding to pea seed lipoxygenase (2001), Eur. J. Biochem., 268, 1030-1040.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.13.11.B6 sequence comparison and homology modelling Pisum sativum

Protein Variants

EC Number Protein Variants Comment Organism
1.13.11.B6 F580A kcat/KM for linoleate hydroperoxidation is increased by 35% Pisum sativum
1.13.11.B6 F580A possesses activity profile that is similar to wild-type Pisum sativum
1.13.11.B6 F580V possesses activity profile that is similar to wild-type Pisum sativum
1.13.11.B6 K578/T579RS possesses activity profile that is similar to wild-type Pisum sativum
1.13.11.B6 L569V kcat/KM for linoleate hydroperoxidation is reduced by 38% Pisum sativum
1.13.11.B6 T579F kcat/KM for linoleate hydroperoxidation is reduced by 89% Pisum sativum
1.13.11.B6 T579S possesses activity profile that is similar to wild-type Pisum sativum
1.13.11.B6 V570I possesses activity profile that is similar to wild-type Pisum sativum
1.13.11.B6 W523A kcat/KM for linoleate hydroperoxidation is reduced by 98% Pisum sativum

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.13.11.B6 0.9
-
linoleate wild-type enzyme Pisum sativum

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
1.13.11.B6 100000
-
x * 100000, wild-type enzyme and mutant enzymes T579F, L569V and W523A, SDS-PAGE Pisum sativum

Organism

EC Number Organism UniProt Comment Textmining
1.13.11.B6 Pisum sativum
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
1.13.11.B6
-
Pisum sativum

Source Tissue

EC Number Source Tissue Comment Organism Textmining

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.13.11.B6 linoleate + O2 identification of some of the primary determinants at the catalytic centre of pea 9/13-LOX. Validation of a model of linoleate-binding to this enzyme. Evidence is provided that the primary determinants of pocket volume and conformation are more important than substrate orientation in pea lipoxygenase catalysis. Inverse models may account for the positional specificity of only selected plant lipoxygenases Pisum sativum (10E,12Z)-9-hydroperoxy-10,12-octadecadienoate + (9Z,11E)-13-hydroperoxy-9,11-octadecadienoate ratio of (9Z,11E)-13-hydroperoxy-9,11-octadecadienoate to (10E,12Z)-9-hydroperoxy-10,12-octadecadienoate: 1.1 (wild-type enzyme), 1.6 (mutant enzyme T579S), 1.5 (mutant enzyme V570I), 1.4 (mutant enzyme T579F), 1.3 (mutant enzyme F580A), 0.9 (mutant enzyme L569V), 1.7 (mutant enzyme W523A), 1.3 (mutant enzyme F580V) ?

Subunits

EC Number Subunits Comment Organism
1.13.11.B6 ? x * 100000, wild-type enzyme and mutant enzymes T579F, L569V and W523A, SDS-PAGE Pisum sativum

Synonyms

EC Number Synonyms Comment Organism
1.13.11.B6 9/13-lipoxygenase
-
Pisum sativum
1.13.11.B6 9/13-LOX
-
Pisum sativum

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
1.13.11.B6 65
-
linoleate wild-type enzyme Pisum sativum

kcat/KM [mM/s]

EC Number kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
1.13.11.B6 74
-
linoleate wild-type enzyme Pisum sativum