Any feedback?
Please rate this page
(enzyme.php)
(0/150)

BRENDA support

BRENDA Home
show all | hide all No of entries

Information on EC 1.13.11.B6 - linoleate 9/13-lipoxygenase and Organism(s) Glycine max and UniProt Accession P09186

for references in articles please use BRENDA:EC1.13.11.B6
preliminary BRENDA-supplied EC number
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
Specify your search results
Select one or more organisms in this record: ?
This record set is specific for:
Glycine max
UNIPROT: P09186 not found.
Show additional data
Do not include text mining results
Include (text mining) results
Include results (AMENDA + additional results, but less precise)
Word Map
hide
The taxonomic range for the selected organisms is: Glycine max
The enzyme appears in selected viruses and cellular organisms
Synonyms
oslox1, pnlox1, lox1:md:1a, 9/13-lipoxygenase, lox2:md:2a, 13/9-lox, linoleate 9 s-lipoxygenase, more
SYSTEMATIC NAME
IUBMB Comments
lineate:oxygen 9/13-oxidoreductase
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
linoleate + O2
(9R,10E,12Z)-9-hydroperoxy-10,12-octadecadienoate + (9Z,11E,13R)-13-hydroperoxy-9,11-octadecadienoate
show the reaction diagram
-
the enzyme delivers a 50:50 mixture of (9R,10E,12Z)-9-hydroperoxy-10,12-octadecadienoate + (9Z,11E,13R)-13-hydroperoxy-9,11-octadecadienoate, with higher turn out of R stereoisomers over S isomers (60:40)
-
?
linoleate + O2
(9S,10E,12Z)-9-hydroperoxy-10,12-octadecadienoate + (9Z,11E,13S)-13-hydroperoxy-9,11-octadecadienoate
show the reaction diagram
-
soybean lipoxygenase-1 produces a preponderance of two chiral products from linoleic acid, (9Z,11E,13S)-13-hydroperoxy-9,11-octadecadienoate and (9S,10E,12Z)-9-hydroperoxy-10,12-octadecadienoate. (9Z,11E,13S)-13-hydroperoxy-9,11-octadecadienoate is generated at all pH values, but in the presence of Tween 20, (9S,10E,12Z)-9-hydroperoxy-10,12-octadecadienoate does not form at pH values above 8.5. As the pH decreases below 8.5, the proportion of (9S,10E,12Z)-9-hydroperoxy-10,12-octadecadienoate increases linearly until at pH 6 it constitutes about 25% of the chiral products attributed to enzymic action. Below pH 6, lipoxygenase activity is barely measurable, and the hydroperoxide product arises mainly from autoxidation and possibly non-enzymic oxygenation of the pentadienyl radical formed by the enzyme. The change in percent enzymically formed 9-hydroperoxide between pH 6.0 and 8.5 parallels the pH plot of a sodium linoleate/linoleic acid titration. It is concluded that the (9S)-hydroperoxide is formed only from the nonionized carboxylic acid form of linoleic acid. Methyl esterification of linoleic acid blocks the formation of the (9S,10E,12Z)-9-hydroperoxy-10,12-octadecadienoate by lipoxygenase-1, but not the (13S)-hydroperoxide. Since the hydroperoxydiene moieties of the (9S)- and (13S)-hydroperoxides are spatially identical when the molecules are arranged head to tail in opposite orientations, it is suggested that the carboxylic acid form of the substrate can arrange itself at the active site in either orientation, but the carboxylate anion can be positioned only in one orientation. Active-site model for soybean lipoxygenase-1
-
-
?
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
cv. Provar
UniProt
Manually annotated by BRENDA team
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
LOX3_SOYBN
857
0
96758
Swiss-Prot
-
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
comparison of the structure of lipoxygenase L3 with its L1 isoenzyme
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Gardner, H.W.
Soybean lipoxygenase-1 enzymically forms both (9S)- and (13S)-hydroperoxides from linoleic acid by a pH-dependent mechanism
Biochim. Biophys. Acta
1001
274-281
1989
Glycine max
Manually annotated by BRENDA team
Skrzypczak-Jankun, E.; Amzel, L.M.; Kroa, B.A.; Funk, M.O. Jr.
Structure of soybean lipoxygenase L3 and a comparison with its L1 isoenzyme
Proteins
29
15-31
1997
Glycine max (P09186)
Manually annotated by BRENDA team