Literature summary for 1.13.11.B6 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.

Search for more literature for 1.13.11.B6

Cloned(Commentary)

Cloned (Comment)	Organism
sequence comparison and homology modelling	Pisum sativum

Protein Variants

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

KM Value [mM]

KM Value [mM]	KM Value Maximum [mM]	Substrate	Comment	Organism	Structure
0.9	-	linoleate	wild-type enzyme	Pisum sativum

Molecular Weight [Da]

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

Organism

Organism	UniProt	Comment	Textmining
Pisum sativum	-	-	-

Purification (Commentary)

Purification (Comment)	Organism
-	Pisum sativum

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
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

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

Synonyms

Synonyms	Comment	Organism
9/13-lipoxygenase	-	Pisum sativum
9/13-LOX	-	Pisum sativum

Turnover Number [1/s]

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

kcat/KM [mM/s]

kcat/KM Value [1/mMs^-1]	kcat/KM Value Maximum [1/mMs^-1]	Substrate	Comment	Organism	Structure
74	-	linoleate	wild-type enzyme	Pisum sativum

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Release 2023.1 (January 2023)