1.13.11.45: linoleate 11-lipoxygenase
This is an abbreviated version!
For detailed information about linoleate 11-lipoxygenase, go to the full flat file.
Word Map on EC 1.13.11.45
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1.13.11.45
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oxylipins
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graminis
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bis-allylic
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gaeumannomyces
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suprafacial
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take-all
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antarafacial
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atlox2
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lipoxygenation
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hydroperoxy
- 1.13.11.45
- oxylipins
- graminis
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bis-allylic
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gaeumannomyces
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suprafacial
-
take-all
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antarafacial
-
atlox2
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lipoxygenation
-
hydroperoxy
Reaction
Synonyms
13 R -MnLOX, 13R-MnLOX, Cg-MnLOX, CspLOX2, Fo-MnLOX, linoleate dioxygenase, lipoxygenase 2, LOX-1, manganese lipoxygenase, manganese LOX, MGG_08499, Mn-LO, Mn-LOX, MnLOX, Mo-MnLOX
ECTree
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Metals Ions
Metals Ions on EC 1.13.11.45 - linoleate 11-lipoxygenase
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Ca2+
Cu2+
enzyme-bound, is eliminated by denaturation of the enzyme protein
Fe2+
Fe3+
non-heme iron, required. The catalytic non-heme iron, deeply buried in the CspLOX2 active site, is coordinated by three invariant histidines (His257, His262, His449), Asn453 and the carboxy group of the C-terminal Ile569. The sixth ligand of the octahedrally coordinated iron, which is positioned towards the putative substrate binding channel, is a water (Fe2+-H2O) or hydroxide molecule (Fe3+-OH) acting as a catalytic base for hydrogen abstraction during catalysis, coordination of the iron cofactor, overview
Mn2+
additional information
Mn2+
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enzyme-bound, has catalytic function, but does not activate the enzyme exogenously
Mn2+
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manganese 13R-lipoxygenase contains catalytic manganese, the catalytic domain of 13R-MnLOX contains a pentamer motif flanked by two His metal ligands, His-Val-Leu-Phe-His, in the presumed manganese binding region
Mn2+
required, high amount bound to the enzyme, exogenous Mn2+ does not enhance the enzyme activity
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determination of metal contents by EPR analysis